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Lysine bioavailability among 2 lipid-coated lysine products after exposure to silage

Lysine bioavailability among 2 lipid-coated lysine products after exposure to silage J. N. Reiners,* J. E. Held,* C. L. Wright,* Q. Qiao,† G. D. Djira,‡ B. R. Brunsvig,* K. M. Reza,† and D. W. Brake* *Department of Animal Science, South Dakota State University, Brookings 57007; and †Department of Electrical Engineering and Computer Science, South Dakota State University, Brookings 57007 and ‡Department of Mathematics and Statistics, South Dakota State University, Brookings 57007 ABSTRACT: We conducted 2 experiments to deter- dietary lysine-HCl were calculated to be 23, 15, and mine lysine bioavailability from 2 lipid-coated lysine 18%, respectively. Even though each dietary source products. In an in vitro experiment we mixed each of lysine increased plasma lysine, rates of increases in lipid-coated lysine product with either alfalfa- or plasma lysine from one lipid-coated lysine source (lin- corn-silage at different amounts of acidity. Scanning ear; P = 0.20) and lysine-HCl (linear; P = 0.11) were electron micrographs indicated that surface struc- not different from plasma lysine levels supported by ture of each lipid-coated lysine particle was eroded diet alone. However, the rate of plasma lysine increase after mixing with silage. Additionally, visual evalua- in response to lysine from the other lipid-coated lysine tion of scanning electron micrographs suggested that source was greater (P = 0.04) than plasma lysine from peripheral surface abrasion of lipid-coated lysine may feed alone. Nonetheless, the rate of plasma lysine be greater when lipid-coated lysine was mixed with increase in response to lipid-coated lysine did not dif- alfalfa silage in comparison to corn silage. In a cor- fer (P ≥ 0.70) from the rate of plasma lysine increase responding experiment, in vivo measures of lysine from lysine-HCl. Clearly, methods of manufacture, bioavailability to sheep from 2 lipid-coated lysine together with physical and chemical characteristics products and lysine-HCl were determined after mix- of diet, can impact amounts of metabolizable lysine ing in corn silage. Plasma lysine concentrations provided from lipid-coated lysine products. Direct increased linearly (P < 0.01) in response to aboma- measures of lysine bioavailability from lipid-coated sal lysine infusion indicating that our model was lysine products after mixing with diets should be sensitive to increases in metabolizable lysine flow. based on measurements with the products treated sim- Bioavailability of each lipid-coated lysine source and ilarly to the method of feeding. Key words: amino acid, bioavailability, cattle, lysine, silage © 2017 American Society of Animal Science. This is an open access article distributed under the CC BY-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/4.0/) Transl. Anim. Sci. 2017.1:311–319 doi:10.2527/tas2017.0037 INTRODUCTION cows are fed diets with greater amounts of metaboliz- able lysine. Specifically, greater metabolizable lysine Protein synthesis and milk protein production can increase milk protein content and yield (Clark, among lactating cows fed corn-based diets is often 1975; NRC, 2001; Paz and Kononoff, 2014) and milk first-limited by metabolizable lysine (NRC, 2001). protein secretions. Several authors have also reported Therefore, efficiency of N used for productive purposes that greater amounts of metabolizable lysine can also (i.e., milk N and N retained) is increased when lactating improve milk fat content and secretions (Bremmer et al., 1997; Xu et al., 1998). Most feeds commonly used to increase flow of metabolizable protein to cows do not This project was supported by the USDA National Institute perfectly complement metabolizable proteins from corn. of Food and Agriculture (Washington, DC). This project is a con- Thus, supplementation of complex proteins to improve tribution from the South Dakota Agricultural Experiment Station, Brookings, SD 57007. efficiency of N use in cows is limited in comparison Corresponding author: derek.brake@sdstate.edu to supplementation of individual amino acids to meet Received May 10, 2017. limits in metabolizable amino acids. Unfortunately, Accepted July 15, 2017. Downloaded from https://academic.oup.com/tas/article-abstract/1/3/311/4636631 by Ed 'DeepDyve' Gillespie user on 10 April 2018 312 Reiners et al. most free amino acids are rapidly degraded by ruminal for 169 and 154 d, respectively. Alfalfa (pH = 4.4 ± 0.1) microbiota (Lewis and Emery, 1962; Chalupa, 1975) and corn silage (pH = 3.7 ± 0.1) from each miniature silo and supplementation of crystalline amino acids provides were composited by silage type after ensiling. only small increases in metabolizable amino acid supply Acidity of silage was modified prior to incubation of (Mangan, 1972). Many technologies have been devel- lipid-coated lysine to evaluate effects of acidity and si - oped to increase metabolizable amino acid flows from lage type on surface structure of lipid-coated lysine. The crystalline amino acids to ruminants (Wu and Papas, pH in an aliquot (9.5 kg DM) of alfalfa silage was in- 1997). Hydroxymethyl analogs (Elwakeel et al., 2012), creased to 6.8 after initial measures of acidity by mixing acid degradable polymeric coatings (Titgemeyer et al., (model 2030, Marion Mixer) with 2.8 kg of 10% (wt/wt) 1988; Klemesrud et al., 2000) and lipid coatings (Block NaOH for 5 min. Similarly, pH in 1 aliquot of corn silage and Jenkins, 1994) have been suggested as methods to (11 kg DM) was adjusted to be similar to alfalfa silage increase metabolizable lysine supplies from crystalline (pH = 4.6) by addition of 1.55 kg of 10% (wt/wt) NaOH, lysine. However, many diets fed to cows limited by me- and acidity in another aliquot (11 kg DM) of corn silage tabolizable lysine contain appreciable amounts of acidic was modified by mixing 3.15 kg of 10% (wt/wt) NaOH ingredients (e.g., corn silage, alfalfa silage) that may di- to achieve a pH (pH = 6.9) similar to the aliquot of alfalfa minish effectiveness of technologies sensitive to pH, and silage with added NaOH. mechanical forces associated with mixing may disturb Samples (4 g) of 2 lipid-coated lysine products capsule coatings. Most feed technologies currently used were each placed in heat sealed polyethylene bags (10 × to augment metabolizable lysine supply from crystalline 20 cm, pore size = 50 μm; Dacron, Ankom Technology, lysine utilize lipid coating. Yet, few data are available on Fairport, NY) and hand-mixed with each silage im- amounts of metabolizable lysine provided from lipid- mediately after modification of silage acidity. One coated lysine. Most evaluations of lipid-coated lysine lipid-coated lysine product (EB; LysiPEARL, Kemin are limited to measures of lysine loss from lipid-coated Industries, Des Moines, IA) was manufactured by ex- lysine after ruminal incubation or performance respons- trusion of lysine-HCl and lipid into small particles and es. Several reports suggest that appreciable amounts of contained 47.5% lysine-HCl and 52.5% lipid. Similarly, lysine are lost from lipid-coated lysine after ruminal in- the other lipid-coated lysine product (EC; USA Lysine, cubation and Wu et al. (2012) calculated that less than Kemin Industries) was also manufactured by extrusion half of lipid-coated lysine was able to disappear from of lysine-HCl and lipid into small particles and sub- mobile bags placed in the intestine. Direct measures of sequently the lysine-lipid particles were encapsulated metabolizable lysine to ruminants allows producers and with lipid; EC contained 65% lysine-HCl and 35% lip- nutritionists to appropriately value supplemental lysine id. After samples of lipid-coated lysine were incubated sources when formulating diets designed to meet me- in silage for 24 h polyethylene bags were removed tabolizable lysine requirements. Therefore, our objective and immediately rinsed with 5 L of cold tap water per in this work was to directly measure amounts of metabo- side over a 40 μm screen. After rinsing, samples were lizable lysine provided to ruminants from 2 lipid-coated frozen (–20°C) and lyophilized prior to removal from lysine products after exposure to silage. polyethylene bags. Effects of acidity and silage type on surface structure of each lipid-coated lysine was MATERIALS AND METHODS imaged by a scanning electron micrograph (Hitachi S-3400 N) after coating (10 nm) replicate subsamples All procedures involving the use of animals of each lipid-coated lysine with Au and 2 scanning were approved by the South Dakota State University electron micrographs from each replicate were cap- Institutional Animal Care and Use Committee. tured. Representative scanning electron micrographs are presented in Figs. 1, 2, and 3, respectively. All captured scanning electron micrographs are available Experiment 1 as supplementary material (Supplemental Figures S1 In a preliminary experiment, we evaluated effects thrugh S12; see online version of article to access the of mixing 2 lipid-coated lysine products with alfalfa- or material). Samples of lipid-coated lysine not incubated corn-silage at 2 different amounts of acidity. Alfalfa and with silage were imaged to allow visualization of lipid- corn silage were prepared by chopping alfalfa (50% DM; coated lysine surface structure before incubation with average particle size = 0.81 cm) or whole corn plants silage and prior to rinsing freezing and lyophilizing. (46% DM; average particle size = 0.79 cm). Chopped al- Additionally, samples (4 g) of each lipid-coated lysine falfa (0.7 ± 0.05 kg/L) and whole corn plants (0.6 ± 0.05 placed in polyethylene bags rinsed with 5 L of cold tap kg/L) were each packed separately into 4 miniature silos water per side over a 40 μm screen, frozen (–20 °C) and (121 L; 2 miniature silos for each silage type) and ensiled lyophilized but not incubated with silage were imaged Translate basic science to industry innovation Downloaded from https://academic.oup.com/tas/article-abstract/1/3/311/4636631 by Ed 'DeepDyve' Gillespie user on 10 April 2018 Bioavailability of lipid-coated lysine 313 Table 1. Composition of diet fed to ewes in Exp. 2 culated maintenance metabolizable energy requirement; NRC, 2007) twice daily (0730 and 1930 h). The diet was Item % of diet dry matter Ingredient composition, % dry matter designed to meet or slightly exceed requirements for pro- Corn silage 50.00 tein (NRC, 2007). Diet composition is reported in Table Dry-rolled corn 42.81 1. Samples (100 g) of the diet were collected daily and Cane molasses 2.50 composited by period and immediately frozen at –20°C. Fishmeal 2.00 Ewes were surgically fitted with abomasal cath - Limestone 1.00 eters as described by Freetly et al. (2010) at least 14 d Urea 0.66 prior to the experiment to allow abomasal infusion of Salt 0.50 lysine. Briefly, abomasal catheters were constructed Ammonium chloride 0.50 in the laboratory using 1 m of flexible polymer tub - Mineral premix 0.03 ing (0.8 cm o.d., 0.5 cm i.d.; Tygon, Saint-Gobain Chemical composition, % dry matter Performance Plastics, Akron, OH) that had a pair of Dry matter 61.12 cuffs constructed from slightly larger flexible polymer Organic matter 95.37 Crude protein 11.25 tubing (1.0 cm o.d., 0.5 cm i.d.) placed 2.54 cm apart Neutral detergent fiber 34.85 to create a 5 cm tip. Subsequently, catheters were sur- Acid detergent fiber 15.74 gically placed by dissection of the fundus under gen- Ether extract 4.67 eral anesthesia using isoflurane, and the tip of cath - Total amino acids 7.47 eters were inserted in the abomasum and a purse string Amino acid composition, % total amino acids suture was placed between each cuff. Catheters were Glutamic acid 16.61 exteriorized 1 cm ventral to the transverse process of Leucine 11.45 the L3 vertebra, and a permanent cuff (1.0 cm o.d., 0.5 Alanine 9.01 cm i.d.) was fixed to the external portion of the cath - Proline 9.00 eter to prevent retraction into the abdominal cavity. Aspartic acid 7.40 Ewes were placed in a 9 × 9 Latin square and treat- Valine 5.31 ments included control (no lysine supplementation) as Phenylalanine 5.16 Glycine 5.10 well as 5 or 10 g/d of lysine from EB, EC, or lysine-HCl Lysine 4.68 mixed with the diet 30 min prior to feeding. Additions Isoleucine 4.19 of EB, EC, or lysine-HCl to the diet was divided evenly Arginine 4.18 between feedings. Abomasal infusion of 5 or 10 g/d ly- Serine 4.05 sine acted as a positive control. Abomasal lysine was pre- Threonine 4.05 pared and delivered daily in 2.6 L of distilled water via Tyrosine 3.00 a peristaltic pump. When ewes did not receive aboma- Histidine 2.44 sal lysine infusion 2.6 L/d of distilled water alone was Methionine 1.88 abomasally infused. Each period consisted of 7 d; 6 d Cysteine 1.75 for adaptation and measures of plasma amino acids were Tryptophan 0.77 collected on Day 7 via jugular venipuncture 4 h after the Provided to diet (dry matter basis) 11.0 mg/kg Zn, 0.4 mg/kg Co, 44.4 morning feeding. Blood samples were placed on ice af- mg/kg ethylenediamine dihydroiodide, 20.3 mg/kg Fe, 38.7 mg/kg Mn, 4.2 mg/kg Na, 5528 IU of vitamin A/kg, 361 IU of vitamin D/kg, and 15 ter collection, immediately transferred to the laboratory IU of vitamin E/kg. and plasma was harvested by centrifugation (2,200 × g at 4°C) for 15 min. Plasma was stored frozen at –20°C until to visualize effects of rinsing, freezing and lyophilizing subsequent analysis of lysine via ultra-high performance on surface structure of lipid-coated lysine. chromatography. Ewe weights were collected immedi- ately following blood collection and used to calculate the subsequent periods daily feed offering. Experiment 2 Diet samples were thawed at room temperature Nine abomasally cannulated ewes (70.1 ± 5.2 kg; 5.3 (18°C), dried (55°C) in a forced-air oven for 48 h and ± 0.6 yr) were used in an experiment to measure lysine ground to pass a 1 mm screen (Thomas-Wiley laboratory bioavailability from feeding EB, EC, and lysine-HCl to mill model 4; Thomas Scientific USA, Swedesboro, NJ) ruminants by a slope-ratio analysis (Roach et al., 1967; prior to analyses of dry matter, organic matter, crude pro- Finney, 1978; Batterham et al., 1979; Elwakeel et al., tein, neutral detergent fiber, acid detergent fiber, and ether 2012). Ewes were individually housed (1.8 m × 0.72 extract. Dry matter content was determined by drying m) in a temperature (18°C) and light (16 h light daily) samples at 105°C for 24 h in a forced-air oven. The wet controlled room, and were limit-fed (1.6-times the cal- chemistry techniques of Van Soest et al. (1991) were used Translate basic science to industry innovation Downloaded from https://academic.oup.com/tas/article-abstract/1/3/311/4636631 by Ed 'DeepDyve' Gillespie user on 10 April 2018 314 Reiners et al. to quantify neutral detergent fiber and acid detergent fiber amino acids and the square correlation coefficients (R ) non-sequentially; diet neutral detergent fiber was mea - were 0.9983 for aspartic acid, 0.9977 for glutamic acid, sured in the presence of sodium sulfite and with addition 0.9996 for serine, 0.9991 for histidine, 0.9989 for gly- of ɑ-amylase. Diet samples were analyzed for ether ex- cine, 0.9996 for threonine, 0.9993 for arginine, 0.9991 tract (procedure AM 5–04; AOCS, 2005; Ankom XT10; for alanine, 0.9981 for tyrosine, 0.9963 for valine, 0.9964 Ankom Technology). Nitrogen content of diet samples for methionine, 0.9966 for phenylalanine, 0.9949 for iso- were determined by combustion (method 968.06; AOAC leucine and 0.9963 for lysine. International, 2012; Elementar Rapid MAX N exceed; Calculations. Slopes for each treatment were cal- Elementar, Langenselbold, Germany), and crude protein culated by regressing plasma lysine against amounts was calculated as 6.25 × N. Amino acid concentration of lysine provided in feed or abomasally infused. of diet samples was analyzed by high performance liq- Subsequently, lysine bioavailability was calculated as the uid chromatography (method number 982.30; AOAC ratio of the slopes of EB, EC or lysine-HCl to that of ab- International, 2006). Prior to measures of methionine omasal lysine infusion (Roach et al., 1967; Finney, 1978; and cysteine in diet, the sulfur containing amino acid Batterham et al., 1979; Elwakeel et al., 2012). were oxidized with performic acid, and tryptophan was Statistical Analyses. Plasma lysine was regressed on determined from diet samples after alkaline hydrolysis amounts of lysine added from EB, EC, lysine-HCl, or ab- (method number 982.30; AOAC International, 2006). omasal infusion using the MIXED procedures of SAS ( Plasma lysine content was analyzed for free lysine SAS Inst. Inc., Cary, NC); sheep and period were random by reversed phase ultra-high performance liquid chro- class variables, and amounts of lysine within source of matography after pre-column derivatization of amino supplemental lysine were regression variables. Plasma acids with o-phthaldialdehyde (Dai et al., 2014). Prior amino acid concentration was analyzed as a Latin square to chromatography, 2 mL of plasma was mixed with 2 using the MIXED procedure of SAS; the model included mL of 10% sulfosalicylic acid containing 1 mM norva- effects of treatment and effects of animal and period were line as an internal standard for amino acid analysis. After considered random. Denominator degrees of freedom cooling on ice for 30 min., samples were vortexed and were calculated by the Kenward and Roger adjustment centrifuged (13,800 × g). The supernatant was analyzed (Kenward and Roger, 1997). Effects of added lysine to and chromatography was achieved on a C column (3.0 feed from EB, EC, lysine-HCl or abomasal infusion were × 150 mm, 3.5 µm; Agilent Corp, Santa Clara, CA) af- determined by linear contrasts. ter passing a C guard column (2.1 × 12.5 mm, 5 µm). The combined flow rate of the mobile phase was con - RESULTS AND DISCUSSION stant and 0.64 mL/min. The initial mobile phase (A) was composed of water containing 9.87 µmol/L Na HPO , 2 4 Experiment 1 18.89 µmol/L Na B O , and 0.49 µmol/L NaN . The 2 4 7 3 second mobile phase (B) was composed of water con- Block and Jenkins (1994) observed large amounts taining 8.58 mol/L acetonitrile and 11.11 mol/L metha- of lysine loss from lipid-associated lysine during rumi- nol. The percentage of mobile phase A was as follows: 0 nal incubation. These authors (Block and Jenkins, 1994) min, 98%; 20 min, 43%; 20.1 min, 0%; 23.6 min, 98%. speculated that lysine associated with the surface of the The column was maintained at 40°C and injection vol- lysine-lipid particle was rapidly solubilized during rumi- umes were 16 μL. Amounts of plasma lysine were quan- nal incubation and that diminished surface integrity of tified in reference to norvaline and measured at 338 nm the lysine-lipid particle allowed movement of ruminal (bandwidth = 10 nm) and the reference wavelength was fluid throughout the lysine-lipid particle. Reduced in - 390 nm (bandwidth = 20 nm) with a diode array detector tegrity of the lipid-lysine particle may also allow move- (Ultimate 3000; Thermo Electron North America, West ment of water throughout the lysine-lipid particle when Palm Beach, FL). Prior to analyses of plasma amino mixed with diets that contain large amounts of moisture acids, replicate amino acid standards at 15, 30 and 60 and increase lysine lost from lipid-coated lysine. Ji et al. μmol/L were analyzed to evaluate precision of analy- (2016) reported that increased exposure to a silage-based sis. The intra-assay coefficients of variation were 1.7 ± diet increased amount of lysine loss from lipid-coated 0.46 for aspartic acid, 1.5 ± 0.41 for glutamic acid, 1.2 lysine products. Further, we (Reiners and Brake, 2016) ± 0.44 for serine, 1.2 ± 0.11 for histidine, 1.6 ± 0.42 for previously reported that amounts of lysine lost from lip- glycine, 1.3 ± 0.42 for threonine, 1.6 ± 0.42 for arginine, id-associated lysine affected by silage type, acidity, and 1.8 ± 0.26 for alanine, 1.7 ± 0.26 for tyrosine, 2.4 ± 0.15 manufacture; however, we are not aware of any effort to for valine, 2.1 ± 0.04 for methionine, 2.1 ± 0.19 for phe- image lipid-associated lysine surface structure after mix- nylalanine, 2.0 ± 0.25 for isoleucine and 2.6 ± 0.19 for ing lipid-associated lysine with alfalfa or corn silage con- lysine. Additionally, the area response was linear for all taining different amounts of acidity. Translate basic science to industry innovation Downloaded from https://academic.oup.com/tas/article-abstract/1/3/311/4636631 by Ed 'DeepDyve' Gillespie user on 10 April 2018 Bioavailability of lipid-coated lysine 315 Figure 1. Scanning electron microscropy of lipid-coated lysine after 24 h incubation in alfalfa silage. Panel A: Scanning electron micrograph of EB (lipid-coated lysine that contained 47.5% lysine-HCl and 52.5% lipid) after incubation in low pH alfalfa silage. Panel B: Scanning electron micrograph of EC (lipid-coated lysine that contained 65% lysine-HCl and 35% lipid) incubated in low pH alfalfa silage. Panel C: Scanning electron micrograph of EB incubated in neutral pH alfalfa silage. Panel D: Scanning electron micrograph of EC incubated in neutral pH alfalfa silage. Surface structures of lipid-coated lysine appeared to crographs seemed to indicate that the surface structure of be impacted by mixing it with alfalfa- (Fig. 1) or corn lipid-associated lysine mixed with alfalfa silage was de- silage (Fig. 2) in comparison coated lysine that was not graded equally despite differences in silage pH; however, mixed with silage (Fig. 3). Evaluation of scanning elec- the surface structure of lipid-associated lysine mixed with tron micrographs of lipid-coated lysine not exposed to corn silage appeared to be more disrupted when mixed silage, rinsing, freezing and lyophilizing compared to lip- with more acidic corn silage in comparison to less acidic id-coated lysine that was rinsed, frozen and lyophilized corn silage. Indeed, these surface structure images ap- but not exposed to silage indicate that rinsing, freezing pear to be in agreement with our previous observation and lyophilizing had little impact on lipid-coated lysine (Reiners and Brake, 2016) that greater acidity increased surface structures. Additionally, scanning electron mi- amounts of lysine lost from lipid-associated lysine mixed Figure 2. Scanning electron microscopy of lipid-coated lysine after 24 h incubation in corn silage. Panel A: Scanning electron micrograph of EB (lipid-coated lysine that contained 47.5% lysine-HCl and 52.5% lipid) incubated in low pH corn silage. Panel B: Scanning electron micrograph of EC (lipid- coated lysine that contained 65% lysine-HCl and 35% lipid) incubated in low pH corn silage. Panel C: Scanning electron micrograph of EB incubated in neutral pH corn silage. Panel D: Scanning electron micrograph of EC incubated in neutral pH corn silage Translate basic science to industry innovation Downloaded from https://academic.oup.com/tas/article-abstract/1/3/311/4636631 by Ed 'DeepDyve' Gillespie user on 10 April 2018 316 Reiners et al. Figure 3. Scanning electron microscopy of lipid-coated lysine products prior to incubation in silages. Panel A: Scanning electron micrograph of EB (lipid-coated lysine that contained 47.5% lysine-HCl and 52.5% lipid). Panel B: Scanning electron micrograph of EC (lipid-coated lysine that contained 65% lysine-HCl and 35% lipid). Panel C: Scanning electron micrograph of EB not exposed to silage but after rinsing with water, freezing and lyophilizing. Panel D: Scanning electron micrograph of EC not exposed to silage but after rinsing with water, freezing and lyophilizing. with corn silage but that acidity had little impact on omasum. Our data indicate that bioavailability of lysine amount of lysine lost from lipid-associated lysine mixed from EC, EB, and lysine-HCl in feed was 23, 15, and with alfalfa silage. Obviously, surface structure images 18%, respectively. Even though each source of lysine are subjective measures, but these images appear to agree provided a positive rate of increase among plasma ly- with the report of Ji et al. (2016), our previous observa- sine sources, rates of increase in plasma lysine from EB tions (Reiners and Brake, 2016) and the conclusions of (linear; P = 0.20) and lysine-HCl (linear; P = 0.11) were Block and Jenkins (1994). Regardless, images from this not different from plasma lysine levels supported by preliminary study clearly indicate that measures of lysine diet alone. However, the rate of plasma lysine increase bioavailability are necessary to allow an improved un- in response to lysine from EC was greater (linear; P = derstanding of amounts of metabolizable lysine provided 0.04) than plasma lysine from feed alone. Yet, the rate from lipid-coated lysine after exposure to silage. of plasma lysine increase in response to lipid-coated ly- sine did not differ ( P ≥ 0.70) from the rate of plasma lysine increase from lysine-HCl. Experiment 2 Effects of feeding lipid-coated lysine on plasma ly - Rulquin and Kowalczyk (2003) reported that ab- sine concentration and lactation performance among lac- omasal infusion of graded amounts of lysine to lac- tating cows fed silage-based diets are variable. Several tating cows and subsequent measurement of plasma authors (Robinson et al., 2011; Giallongo et al., 2016) lysine is more effective than in vitro procedures to reported increases in plasma lysine and milk protein determine amounts of metabolizable lysine from lip- content when lactating cows were supplemented with id-coated lysine. We used 9 mature ewes fitted with lipid-coated lysine. Conversely, others (Swanepoel et al., abomasal catheters and fed diets designed to not be 2010; Robinson et al., 2010; Lee et al., 2012, 2015) re- limiting in lysine to evaluate amounts of metaboliz- ported no effect of lipid-coated lysine on plasma lysine able lysine provided from lipid-coated lysine or ly- and milk protein concentration. Authors have speculated sine-HCl after mixing with corn silage. (Robinson et al., 2010; Swanepoel et al., 2010) that a lack Plasma lysine concentrations (Fig. 4) increased lin- of response among plasma lysine or milk protein may early (P < 0.01) in response to abomasal infusion of ly- have been related to changes in partitioning of amino sine indicating that our model was sensitive to increases acids for physiological functions other than milk pro- in metabolizable lysine flow. Bioavailability of EC, EB, tein production or because diets were not first-limited by and lysine-HCl in feed was calculated as the ratio of metabolizable lysine. However, Wu et al. (2012) calcu- the rate of plasma lysine increase from EC, EB, or ly- lated that only 11.5% of lysine from lipid-coated lysine sine-HCl in feed to the rate of plasma lysine increase in was digested in the small intestine of cows when they response to known amounts of lysine infused to the ab- measured lysine loss from lipid-coated lysine in mobile Translate basic science to industry innovation Downloaded from https://academic.oup.com/tas/article-abstract/1/3/311/4636631 by Ed 'DeepDyve' Gillespie user on 10 April 2018 Bioavailability of lipid-coated lysine 317 Figure 4. Plasma lysine concentration in ewes provided lysine as an abomasal infusion of lysine-HCL or as dietary lysine-HCl (Panel A), EB (Panel B; lipid-coated lysine that contained 47.5% lysine-HCl and 52.5% lipid), or EC (Panel C; lipid-coated lysine that contained 65% lysine-HCl and 35% lipid). Standard error of estimate = 1.3. Translate basic science to industry innovation Downloaded from https://academic.oup.com/tas/article-abstract/1/3/311/4636631 by Ed 'DeepDyve' Gillespie user on 10 April 2018 318 Reiners et al. Table 2. Effect of 0, 5 or 10 g/d lysine from abomasal infusion or from lysine-HCl and 2 lipid-coated lysine prod - ucts added to a corn silage-based diet on plasma amino acid concentrations (µmol/L) in sheep 2 3 Control Infused Lysine-HCl EB EC Linear contrasts AA None 5 10 5 10 5 10 5 10 SEM Infused Lysine-HCl EB EC Glu 28.8 25.3 26.0 29.5 27.7 22.3 24.1 30.6 23.5 3.9 0.35 0.71 0.11 0.07 Asp 20.5 16.0 17.0 19.4 17.8 18.3 19.9 17.9 17.1 1.8 0.06 0.14 0.75 0.07 Ser 21.1 18.3 21.0 19.9 18.4 18.8 20.6 23.0 17.6 1.5 0.94 0.12 0.78 0.04 Gln 252.3 232.8 250.0 257.7 226.7 228.6 264.0 263.0 232.7 16.2 0.88 0.11 0.46 0.22 His 49.4 46.6 45.2 47.7 45.6 47.6 48.0 50.1 48.3 3.7 0.23 0.27 0.68 0.75 Gly 123.9 109.1 110.3 110.6 109.5 114.0 128.2 119.9 107.6 9.0 0.09 0.07 0.58 0.04 Thr 32.8 26.0 25.3 25.4 31.8 28.4 28.3 30.9 25.1 3.9 0.08 0.82 0.29 0.08 Arg 66.6 66.4 78.5 64.9 61.0 63.0 68.3 64.9 64.9 5.8 0.06 0.38 0.80 0.79 Ala 45.9 44.9 47.2 46.0 40.8 42.4 43.6 45.9 41.0 3.1 0.72 0.14 0.51 0.15 Tyr 26.1 21.3 20.3 24.6 24.8 24.5 23.0 24.4 20.9 2.1 <0.01 0.47 0.10 0.01 Val 40.3 42.9 43.3 42.3 40.9 41.6 42.8 41.8 38.6 4.7 0.52 0.90 0.59 0.72 Phe 17.9 16.3 14.6 17.4 16.9 17.0 15.9 16.5 15.5 1.5 0.01 0.42 0.12 0.07 Ile 22.3 21.3 21.8 21.7 19.8 20.4 21.0 19.6 19.4 2.5 0.82 0.30 0.60 0.23 Leu 28.3 27.3 27.1 27.5 24.9 26.7 28.0 26.9 21.3 3.0 0.67 0.19 0.91 0.01 Lys 39.5 81.1 158.8 48.2 53.7 39.9 52.3 46.5 62.0 11.3 <0.01 0.36 0.41 0.15 Amino acids are described by standard 3 letter abbreviations. Lipid coated lysine that contained 47.5% lysine-HCl and 52.5% lipid. Lipid coated lysine that contained 65% lysine-HCl and 35% lipid. bags, and Paz and Kononoff (2014) speculated that a of lysine apparently available to be digested in the small lack of response in arterial lysine concentration among intestine of cows (Wu et al., 2012). cows fed lipid-coated lysine was because lipid-coated Plasma amino acid concentrations are reported in lysine provided less metabolizable lysine than expected. Table 2. The only amino acids affected by treatment other Regardless of the reason for a lack of response to lipid- than lysine were modest changes in serine, tyrosine, phe- coated lysine, it cannot be discounted that one explana- nylalanine, leucine, and glycine. Specifically, increased in - tion to a lack of performance response to lipid-coated take of EC and greater abomasal infusion of lysine reduced lysine may be that amounts of metabolizable lysine from (linear; P ≤ 0.01) plasma tyrosine. Greater amounts of ly - lipid-coated lysine were less than anticipated. sine from EC decreased (linear; P = 0.03) plasma serine, Rulquin and Kowalczyk (2003) concluded that use leucine, and glycine. Additionally abomasal infusion of of lipid-coated lysine may be useful to evaluate bio- lysine decreased (linear; P = 0.01) plasma phenylalanine. availability of amino acids from feed. However, our A specific explanation for slight changes in circulating data together with others (Ji et al., 2016) emphasize concentrations of serine, tyrosine, phenylalanine, leucine, caution when using lipid-coated lysine as a positive and glycine remains unknown. Evidently, increases in control in determining estimates of lysine bioavailabil- both metabolizable lysine and ruminally degraded lysine ity, and that lipid-coated lysine should only be used as can impact circulating amino acid concentrations. a positive control after effects of physical and chemi - cal characteristics of diet on availability of lysine from Conclusions lipid-coated lysine has been validated. Generally, slope ratio analyses represent direct mea- Our data indicate that lipid-coated lysine can sures of an amino acid’s availability to non-splanchnic provide metabolizable lysine to ruminants, but that tissues (McNab, 1994; Moehn et al., 2005). Thus, it is amounts of metabolizable lysine from lipid-coated surprising that only a limited number of reports are avail- lysine are affected by both physical and chemical able that have measured amino acid availability from characteristics of diet. More direct measurements of “ruminally-protected” amino acid products to ruminants. lysine availability to ruminants are needed to improve Our data indicate that relatively modest amounts of me- estimates of metabolizable lysine from lipid-coated tabolizable lysine were available to sheep from lipid- lysine products in various feeding conditions, and it is coated lysine mixed with corn silage. It is possible that possible that variation in production responses to lip- measures of metabolizable lysine from lipid-coated ly- id-coated lysine are related to inaccurate estimates of sine could differ between ruminant species; however, our amounts of metabolizable lysine provided from lipid- measures of lysine bioavailability are similar to amounts coated lysine. Reduced exposure of lipid-coated lysine Translate basic science to industry innovation Downloaded from https://academic.oup.com/tas/article-abstract/1/3/311/4636631 by Ed 'DeepDyve' Gillespie user on 10 April 2018 Bioavailability of lipid-coated lysine 319 to silage-based or acidic diets may augment amounts Lewis, T. R., and R. S. Emery. 1962. Relative deamination rates of amino acids in rumen microorganisms. J. Dairy Sci. 45:765–768. of metabolizable lysine provided to ruminants. doi:10.3168/jds.S0022-0302(62)89485-5 Mangan, J. L. 1972. Quantitative studies on nitrogen metabolism in the LITERATURE CITED bovine rumen. Br. J. Nutr. 27:261–283. doi:10.1079/BJN19720092 McNab, J. M. 1994. Amino acid digestibility and availability studies AOAC International. 2006. Official Methods of Analysis. 18th ed. with poultry. In: J. P. F. D’Mello, editor, Amino Acids in Farm AOAC International, Arlington, VA. Animal Nutrition. CAB International, UK. p. 63–98. AOAC International. 2012. Official Methods of Analysis. 19th ed. Moehn, S., R. F. P. Bertolo, P. B. Pencharz, and R. O. Ball. 2005. AOAC International, Arlington, VA. Development of the indicator amino acid oxidation technique to AOCS. 2005. Official Methods and Recommended Practices of the determine the availability of amino acids for dietary protein in AOCS. 6th ed. AOCS, Urbana, IL. pigs. J. Nutr. 135:2866–2870. Batterham, E. S., R. D. Murison, and C. E. Lewis. 1979. Availability NRC. 2001. Nutrient Requirements of Dairy Cattle. 7th rev. ed. Natl. of lysine in protein concentrates as determined by the slope-ratio Acad. Press, Washington, DC. assay with growing pigs and rate and by chemical techniques. Br. NRC. 2007. Nutrient Requirements of Small Ruminants: Sheep, J. Nutr. 41:383–391. doi:10.1079/BJN19790047 Goats, Cervids, and New World Camelids. Natl. Acad. Press, Block, S. M., and T. C. Jenkins. 1994. The use of prilled fat to coat and Washington, DC. protect amino acids from ruminal degradation. J. Sci. Food Agric. Paz, H. A., and P. J. Kononoff. 2014. Lactation responses and amino 65:441–447. doi:10.1002/jsfa.2740650412 acid utilization of dairy cows fed low-fat distillers dried grains Bremmer, D. R., T. R. Overton, and J. H. Clark. 1997. Production and with solubles with or without rumen-protected lysine supplemen- composition of milk from Jersey cows administered bovine so- tation. J. Dairy Sci. 97:6519–6530. doi:10.3168/jds.2014-8315 matotropin and fed ruminally protected amino acids. J. Dairy Sci. Reiners, J. N., and D. W. Brake. 2016. 1492 Effects of acidity and 80:1374–1380. doi:10.3168/jds.S0022-0302(97)76066-1 silage type on lysine retention among two lipid-coated rumi- Chalupa, W. 1975. Rumen bypass and protection of proteins and ami- nally protected lysine products. J. Anim. Sci. 94(Suppl5):724. no acids. J. Dairy Sci. 58:1198–1218. doi:10.3168/jds.S0022- doi:10.2527/jam2016-1492 0302(75)84697-2 Roach, A. G., P. Sanderson, and D. R. Williams. 1967. Comparison of Clark, J. H. 1975. Lactational responses to postruminal administra- methods for the determination of available lysine value in animal tion of proteins and amino acids. J. Dairy Sci. 58:1178–1197. and vegetable protein sources. J. Sci. Food Agric. 18:274–278. doi:10.3168/jds.S0022-0302(75)84696-0 doi:10.1002/jsfa.2740180702 Dai, Z., Z. Wu, S. Jia, and G. Wu. 2014. Analysis of amino acid com- Robinson, P. H., N. Swanepoel, and E. Evans. 2010. Effects of feeding a position in proteins of animal tissues and foods as pre-column ruminally protected lysine product, with or without isoleucine, va- o-phthaldialdehyde derivatives by HPLC with fluorescence line and histidine, to lactating dairy cows on their productive per- detection. J. Chromatogr. B Analyt. Technol. Biomed. Life Sci. formance and plasma amino acid profiles. Anim. Feed Sci. Technol. 964:116–127. doi:10.1016/j.jchromb.2014.03.025 161:75–84. doi:10.1016/j.anifeedsci.2010.07.017 Elwakeel, E. A., E. C. Titgemeyer, B. R. Faris, D. W. 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Parys. 2012. Rumen- cape and intestinal digestibility of ruminally protected lysine supple- protected lysine, methionine, and histidine increase milk protein ments differing in oleic acid and lysine concentrations. J. Dairy Sci. yield in dairy cows fed a metabolizable protein-deficient diet. J. 95:2680–2684. doi:10.3168/jds.2011-5203 Dairy Sci. 95:6042–6056. doi:10.3168/jds.2012-5581 Xu, S., J. H. Harrison, W. Chalupa, C. Sniffen, W. Julien, H. Sato, T. Lee, C., F. Giallongo, A. N. Hristov, H. Lapierre, T. W. Cassidy, K. S. Fujieda, H. Watanabe, T. Ueda, and H. Suzuki. 1998. The ef- Heyler, G. A. Varga, and C. Parys. 2015. Effect of dietary protein fect of ruminal bypass lysine and methionine on milk yield and level and rumen-protected amino acid supplementation on amino composition of lactating cows. J. Dairy Sci. 81:1062–1077. acid utilization for milk protein in lactating dairy cows. J. Dairy Sci. doi:10.3168/jds.S0022-0302(98)75668-1 98:1885–1902. doi:10.3168/jds.2014-8496 Translate basic science to industry innovation Downloaded from https://academic.oup.com/tas/article-abstract/1/3/311/4636631 by Ed 'DeepDyve' Gillespie user on 10 April 2018 http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Translational Animal Science Oxford University Press

Lysine bioavailability among 2 lipid-coated lysine products after exposure to silage

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10.2527/tas2017.0037
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J. N. Reiners,* J. E. Held,* C. L. Wright,* Q. Qiao,† G. D. Djira,‡ B. R. Brunsvig,* K. M. Reza,† and D. W. Brake* *Department of Animal Science, South Dakota State University, Brookings 57007; and †Department of Electrical Engineering and Computer Science, South Dakota State University, Brookings 57007 and ‡Department of Mathematics and Statistics, South Dakota State University, Brookings 57007 ABSTRACT: We conducted 2 experiments to deter- dietary lysine-HCl were calculated to be 23, 15, and mine lysine bioavailability from 2 lipid-coated lysine 18%, respectively. Even though each dietary source products. In an in vitro experiment we mixed each of lysine increased plasma lysine, rates of increases in lipid-coated lysine product with either alfalfa- or plasma lysine from one lipid-coated lysine source (lin- corn-silage at different amounts of acidity. Scanning ear; P = 0.20) and lysine-HCl (linear; P = 0.11) were electron micrographs indicated that surface struc- not different from plasma lysine levels supported by ture of each lipid-coated lysine particle was eroded diet alone. However, the rate of plasma lysine increase after mixing with silage. Additionally, visual evalua- in response to lysine from the other lipid-coated lysine tion of scanning electron micrographs suggested that source was greater (P = 0.04) than plasma lysine from peripheral surface abrasion of lipid-coated lysine may feed alone. Nonetheless, the rate of plasma lysine be greater when lipid-coated lysine was mixed with increase in response to lipid-coated lysine did not dif- alfalfa silage in comparison to corn silage. In a cor- fer (P ≥ 0.70) from the rate of plasma lysine increase responding experiment, in vivo measures of lysine from lysine-HCl. Clearly, methods of manufacture, bioavailability to sheep from 2 lipid-coated lysine together with physical and chemical characteristics products and lysine-HCl were determined after mix- of diet, can impact amounts of metabolizable lysine ing in corn silage. Plasma lysine concentrations provided from lipid-coated lysine products. Direct increased linearly (P < 0.01) in response to aboma- measures of lysine bioavailability from lipid-coated sal lysine infusion indicating that our model was lysine products after mixing with diets should be sensitive to increases in metabolizable lysine flow. based on measurements with the products treated sim- Bioavailability of each lipid-coated lysine source and ilarly to the method of feeding. Key words: amino acid, bioavailability, cattle, lysine, silage © 2017 American Society of Animal Science. This is an open access article distributed under the CC BY-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/4.0/) Transl. Anim. Sci. 2017.1:311–319 doi:10.2527/tas2017.0037 INTRODUCTION cows are fed diets with greater amounts of metaboliz- able lysine. Specifically, greater metabolizable lysine Protein synthesis and milk protein production can increase milk protein content and yield (Clark, among lactating cows fed corn-based diets is often 1975; NRC, 2001; Paz and Kononoff, 2014) and milk first-limited by metabolizable lysine (NRC, 2001). protein secretions. Several authors have also reported Therefore, efficiency of N used for productive purposes that greater amounts of metabolizable lysine can also (i.e., milk N and N retained) is increased when lactating improve milk fat content and secretions (Bremmer et al., 1997; Xu et al., 1998). Most feeds commonly used to increase flow of metabolizable protein to cows do not This project was supported by the USDA National Institute perfectly complement metabolizable proteins from corn. of Food and Agriculture (Washington, DC). This project is a con- Thus, supplementation of complex proteins to improve tribution from the South Dakota Agricultural Experiment Station, Brookings, SD 57007. efficiency of N use in cows is limited in comparison Corresponding author: derek.brake@sdstate.edu to supplementation of individual amino acids to meet Received May 10, 2017. limits in metabolizable amino acids. Unfortunately, Accepted July 15, 2017. Downloaded from https://academic.oup.com/tas/article-abstract/1/3/311/4636631 by Ed 'DeepDyve' Gillespie user on 10 April 2018 312 Reiners et al. most free amino acids are rapidly degraded by ruminal for 169 and 154 d, respectively. Alfalfa (pH = 4.4 ± 0.1) microbiota (Lewis and Emery, 1962; Chalupa, 1975) and corn silage (pH = 3.7 ± 0.1) from each miniature silo and supplementation of crystalline amino acids provides were composited by silage type after ensiling. only small increases in metabolizable amino acid supply Acidity of silage was modified prior to incubation of (Mangan, 1972). Many technologies have been devel- lipid-coated lysine to evaluate effects of acidity and si - oped to increase metabolizable amino acid flows from lage type on surface structure of lipid-coated lysine. The crystalline amino acids to ruminants (Wu and Papas, pH in an aliquot (9.5 kg DM) of alfalfa silage was in- 1997). Hydroxymethyl analogs (Elwakeel et al., 2012), creased to 6.8 after initial measures of acidity by mixing acid degradable polymeric coatings (Titgemeyer et al., (model 2030, Marion Mixer) with 2.8 kg of 10% (wt/wt) 1988; Klemesrud et al., 2000) and lipid coatings (Block NaOH for 5 min. Similarly, pH in 1 aliquot of corn silage and Jenkins, 1994) have been suggested as methods to (11 kg DM) was adjusted to be similar to alfalfa silage increase metabolizable lysine supplies from crystalline (pH = 4.6) by addition of 1.55 kg of 10% (wt/wt) NaOH, lysine. However, many diets fed to cows limited by me- and acidity in another aliquot (11 kg DM) of corn silage tabolizable lysine contain appreciable amounts of acidic was modified by mixing 3.15 kg of 10% (wt/wt) NaOH ingredients (e.g., corn silage, alfalfa silage) that may di- to achieve a pH (pH = 6.9) similar to the aliquot of alfalfa minish effectiveness of technologies sensitive to pH, and silage with added NaOH. mechanical forces associated with mixing may disturb Samples (4 g) of 2 lipid-coated lysine products capsule coatings. Most feed technologies currently used were each placed in heat sealed polyethylene bags (10 × to augment metabolizable lysine supply from crystalline 20 cm, pore size = 50 μm; Dacron, Ankom Technology, lysine utilize lipid coating. Yet, few data are available on Fairport, NY) and hand-mixed with each silage im- amounts of metabolizable lysine provided from lipid- mediately after modification of silage acidity. One coated lysine. Most evaluations of lipid-coated lysine lipid-coated lysine product (EB; LysiPEARL, Kemin are limited to measures of lysine loss from lipid-coated Industries, Des Moines, IA) was manufactured by ex- lysine after ruminal incubation or performance respons- trusion of lysine-HCl and lipid into small particles and es. Several reports suggest that appreciable amounts of contained 47.5% lysine-HCl and 52.5% lipid. Similarly, lysine are lost from lipid-coated lysine after ruminal in- the other lipid-coated lysine product (EC; USA Lysine, cubation and Wu et al. (2012) calculated that less than Kemin Industries) was also manufactured by extrusion half of lipid-coated lysine was able to disappear from of lysine-HCl and lipid into small particles and sub- mobile bags placed in the intestine. Direct measures of sequently the lysine-lipid particles were encapsulated metabolizable lysine to ruminants allows producers and with lipid; EC contained 65% lysine-HCl and 35% lip- nutritionists to appropriately value supplemental lysine id. After samples of lipid-coated lysine were incubated sources when formulating diets designed to meet me- in silage for 24 h polyethylene bags were removed tabolizable lysine requirements. Therefore, our objective and immediately rinsed with 5 L of cold tap water per in this work was to directly measure amounts of metabo- side over a 40 μm screen. After rinsing, samples were lizable lysine provided to ruminants from 2 lipid-coated frozen (–20°C) and lyophilized prior to removal from lysine products after exposure to silage. polyethylene bags. Effects of acidity and silage type on surface structure of each lipid-coated lysine was MATERIALS AND METHODS imaged by a scanning electron micrograph (Hitachi S-3400 N) after coating (10 nm) replicate subsamples All procedures involving the use of animals of each lipid-coated lysine with Au and 2 scanning were approved by the South Dakota State University electron micrographs from each replicate were cap- Institutional Animal Care and Use Committee. tured. Representative scanning electron micrographs are presented in Figs. 1, 2, and 3, respectively. All captured scanning electron micrographs are available Experiment 1 as supplementary material (Supplemental Figures S1 In a preliminary experiment, we evaluated effects thrugh S12; see online version of article to access the of mixing 2 lipid-coated lysine products with alfalfa- or material). Samples of lipid-coated lysine not incubated corn-silage at 2 different amounts of acidity. Alfalfa and with silage were imaged to allow visualization of lipid- corn silage were prepared by chopping alfalfa (50% DM; coated lysine surface structure before incubation with average particle size = 0.81 cm) or whole corn plants silage and prior to rinsing freezing and lyophilizing. (46% DM; average particle size = 0.79 cm). Chopped al- Additionally, samples (4 g) of each lipid-coated lysine falfa (0.7 ± 0.05 kg/L) and whole corn plants (0.6 ± 0.05 placed in polyethylene bags rinsed with 5 L of cold tap kg/L) were each packed separately into 4 miniature silos water per side over a 40 μm screen, frozen (–20 °C) and (121 L; 2 miniature silos for each silage type) and ensiled lyophilized but not incubated with silage were imaged Translate basic science to industry innovation Downloaded from https://academic.oup.com/tas/article-abstract/1/3/311/4636631 by Ed 'DeepDyve' Gillespie user on 10 April 2018 Bioavailability of lipid-coated lysine 313 Table 1. Composition of diet fed to ewes in Exp. 2 culated maintenance metabolizable energy requirement; NRC, 2007) twice daily (0730 and 1930 h). The diet was Item % of diet dry matter Ingredient composition, % dry matter designed to meet or slightly exceed requirements for pro- Corn silage 50.00 tein (NRC, 2007). Diet composition is reported in Table Dry-rolled corn 42.81 1. Samples (100 g) of the diet were collected daily and Cane molasses 2.50 composited by period and immediately frozen at –20°C. Fishmeal 2.00 Ewes were surgically fitted with abomasal cath - Limestone 1.00 eters as described by Freetly et al. (2010) at least 14 d Urea 0.66 prior to the experiment to allow abomasal infusion of Salt 0.50 lysine. Briefly, abomasal catheters were constructed Ammonium chloride 0.50 in the laboratory using 1 m of flexible polymer tub - Mineral premix 0.03 ing (0.8 cm o.d., 0.5 cm i.d.; Tygon, Saint-Gobain Chemical composition, % dry matter Performance Plastics, Akron, OH) that had a pair of Dry matter 61.12 cuffs constructed from slightly larger flexible polymer Organic matter 95.37 Crude protein 11.25 tubing (1.0 cm o.d., 0.5 cm i.d.) placed 2.54 cm apart Neutral detergent fiber 34.85 to create a 5 cm tip. Subsequently, catheters were sur- Acid detergent fiber 15.74 gically placed by dissection of the fundus under gen- Ether extract 4.67 eral anesthesia using isoflurane, and the tip of cath - Total amino acids 7.47 eters were inserted in the abomasum and a purse string Amino acid composition, % total amino acids suture was placed between each cuff. Catheters were Glutamic acid 16.61 exteriorized 1 cm ventral to the transverse process of Leucine 11.45 the L3 vertebra, and a permanent cuff (1.0 cm o.d., 0.5 Alanine 9.01 cm i.d.) was fixed to the external portion of the cath - Proline 9.00 eter to prevent retraction into the abdominal cavity. Aspartic acid 7.40 Ewes were placed in a 9 × 9 Latin square and treat- Valine 5.31 ments included control (no lysine supplementation) as Phenylalanine 5.16 Glycine 5.10 well as 5 or 10 g/d of lysine from EB, EC, or lysine-HCl Lysine 4.68 mixed with the diet 30 min prior to feeding. Additions Isoleucine 4.19 of EB, EC, or lysine-HCl to the diet was divided evenly Arginine 4.18 between feedings. Abomasal infusion of 5 or 10 g/d ly- Serine 4.05 sine acted as a positive control. Abomasal lysine was pre- Threonine 4.05 pared and delivered daily in 2.6 L of distilled water via Tyrosine 3.00 a peristaltic pump. When ewes did not receive aboma- Histidine 2.44 sal lysine infusion 2.6 L/d of distilled water alone was Methionine 1.88 abomasally infused. Each period consisted of 7 d; 6 d Cysteine 1.75 for adaptation and measures of plasma amino acids were Tryptophan 0.77 collected on Day 7 via jugular venipuncture 4 h after the Provided to diet (dry matter basis) 11.0 mg/kg Zn, 0.4 mg/kg Co, 44.4 morning feeding. Blood samples were placed on ice af- mg/kg ethylenediamine dihydroiodide, 20.3 mg/kg Fe, 38.7 mg/kg Mn, 4.2 mg/kg Na, 5528 IU of vitamin A/kg, 361 IU of vitamin D/kg, and 15 ter collection, immediately transferred to the laboratory IU of vitamin E/kg. and plasma was harvested by centrifugation (2,200 × g at 4°C) for 15 min. Plasma was stored frozen at –20°C until to visualize effects of rinsing, freezing and lyophilizing subsequent analysis of lysine via ultra-high performance on surface structure of lipid-coated lysine. chromatography. Ewe weights were collected immedi- ately following blood collection and used to calculate the subsequent periods daily feed offering. Experiment 2 Diet samples were thawed at room temperature Nine abomasally cannulated ewes (70.1 ± 5.2 kg; 5.3 (18°C), dried (55°C) in a forced-air oven for 48 h and ± 0.6 yr) were used in an experiment to measure lysine ground to pass a 1 mm screen (Thomas-Wiley laboratory bioavailability from feeding EB, EC, and lysine-HCl to mill model 4; Thomas Scientific USA, Swedesboro, NJ) ruminants by a slope-ratio analysis (Roach et al., 1967; prior to analyses of dry matter, organic matter, crude pro- Finney, 1978; Batterham et al., 1979; Elwakeel et al., tein, neutral detergent fiber, acid detergent fiber, and ether 2012). Ewes were individually housed (1.8 m × 0.72 extract. Dry matter content was determined by drying m) in a temperature (18°C) and light (16 h light daily) samples at 105°C for 24 h in a forced-air oven. The wet controlled room, and were limit-fed (1.6-times the cal- chemistry techniques of Van Soest et al. (1991) were used Translate basic science to industry innovation Downloaded from https://academic.oup.com/tas/article-abstract/1/3/311/4636631 by Ed 'DeepDyve' Gillespie user on 10 April 2018 314 Reiners et al. to quantify neutral detergent fiber and acid detergent fiber amino acids and the square correlation coefficients (R ) non-sequentially; diet neutral detergent fiber was mea - were 0.9983 for aspartic acid, 0.9977 for glutamic acid, sured in the presence of sodium sulfite and with addition 0.9996 for serine, 0.9991 for histidine, 0.9989 for gly- of ɑ-amylase. Diet samples were analyzed for ether ex- cine, 0.9996 for threonine, 0.9993 for arginine, 0.9991 tract (procedure AM 5–04; AOCS, 2005; Ankom XT10; for alanine, 0.9981 for tyrosine, 0.9963 for valine, 0.9964 Ankom Technology). Nitrogen content of diet samples for methionine, 0.9966 for phenylalanine, 0.9949 for iso- were determined by combustion (method 968.06; AOAC leucine and 0.9963 for lysine. International, 2012; Elementar Rapid MAX N exceed; Calculations. Slopes for each treatment were cal- Elementar, Langenselbold, Germany), and crude protein culated by regressing plasma lysine against amounts was calculated as 6.25 × N. Amino acid concentration of lysine provided in feed or abomasally infused. of diet samples was analyzed by high performance liq- Subsequently, lysine bioavailability was calculated as the uid chromatography (method number 982.30; AOAC ratio of the slopes of EB, EC or lysine-HCl to that of ab- International, 2006). Prior to measures of methionine omasal lysine infusion (Roach et al., 1967; Finney, 1978; and cysteine in diet, the sulfur containing amino acid Batterham et al., 1979; Elwakeel et al., 2012). were oxidized with performic acid, and tryptophan was Statistical Analyses. Plasma lysine was regressed on determined from diet samples after alkaline hydrolysis amounts of lysine added from EB, EC, lysine-HCl, or ab- (method number 982.30; AOAC International, 2006). omasal infusion using the MIXED procedures of SAS ( Plasma lysine content was analyzed for free lysine SAS Inst. Inc., Cary, NC); sheep and period were random by reversed phase ultra-high performance liquid chro- class variables, and amounts of lysine within source of matography after pre-column derivatization of amino supplemental lysine were regression variables. Plasma acids with o-phthaldialdehyde (Dai et al., 2014). Prior amino acid concentration was analyzed as a Latin square to chromatography, 2 mL of plasma was mixed with 2 using the MIXED procedure of SAS; the model included mL of 10% sulfosalicylic acid containing 1 mM norva- effects of treatment and effects of animal and period were line as an internal standard for amino acid analysis. After considered random. Denominator degrees of freedom cooling on ice for 30 min., samples were vortexed and were calculated by the Kenward and Roger adjustment centrifuged (13,800 × g). The supernatant was analyzed (Kenward and Roger, 1997). Effects of added lysine to and chromatography was achieved on a C column (3.0 feed from EB, EC, lysine-HCl or abomasal infusion were × 150 mm, 3.5 µm; Agilent Corp, Santa Clara, CA) af- determined by linear contrasts. ter passing a C guard column (2.1 × 12.5 mm, 5 µm). The combined flow rate of the mobile phase was con - RESULTS AND DISCUSSION stant and 0.64 mL/min. The initial mobile phase (A) was composed of water containing 9.87 µmol/L Na HPO , 2 4 Experiment 1 18.89 µmol/L Na B O , and 0.49 µmol/L NaN . The 2 4 7 3 second mobile phase (B) was composed of water con- Block and Jenkins (1994) observed large amounts taining 8.58 mol/L acetonitrile and 11.11 mol/L metha- of lysine loss from lipid-associated lysine during rumi- nol. The percentage of mobile phase A was as follows: 0 nal incubation. These authors (Block and Jenkins, 1994) min, 98%; 20 min, 43%; 20.1 min, 0%; 23.6 min, 98%. speculated that lysine associated with the surface of the The column was maintained at 40°C and injection vol- lysine-lipid particle was rapidly solubilized during rumi- umes were 16 μL. Amounts of plasma lysine were quan- nal incubation and that diminished surface integrity of tified in reference to norvaline and measured at 338 nm the lysine-lipid particle allowed movement of ruminal (bandwidth = 10 nm) and the reference wavelength was fluid throughout the lysine-lipid particle. Reduced in - 390 nm (bandwidth = 20 nm) with a diode array detector tegrity of the lipid-lysine particle may also allow move- (Ultimate 3000; Thermo Electron North America, West ment of water throughout the lysine-lipid particle when Palm Beach, FL). Prior to analyses of plasma amino mixed with diets that contain large amounts of moisture acids, replicate amino acid standards at 15, 30 and 60 and increase lysine lost from lipid-coated lysine. Ji et al. μmol/L were analyzed to evaluate precision of analy- (2016) reported that increased exposure to a silage-based sis. The intra-assay coefficients of variation were 1.7 ± diet increased amount of lysine loss from lipid-coated 0.46 for aspartic acid, 1.5 ± 0.41 for glutamic acid, 1.2 lysine products. Further, we (Reiners and Brake, 2016) ± 0.44 for serine, 1.2 ± 0.11 for histidine, 1.6 ± 0.42 for previously reported that amounts of lysine lost from lip- glycine, 1.3 ± 0.42 for threonine, 1.6 ± 0.42 for arginine, id-associated lysine affected by silage type, acidity, and 1.8 ± 0.26 for alanine, 1.7 ± 0.26 for tyrosine, 2.4 ± 0.15 manufacture; however, we are not aware of any effort to for valine, 2.1 ± 0.04 for methionine, 2.1 ± 0.19 for phe- image lipid-associated lysine surface structure after mix- nylalanine, 2.0 ± 0.25 for isoleucine and 2.6 ± 0.19 for ing lipid-associated lysine with alfalfa or corn silage con- lysine. Additionally, the area response was linear for all taining different amounts of acidity. Translate basic science to industry innovation Downloaded from https://academic.oup.com/tas/article-abstract/1/3/311/4636631 by Ed 'DeepDyve' Gillespie user on 10 April 2018 Bioavailability of lipid-coated lysine 315 Figure 1. Scanning electron microscropy of lipid-coated lysine after 24 h incubation in alfalfa silage. Panel A: Scanning electron micrograph of EB (lipid-coated lysine that contained 47.5% lysine-HCl and 52.5% lipid) after incubation in low pH alfalfa silage. Panel B: Scanning electron micrograph of EC (lipid-coated lysine that contained 65% lysine-HCl and 35% lipid) incubated in low pH alfalfa silage. Panel C: Scanning electron micrograph of EB incubated in neutral pH alfalfa silage. Panel D: Scanning electron micrograph of EC incubated in neutral pH alfalfa silage. Surface structures of lipid-coated lysine appeared to crographs seemed to indicate that the surface structure of be impacted by mixing it with alfalfa- (Fig. 1) or corn lipid-associated lysine mixed with alfalfa silage was de- silage (Fig. 2) in comparison coated lysine that was not graded equally despite differences in silage pH; however, mixed with silage (Fig. 3). Evaluation of scanning elec- the surface structure of lipid-associated lysine mixed with tron micrographs of lipid-coated lysine not exposed to corn silage appeared to be more disrupted when mixed silage, rinsing, freezing and lyophilizing compared to lip- with more acidic corn silage in comparison to less acidic id-coated lysine that was rinsed, frozen and lyophilized corn silage. Indeed, these surface structure images ap- but not exposed to silage indicate that rinsing, freezing pear to be in agreement with our previous observation and lyophilizing had little impact on lipid-coated lysine (Reiners and Brake, 2016) that greater acidity increased surface structures. Additionally, scanning electron mi- amounts of lysine lost from lipid-associated lysine mixed Figure 2. Scanning electron microscopy of lipid-coated lysine after 24 h incubation in corn silage. Panel A: Scanning electron micrograph of EB (lipid-coated lysine that contained 47.5% lysine-HCl and 52.5% lipid) incubated in low pH corn silage. Panel B: Scanning electron micrograph of EC (lipid- coated lysine that contained 65% lysine-HCl and 35% lipid) incubated in low pH corn silage. Panel C: Scanning electron micrograph of EB incubated in neutral pH corn silage. Panel D: Scanning electron micrograph of EC incubated in neutral pH corn silage Translate basic science to industry innovation Downloaded from https://academic.oup.com/tas/article-abstract/1/3/311/4636631 by Ed 'DeepDyve' Gillespie user on 10 April 2018 316 Reiners et al. Figure 3. Scanning electron microscopy of lipid-coated lysine products prior to incubation in silages. Panel A: Scanning electron micrograph of EB (lipid-coated lysine that contained 47.5% lysine-HCl and 52.5% lipid). Panel B: Scanning electron micrograph of EC (lipid-coated lysine that contained 65% lysine-HCl and 35% lipid). Panel C: Scanning electron micrograph of EB not exposed to silage but after rinsing with water, freezing and lyophilizing. Panel D: Scanning electron micrograph of EC not exposed to silage but after rinsing with water, freezing and lyophilizing. with corn silage but that acidity had little impact on omasum. Our data indicate that bioavailability of lysine amount of lysine lost from lipid-associated lysine mixed from EC, EB, and lysine-HCl in feed was 23, 15, and with alfalfa silage. Obviously, surface structure images 18%, respectively. Even though each source of lysine are subjective measures, but these images appear to agree provided a positive rate of increase among plasma ly- with the report of Ji et al. (2016), our previous observa- sine sources, rates of increase in plasma lysine from EB tions (Reiners and Brake, 2016) and the conclusions of (linear; P = 0.20) and lysine-HCl (linear; P = 0.11) were Block and Jenkins (1994). Regardless, images from this not different from plasma lysine levels supported by preliminary study clearly indicate that measures of lysine diet alone. However, the rate of plasma lysine increase bioavailability are necessary to allow an improved un- in response to lysine from EC was greater (linear; P = derstanding of amounts of metabolizable lysine provided 0.04) than plasma lysine from feed alone. Yet, the rate from lipid-coated lysine after exposure to silage. of plasma lysine increase in response to lipid-coated ly- sine did not differ ( P ≥ 0.70) from the rate of plasma lysine increase from lysine-HCl. Experiment 2 Effects of feeding lipid-coated lysine on plasma ly - Rulquin and Kowalczyk (2003) reported that ab- sine concentration and lactation performance among lac- omasal infusion of graded amounts of lysine to lac- tating cows fed silage-based diets are variable. Several tating cows and subsequent measurement of plasma authors (Robinson et al., 2011; Giallongo et al., 2016) lysine is more effective than in vitro procedures to reported increases in plasma lysine and milk protein determine amounts of metabolizable lysine from lip- content when lactating cows were supplemented with id-coated lysine. We used 9 mature ewes fitted with lipid-coated lysine. Conversely, others (Swanepoel et al., abomasal catheters and fed diets designed to not be 2010; Robinson et al., 2010; Lee et al., 2012, 2015) re- limiting in lysine to evaluate amounts of metaboliz- ported no effect of lipid-coated lysine on plasma lysine able lysine provided from lipid-coated lysine or ly- and milk protein concentration. Authors have speculated sine-HCl after mixing with corn silage. (Robinson et al., 2010; Swanepoel et al., 2010) that a lack Plasma lysine concentrations (Fig. 4) increased lin- of response among plasma lysine or milk protein may early (P < 0.01) in response to abomasal infusion of ly- have been related to changes in partitioning of amino sine indicating that our model was sensitive to increases acids for physiological functions other than milk pro- in metabolizable lysine flow. Bioavailability of EC, EB, tein production or because diets were not first-limited by and lysine-HCl in feed was calculated as the ratio of metabolizable lysine. However, Wu et al. (2012) calcu- the rate of plasma lysine increase from EC, EB, or ly- lated that only 11.5% of lysine from lipid-coated lysine sine-HCl in feed to the rate of plasma lysine increase in was digested in the small intestine of cows when they response to known amounts of lysine infused to the ab- measured lysine loss from lipid-coated lysine in mobile Translate basic science to industry innovation Downloaded from https://academic.oup.com/tas/article-abstract/1/3/311/4636631 by Ed 'DeepDyve' Gillespie user on 10 April 2018 Bioavailability of lipid-coated lysine 317 Figure 4. Plasma lysine concentration in ewes provided lysine as an abomasal infusion of lysine-HCL or as dietary lysine-HCl (Panel A), EB (Panel B; lipid-coated lysine that contained 47.5% lysine-HCl and 52.5% lipid), or EC (Panel C; lipid-coated lysine that contained 65% lysine-HCl and 35% lipid). Standard error of estimate = 1.3. Translate basic science to industry innovation Downloaded from https://academic.oup.com/tas/article-abstract/1/3/311/4636631 by Ed 'DeepDyve' Gillespie user on 10 April 2018 318 Reiners et al. Table 2. Effect of 0, 5 or 10 g/d lysine from abomasal infusion or from lysine-HCl and 2 lipid-coated lysine prod - ucts added to a corn silage-based diet on plasma amino acid concentrations (µmol/L) in sheep 2 3 Control Infused Lysine-HCl EB EC Linear contrasts AA None 5 10 5 10 5 10 5 10 SEM Infused Lysine-HCl EB EC Glu 28.8 25.3 26.0 29.5 27.7 22.3 24.1 30.6 23.5 3.9 0.35 0.71 0.11 0.07 Asp 20.5 16.0 17.0 19.4 17.8 18.3 19.9 17.9 17.1 1.8 0.06 0.14 0.75 0.07 Ser 21.1 18.3 21.0 19.9 18.4 18.8 20.6 23.0 17.6 1.5 0.94 0.12 0.78 0.04 Gln 252.3 232.8 250.0 257.7 226.7 228.6 264.0 263.0 232.7 16.2 0.88 0.11 0.46 0.22 His 49.4 46.6 45.2 47.7 45.6 47.6 48.0 50.1 48.3 3.7 0.23 0.27 0.68 0.75 Gly 123.9 109.1 110.3 110.6 109.5 114.0 128.2 119.9 107.6 9.0 0.09 0.07 0.58 0.04 Thr 32.8 26.0 25.3 25.4 31.8 28.4 28.3 30.9 25.1 3.9 0.08 0.82 0.29 0.08 Arg 66.6 66.4 78.5 64.9 61.0 63.0 68.3 64.9 64.9 5.8 0.06 0.38 0.80 0.79 Ala 45.9 44.9 47.2 46.0 40.8 42.4 43.6 45.9 41.0 3.1 0.72 0.14 0.51 0.15 Tyr 26.1 21.3 20.3 24.6 24.8 24.5 23.0 24.4 20.9 2.1 <0.01 0.47 0.10 0.01 Val 40.3 42.9 43.3 42.3 40.9 41.6 42.8 41.8 38.6 4.7 0.52 0.90 0.59 0.72 Phe 17.9 16.3 14.6 17.4 16.9 17.0 15.9 16.5 15.5 1.5 0.01 0.42 0.12 0.07 Ile 22.3 21.3 21.8 21.7 19.8 20.4 21.0 19.6 19.4 2.5 0.82 0.30 0.60 0.23 Leu 28.3 27.3 27.1 27.5 24.9 26.7 28.0 26.9 21.3 3.0 0.67 0.19 0.91 0.01 Lys 39.5 81.1 158.8 48.2 53.7 39.9 52.3 46.5 62.0 11.3 <0.01 0.36 0.41 0.15 Amino acids are described by standard 3 letter abbreviations. Lipid coated lysine that contained 47.5% lysine-HCl and 52.5% lipid. Lipid coated lysine that contained 65% lysine-HCl and 35% lipid. bags, and Paz and Kononoff (2014) speculated that a of lysine apparently available to be digested in the small lack of response in arterial lysine concentration among intestine of cows (Wu et al., 2012). cows fed lipid-coated lysine was because lipid-coated Plasma amino acid concentrations are reported in lysine provided less metabolizable lysine than expected. Table 2. The only amino acids affected by treatment other Regardless of the reason for a lack of response to lipid- than lysine were modest changes in serine, tyrosine, phe- coated lysine, it cannot be discounted that one explana- nylalanine, leucine, and glycine. Specifically, increased in - tion to a lack of performance response to lipid-coated take of EC and greater abomasal infusion of lysine reduced lysine may be that amounts of metabolizable lysine from (linear; P ≤ 0.01) plasma tyrosine. Greater amounts of ly - lipid-coated lysine were less than anticipated. sine from EC decreased (linear; P = 0.03) plasma serine, Rulquin and Kowalczyk (2003) concluded that use leucine, and glycine. Additionally abomasal infusion of of lipid-coated lysine may be useful to evaluate bio- lysine decreased (linear; P = 0.01) plasma phenylalanine. availability of amino acids from feed. However, our A specific explanation for slight changes in circulating data together with others (Ji et al., 2016) emphasize concentrations of serine, tyrosine, phenylalanine, leucine, caution when using lipid-coated lysine as a positive and glycine remains unknown. Evidently, increases in control in determining estimates of lysine bioavailabil- both metabolizable lysine and ruminally degraded lysine ity, and that lipid-coated lysine should only be used as can impact circulating amino acid concentrations. a positive control after effects of physical and chemi - cal characteristics of diet on availability of lysine from Conclusions lipid-coated lysine has been validated. Generally, slope ratio analyses represent direct mea- Our data indicate that lipid-coated lysine can sures of an amino acid’s availability to non-splanchnic provide metabolizable lysine to ruminants, but that tissues (McNab, 1994; Moehn et al., 2005). Thus, it is amounts of metabolizable lysine from lipid-coated surprising that only a limited number of reports are avail- lysine are affected by both physical and chemical able that have measured amino acid availability from characteristics of diet. More direct measurements of “ruminally-protected” amino acid products to ruminants. lysine availability to ruminants are needed to improve Our data indicate that relatively modest amounts of me- estimates of metabolizable lysine from lipid-coated tabolizable lysine were available to sheep from lipid- lysine products in various feeding conditions, and it is coated lysine mixed with corn silage. It is possible that possible that variation in production responses to lip- measures of metabolizable lysine from lipid-coated ly- id-coated lysine are related to inaccurate estimates of sine could differ between ruminant species; however, our amounts of metabolizable lysine provided from lipid- measures of lysine bioavailability are similar to amounts coated lysine. 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Dairy Sci. doi:10.3168/jds.S0022-0302(98)75668-1 98:1885–1902. doi:10.3168/jds.2014-8496 Translate basic science to industry innovation Downloaded from https://academic.oup.com/tas/article-abstract/1/3/311/4636631 by Ed 'DeepDyve' Gillespie user on 10 April 2018

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Translational Animal ScienceOxford University Press

Published: Sep 1, 2017

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