Identification and characterization of multifunctional cationic peptides derived from peptic hydrolysates of rice bran protein

In this study, to prepare the fraction containing multifunctional cationic peptides, we first hydrolyzed rice bran protein (RBP) with pepsin. We separated the enzymatic hydrolysate of RBP into 20 fractions containing peptides with different isoelectric point (pI) values by ampholyte-free isoelectric...

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Main Authors: Masayuki Taniguchi, Mitsuhiro Kameda, Toshiki Namae, Akihito Ochiai, Eiichi Saitoh, Takaaki Tanaka
Format: Article
Language:English
Published: Elsevier 2017-07-01
Series:Journal of Functional Foods
Subjects:
Online Access:http://www.sciencedirect.com/science/article/pii/S1756464617302438
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author Masayuki Taniguchi
Mitsuhiro Kameda
Toshiki Namae
Akihito Ochiai
Eiichi Saitoh
Takaaki Tanaka
author_facet Masayuki Taniguchi
Mitsuhiro Kameda
Toshiki Namae
Akihito Ochiai
Eiichi Saitoh
Takaaki Tanaka
author_sort Masayuki Taniguchi
collection DOAJ
description In this study, to prepare the fraction containing multifunctional cationic peptides, we first hydrolyzed rice bran protein (RBP) with pepsin. We separated the enzymatic hydrolysate of RBP into 20 fractions containing peptides with different isoelectric point (pI) values by ampholyte-free isoelectric focusing (autofocusing). Subsequently, we examined the antimicrobial activity of each fraction against four pathogens. In addition, we purified the cationic peptides from fractions exhibiting antimicrobial activity by reversed-phase high-performance liquid chromatography and identified them by matrix-assisted laser/desorption ionization–time-of-flight mass spectroscopy. Of five cationic peptides identified, we chemically synthesized three peptides with high pI values and evaluated their multiple functions, including antimicrobial, lipopolysaccharide-neutralizing and angiogenic activities. Our results demonstrated that the three identified cationic peptides exhibited multiple functions with little or no haemolytic activity. Fractions containing cationic peptides obtained from RBP hydrolysate have the potential to be used as dietary supplements and functional ingredients in food products.
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spelling doaj.art-145658539db547179d5c435212306f442022-12-21T19:07:44ZengElsevierJournal of Functional Foods1756-46462017-07-0134287296Identification and characterization of multifunctional cationic peptides derived from peptic hydrolysates of rice bran proteinMasayuki Taniguchi0Mitsuhiro Kameda1Toshiki Namae2Akihito Ochiai3Eiichi Saitoh4Takaaki Tanaka5Department of Materials Science and Technology, Graduate School of Science and Technology, Niigata University, Niigata 950-2181, Japan; Center for Transdisciplinary Research, Niigata University, Niigata 950-2181, Japan; Corresponding author at: Department of Materials Science and Technology, Graduate School of Science and Technology, Niigata University, Niigata 950-2181, Japan.Department of Materials Science and Technology, Graduate School of Science and Technology, Niigata University, Niigata 950-2181, JapanCenter for Transdisciplinary Research, Niigata University, Niigata 950-2181, JapanCenter for Transdisciplinary Research, Niigata University, Niigata 950-2181, JapanGraduate School of Technology, Niigata Institute of Technology, Niigata 945-1195, JapanDepartment of Materials Science and Technology, Graduate School of Science and Technology, Niigata University, Niigata 950-2181, JapanIn this study, to prepare the fraction containing multifunctional cationic peptides, we first hydrolyzed rice bran protein (RBP) with pepsin. We separated the enzymatic hydrolysate of RBP into 20 fractions containing peptides with different isoelectric point (pI) values by ampholyte-free isoelectric focusing (autofocusing). Subsequently, we examined the antimicrobial activity of each fraction against four pathogens. In addition, we purified the cationic peptides from fractions exhibiting antimicrobial activity by reversed-phase high-performance liquid chromatography and identified them by matrix-assisted laser/desorption ionization–time-of-flight mass spectroscopy. Of five cationic peptides identified, we chemically synthesized three peptides with high pI values and evaluated their multiple functions, including antimicrobial, lipopolysaccharide-neutralizing and angiogenic activities. Our results demonstrated that the three identified cationic peptides exhibited multiple functions with little or no haemolytic activity. Fractions containing cationic peptides obtained from RBP hydrolysate have the potential to be used as dietary supplements and functional ingredients in food products.http://www.sciencedirect.com/science/article/pii/S1756464617302438Hydrolysates of rice bran proteinsMulti-functional cationic peptidesAntimicrobial peptidesLPS-binding peptidesAngiogenic peptides
spellingShingle Masayuki Taniguchi
Mitsuhiro Kameda
Toshiki Namae
Akihito Ochiai
Eiichi Saitoh
Takaaki Tanaka
Identification and characterization of multifunctional cationic peptides derived from peptic hydrolysates of rice bran protein
Journal of Functional Foods
Hydrolysates of rice bran proteins
Multi-functional cationic peptides
Antimicrobial peptides
LPS-binding peptides
Angiogenic peptides
title Identification and characterization of multifunctional cationic peptides derived from peptic hydrolysates of rice bran protein
title_full Identification and characterization of multifunctional cationic peptides derived from peptic hydrolysates of rice bran protein
title_fullStr Identification and characterization of multifunctional cationic peptides derived from peptic hydrolysates of rice bran protein
title_full_unstemmed Identification and characterization of multifunctional cationic peptides derived from peptic hydrolysates of rice bran protein
title_short Identification and characterization of multifunctional cationic peptides derived from peptic hydrolysates of rice bran protein
title_sort identification and characterization of multifunctional cationic peptides derived from peptic hydrolysates of rice bran protein
topic Hydrolysates of rice bran proteins
Multi-functional cationic peptides
Antimicrobial peptides
LPS-binding peptides
Angiogenic peptides
url http://www.sciencedirect.com/science/article/pii/S1756464617302438
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