Comparison of physicochemical properties, antioxidant and metal-chelating activities of protein hydrolysates from Phaseolus lunatus and hard-to-cook Phaseolus vulgaris

Beatriz Guzmán-Méndez, Maria Eugenia Jaramillo-Flores, Luis Chel-Guerrero, David Betancur-Ancona

Research output: Contribution to journalArticle

11 Citations (Scopus)

Abstract

Summary: Limited and extensive hydrolysates were obtained from Phaseolus lunatus (LHl and EHl) and hard-to-cook Phaseolus vulgaris (LHv and EHv) using the enzymes Flavourzyme®, Alcalase®, Pancreatin® and a sequential Pepsin®-Pancreatin® system. Degrees of hydrolysis varied from 8.32% to 31.60%. SDS-PAGE of extensive hydrolysates showed molecular weights smaller than limited hydrolysates. Differential scanning calorimeter (DSC) analysis of LHl and EHl revealed the presence of two endothermic transitions; LHv and EHv had only one. LHv presented a higher content of hydrophobic amino acids whose surface hydrophobicity was 12.17. Functional properties such as nitrogen solubility, foaming capacity and emulsifying activity index in LHv were better than LHl at different pH evaluated. However, the latter showed better foaming stabilities. Amino acids such as His, Tyr, Trp and Arg were observed in greater amounts in both extensive hydrolysates. 1,1-diphenyl-2-picrylhydrazyl (DPPH) radical-scavenging and metal-chelating activities in EHv and EHl increased significantly compared to the source material. © 2014 Institute of Food Science and Technology.
Original languageAmerican English
Pages (from-to)1859-1868
Number of pages1672
JournalInternational Journal of Food Science and Technology
DOIs
StatePublished - 1 Jan 2014

Fingerprint

Pancreatin
Phaseolus lunatus
Protein Hydrolysates
Food Technology
Phaseolus
protein hydrolysates
Chelation
Antioxidants
hydrolysates
Phaseolus vulgaris
Amino acids
physicochemical properties
Metals
metals
Subtilisins
Proteins
antioxidants
Amino Acids
pancreatin
Pepsin A

Cite this

@article{80ac323c11034ab99680e73ec846db8d,
title = "Comparison of physicochemical properties, antioxidant and metal-chelating activities of protein hydrolysates from Phaseolus lunatus and hard-to-cook Phaseolus vulgaris",
abstract = "Summary: Limited and extensive hydrolysates were obtained from Phaseolus lunatus (LHl and EHl) and hard-to-cook Phaseolus vulgaris (LHv and EHv) using the enzymes Flavourzyme{\circledR}, Alcalase{\circledR}, Pancreatin{\circledR} and a sequential Pepsin{\circledR}-Pancreatin{\circledR} system. Degrees of hydrolysis varied from 8.32{\%} to 31.60{\%}. SDS-PAGE of extensive hydrolysates showed molecular weights smaller than limited hydrolysates. Differential scanning calorimeter (DSC) analysis of LHl and EHl revealed the presence of two endothermic transitions; LHv and EHv had only one. LHv presented a higher content of hydrophobic amino acids whose surface hydrophobicity was 12.17. Functional properties such as nitrogen solubility, foaming capacity and emulsifying activity index in LHv were better than LHl at different pH evaluated. However, the latter showed better foaming stabilities. Amino acids such as His, Tyr, Trp and Arg were observed in greater amounts in both extensive hydrolysates. 1,1-diphenyl-2-picrylhydrazyl (DPPH) radical-scavenging and metal-chelating activities in EHv and EHl increased significantly compared to the source material. {\circledC} 2014 Institute of Food Science and Technology.",
author = "Beatriz Guzm{\'a}n-M{\'e}ndez and Jaramillo-Flores, {Maria Eugenia} and Luis Chel-Guerrero and David Betancur-Ancona",
year = "2014",
month = "1",
day = "1",
doi = "10.1111/ijfs.12495",
language = "American English",
pages = "1859--1868",
journal = "International Journal of Food Science and Technology",
issn = "0950-5423",
publisher = "Wiley-Blackwell Publishing Ltd",

}

TY - JOUR

T1 - Comparison of physicochemical properties, antioxidant and metal-chelating activities of protein hydrolysates from Phaseolus lunatus and hard-to-cook Phaseolus vulgaris

AU - Guzmán-Méndez, Beatriz

AU - Jaramillo-Flores, Maria Eugenia

AU - Chel-Guerrero, Luis

AU - Betancur-Ancona, David

PY - 2014/1/1

Y1 - 2014/1/1

N2 - Summary: Limited and extensive hydrolysates were obtained from Phaseolus lunatus (LHl and EHl) and hard-to-cook Phaseolus vulgaris (LHv and EHv) using the enzymes Flavourzyme®, Alcalase®, Pancreatin® and a sequential Pepsin®-Pancreatin® system. Degrees of hydrolysis varied from 8.32% to 31.60%. SDS-PAGE of extensive hydrolysates showed molecular weights smaller than limited hydrolysates. Differential scanning calorimeter (DSC) analysis of LHl and EHl revealed the presence of two endothermic transitions; LHv and EHv had only one. LHv presented a higher content of hydrophobic amino acids whose surface hydrophobicity was 12.17. Functional properties such as nitrogen solubility, foaming capacity and emulsifying activity index in LHv were better than LHl at different pH evaluated. However, the latter showed better foaming stabilities. Amino acids such as His, Tyr, Trp and Arg were observed in greater amounts in both extensive hydrolysates. 1,1-diphenyl-2-picrylhydrazyl (DPPH) radical-scavenging and metal-chelating activities in EHv and EHl increased significantly compared to the source material. © 2014 Institute of Food Science and Technology.

AB - Summary: Limited and extensive hydrolysates were obtained from Phaseolus lunatus (LHl and EHl) and hard-to-cook Phaseolus vulgaris (LHv and EHv) using the enzymes Flavourzyme®, Alcalase®, Pancreatin® and a sequential Pepsin®-Pancreatin® system. Degrees of hydrolysis varied from 8.32% to 31.60%. SDS-PAGE of extensive hydrolysates showed molecular weights smaller than limited hydrolysates. Differential scanning calorimeter (DSC) analysis of LHl and EHl revealed the presence of two endothermic transitions; LHv and EHv had only one. LHv presented a higher content of hydrophobic amino acids whose surface hydrophobicity was 12.17. Functional properties such as nitrogen solubility, foaming capacity and emulsifying activity index in LHv were better than LHl at different pH evaluated. However, the latter showed better foaming stabilities. Amino acids such as His, Tyr, Trp and Arg were observed in greater amounts in both extensive hydrolysates. 1,1-diphenyl-2-picrylhydrazyl (DPPH) radical-scavenging and metal-chelating activities in EHv and EHl increased significantly compared to the source material. © 2014 Institute of Food Science and Technology.

UR - https://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=84904381779&origin=inward

UR - https://www.scopus.com/inward/citedby.uri?partnerID=HzOxMe3b&scp=84904381779&origin=inward

U2 - 10.1111/ijfs.12495

DO - 10.1111/ijfs.12495

M3 - Article

SP - 1859

EP - 1868

JO - International Journal of Food Science and Technology

JF - International Journal of Food Science and Technology

SN - 0950-5423

ER -