Characterization and production of multifunctional cationic peptides derived from rice proteins

• Published in: Bioscience, Biotechnology, and Biochemistry Vol. 81; no. 4; pp. 634 - 650
• Main Authors: Taniguchi, Masayuki, Ochiai, Akihito
• Format: Journal Article Book Review
• Language: English
• Published: England Taylor & Francis 01.04.2017; Oxford University Press
• Subjects: angiogenic peptide; Anti-Infective Agents - chemistry; Anti-Infective Agents - therapeutic use; Antimicrobial Cationic Peptides - chemistry; Antimicrobial Cationic Peptides - therapeutic use; antimicrobial peptide; Arginine - chemistry; endotoxin-neutralizing peptide; Fermentation; Food Handling; Humans; Hydrolysis; Isoelectric Focusing; Milk Proteins - chemistry; multifunctional cationic peptide; Oryza - chemistry; peptides from rice enzymes and proteins; Plant Proteins - chemistry; peptides from rice enzymes and proteins; multifunctional cationic peptide; angiogenic peptide; antimicrobial peptide; endotoxin-neutralizing peptide
• ISSN: 0916-8451; 1347-6947
• DOI: 10.1080/09168451.2016.1277944

Food proteins have been identified as a source of bioactive peptides. These peptides are inactive within the sequence of the parent protein and must be released during gastrointestinal digestion, fermentation, or food processing. Of bioactive peptides, multifunctional cationic peptides are more useful than other peptides that have specific activity in promotion of health and/or the treatment of diseases. We have identified and characterized cationic peptides from rice enzymes and proteins that possess multiple functions, including antimicrobial, endotoxin-neutralizing, arginine gingipain-inhibitory, and/or angiogenic activities. In particular, we have elucidated the contribution of cationic amino acids (arginine and lysine) in the peptides to their bioactivities. Further, we have discussed the critical parameters, particularly proteinase preparations and fractionation or purification, in the enzymatic hydrolysis process for producing bioactive peptides from food proteins. Using an ampholyte-free isoelectric focusing (autofocusing) technique as a tool for fractionation, we successfully prepared fractions containing cationic peptides with multiple functions.