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ACE- inhibitory and radical scavenging activities of bioactive peptides obtained from camel milk casein hydrolysis with proteinase K

ACE- inhibitory and radical scavenging activities of bioactive peptides obtained from camel milk... The aim of this study was to evaluate the effects of enzymatic hydrolysis of camel whole casein on their antioxidant and angiotensin-converting enzyme (ACE)-inhibitory properties. Whole camel casein was hydrolyzed by proteinase K (PK), and the hydrolysates were fractionized by ultrafiltration membranes into three fractions. Semi-preparative reversed-phase high-performance liquid chromatography (RP-HPLC) was used to differentiate the mixture of peptides in the 3 kDa permeate fractions. A fraction (F4) with potentials of ACE-inhibitory activity (IC50 = 73 μg.mL−1) and radical scavenging activity (IC50 = 6.8 μg.mL−1) was selected for further purification and fractionation. The fraction F4C obtained from a second step purification of F4 showed strong ACE-inhibitory activity (IC50 = 36 μg.mL−1) as well as radical scavenging activity (IC50 = 3.3 μg.mL−1). The results of this study suggest that whole camel casein can be considered as a promising source for the production of peptides with potential of ACE-inhibitory and antioxidant activities. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Dairy Science & Technology Springer Journals

ACE- inhibitory and radical scavenging activities of bioactive peptides obtained from camel milk casein hydrolysis with proteinase K

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References (29)

Publisher
Springer Journals
Copyright
Copyright © 2016 by INRA and Springer-Verlag France
Subject
Chemistry; Food Science; Agriculture; Microbiology
ISSN
1958-5586
eISSN
1958-5594
DOI
10.1007/s13594-016-0283-4
Publisher site
See Article on Publisher Site

Abstract

The aim of this study was to evaluate the effects of enzymatic hydrolysis of camel whole casein on their antioxidant and angiotensin-converting enzyme (ACE)-inhibitory properties. Whole camel casein was hydrolyzed by proteinase K (PK), and the hydrolysates were fractionized by ultrafiltration membranes into three fractions. Semi-preparative reversed-phase high-performance liquid chromatography (RP-HPLC) was used to differentiate the mixture of peptides in the 3 kDa permeate fractions. A fraction (F4) with potentials of ACE-inhibitory activity (IC50 = 73 μg.mL−1) and radical scavenging activity (IC50 = 6.8 μg.mL−1) was selected for further purification and fractionation. The fraction F4C obtained from a second step purification of F4 showed strong ACE-inhibitory activity (IC50 = 36 μg.mL−1) as well as radical scavenging activity (IC50 = 3.3 μg.mL−1). The results of this study suggest that whole camel casein can be considered as a promising source for the production of peptides with potential of ACE-inhibitory and antioxidant activities.

Journal

Dairy Science & TechnologySpringer Journals

Published: May 2, 2016

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