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Bioactive proteins and peptides from food sources. Applications of bioprocesses used in isolation and recovery.

Bioactive proteins and peptides from food sources. Applications of bioprocesses used in isolation... There are many examples of biologically active food proteins, with physiological significance beyond the pure nutritional requirements that concern available nitrogen for normal growth and maintenance. Moreover, there are many physiologically active peptides, derived by protease activity from various food protein sources; however, relationships between structural properties and functional activities have not been completely elucidated. Many bioactive peptides have in common structural properties that include a relatively short peptide residue length (e.g. 2-9 amino acids), possessing hydrophobic amino acid residues in addition to proline, lysine or arginine groups. Bioactive peptides are also resistant to the action of digestion peptidases. Antihypertensive peptides, known as Angiotensin I converting enzyme (ACE) inhibitors have been derived from milk, corn and fish protein sources. Peptides with opioid activities are derived from wheat gluten or casein, following digestion with pepsin. Exorphins, or opioid peptides derived from food proteins such as wheat and milk (e.g. exogenous sources) have similar structure to endogenous opioid peptides, with a tyrosine residue located at the amino terminal or bioactive site. Immunomodulatory peptides derived from tryptic hydrolysates of rice and soybean proteins act to stimulate superoxide anions (reactive oxygen species-ROS), which triggers non-specific immune defense systems. Antioxidant properties that prevent peroxidation of essential fatty acids have also been shown for peptides derived from milk proteins. The addition of a Leu or Pro residue to the N-terminus of a His-His, dipeptide will enhance antioxidant activity and facilitate further synergy with non-peptide antioxidants (e.g. BHT). We also show herein, that the tryptic digests of casein yielding caseinophosphopeptides exhibits both hydrophilic and lipophilic antioxidant activity due to both metal ion sequestering and quenching of ROS. The separation and purification of bioactive peptides which will involve development of automated and continuous systems is an important field for Food chemists. Much effort has been given to develop selective column chromatography methods that can replace batch methods of salting out, or using solvent extraction to isolate and purify bioactive peptides. Advances here will enable recovery of bioactive peptides with minimal destruction thus enabling utilization by returning these active peptides to functional food or specific nutraceutical applications. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Current pharmaceutical design Pubmed

Bioactive proteins and peptides from food sources. Applications of bioprocesses used in isolation and recovery.

Current pharmaceutical design , Volume 9 (16): -1285 – Aug 5, 2003

Bioactive proteins and peptides from food sources. Applications of bioprocesses used in isolation and recovery.


Abstract

There are many examples of biologically active food proteins, with physiological significance beyond the pure nutritional requirements that concern available nitrogen for normal growth and maintenance. Moreover, there are many physiologically active peptides, derived by protease activity from various food protein sources; however, relationships between structural properties and functional activities have not been completely elucidated. Many bioactive peptides have in common structural properties that include a relatively short peptide residue length (e.g. 2-9 amino acids), possessing hydrophobic amino acid residues in addition to proline, lysine or arginine groups. Bioactive peptides are also resistant to the action of digestion peptidases. Antihypertensive peptides, known as Angiotensin I converting enzyme (ACE) inhibitors have been derived from milk, corn and fish protein sources. Peptides with opioid activities are derived from wheat gluten or casein, following digestion with pepsin. Exorphins, or opioid peptides derived from food proteins such as wheat and milk (e.g. exogenous sources) have similar structure to endogenous opioid peptides, with a tyrosine residue located at the amino terminal or bioactive site. Immunomodulatory peptides derived from tryptic hydrolysates of rice and soybean proteins act to stimulate superoxide anions (reactive oxygen species-ROS), which triggers non-specific immune defense systems. Antioxidant properties that prevent peroxidation of essential fatty acids have also been shown for peptides derived from milk proteins. The addition of a Leu or Pro residue to the N-terminus of a His-His, dipeptide will enhance antioxidant activity and facilitate further synergy with non-peptide antioxidants (e.g. BHT). We also show herein, that the tryptic digests of casein yielding caseinophosphopeptides exhibits both hydrophilic and lipophilic antioxidant activity due to both metal ion sequestering and quenching of ROS. The separation and purification of bioactive peptides which will involve development of automated and continuous systems is an important field for Food chemists. Much effort has been given to develop selective column chromatography methods that can replace batch methods of salting out, or using solvent extraction to isolate and purify bioactive peptides. Advances here will enable recovery of bioactive peptides with minimal destruction thus enabling utilization by returning these active peptides to functional food or specific nutraceutical applications.

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ISSN
1381-6128
DOI
10.2174/1381612033454883
pmid
12769739

Abstract

There are many examples of biologically active food proteins, with physiological significance beyond the pure nutritional requirements that concern available nitrogen for normal growth and maintenance. Moreover, there are many physiologically active peptides, derived by protease activity from various food protein sources; however, relationships between structural properties and functional activities have not been completely elucidated. Many bioactive peptides have in common structural properties that include a relatively short peptide residue length (e.g. 2-9 amino acids), possessing hydrophobic amino acid residues in addition to proline, lysine or arginine groups. Bioactive peptides are also resistant to the action of digestion peptidases. Antihypertensive peptides, known as Angiotensin I converting enzyme (ACE) inhibitors have been derived from milk, corn and fish protein sources. Peptides with opioid activities are derived from wheat gluten or casein, following digestion with pepsin. Exorphins, or opioid peptides derived from food proteins such as wheat and milk (e.g. exogenous sources) have similar structure to endogenous opioid peptides, with a tyrosine residue located at the amino terminal or bioactive site. Immunomodulatory peptides derived from tryptic hydrolysates of rice and soybean proteins act to stimulate superoxide anions (reactive oxygen species-ROS), which triggers non-specific immune defense systems. Antioxidant properties that prevent peroxidation of essential fatty acids have also been shown for peptides derived from milk proteins. The addition of a Leu or Pro residue to the N-terminus of a His-His, dipeptide will enhance antioxidant activity and facilitate further synergy with non-peptide antioxidants (e.g. BHT). We also show herein, that the tryptic digests of casein yielding caseinophosphopeptides exhibits both hydrophilic and lipophilic antioxidant activity due to both metal ion sequestering and quenching of ROS. The separation and purification of bioactive peptides which will involve development of automated and continuous systems is an important field for Food chemists. Much effort has been given to develop selective column chromatography methods that can replace batch methods of salting out, or using solvent extraction to isolate and purify bioactive peptides. Advances here will enable recovery of bioactive peptides with minimal destruction thus enabling utilization by returning these active peptides to functional food or specific nutraceutical applications.

Journal

Current pharmaceutical designPubmed

Published: Aug 5, 2003

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