title: Characterization and production of multifunctional cationic peptides derived from rice proteins.
abstract: 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.
authors.affiliation: a Department of Materials Science and Technology, Graduate School of Science and Technology , Niigata University , Niigata , Japan.|b Center for Transdisciplinary Research , Niigata University , Niigata , Japan.
authors.forename: Masayuki
authors.initials: M
authors.lastname: Taniguchi
authors.affiliation: a Department of Materials Science and Technology, Graduate School of Science and Technology , Niigata University , Niigata , Japan.
authors.forename: Akihito
authors.initials: A
authors.lastname: Ochiai
mesh_terms: D000890:Anti-Infective Agents / Q000737:chemistry* / Q000627:therapeutic use; D023181:Antimicrobial Cationic Peptides / Q000737:chemistry* / Q000627:therapeutic use; D001120:Arginine / Q000737:chemistry; D005285:Fermentation; D005511:Food Handling; D006801:Humans; D006868:Hydrolysis; D007525:Isoelectric Focusing; D008894:Milk Proteins / Q000737:chemistry; D012275:Oryza / Q000737:chemistry; D010940:Plant Proteins / Q000737:chemistry*
chemical_list: D000890:Anti-Infective Agents; D023181:Antimicrobial Cationic Peptides; D008894:Milk Proteins; D010940:Plant Proteins; D001120:Arginine
keywords: angiogenic peptide; antimicrobial peptide; endotoxin-neutralizing peptide; multifunctional cationic peptide; peptides from rice enzymes and proteins