TY - JOUR
T1 - Germination of Phaseolus vulgaris and alcalase hydrolysis of its proteins produced bioactive peptides capable of improving markers related to type-2 diabetes in vitro
AU - de Souza Rocha, Thaís
AU - Hernandez, Luis Manuel Real
AU - Mojica, Luis
AU - Johnson, Michelle H.
AU - Chang, Yoon Kil
AU - González de Mejía, Elvira
N1 - Author Thais de Souza Rocha was supported by FAPESP (Sao Paulo, Brazil) 2012/19034-0 . Research was supported by funding from a Hatch grant, University of Illinois . Author L. M. Real Hernandez acknowledges the National Science Foundation (NSF) Mentoring in New Biology Fellowship (# 1041233 ) and the Multicultural Advocates in Nutrition Needs & Agriculture (MANNA) scholarship sponsored by the USDA (# 2011-38413-30107 ).
PY - 2015/10/1
Y1 - 2015/10/1
N2 - The aim of this study was to evaluate the effect of germination and alcalase hydrolysis of common bean proteins on the generation of bioactive peptides with potential to reduce parameters related to the risk of developing type-2 diabetes (T2D) in vitro. Germination (25°C up to 72h) and alcalase hydrolysis (up to 4h) produced peptides with high antioxidant capacity (1085μmolTE/g soluble protein, SP). After 24h of germination, there was an increase of 44% in α-amylase inhibitory capacity of the peptides relative to acarbose (1mM). Simulated gastrointestinal digestion of the non-germinated and non-hydrolyzed sample (G0-0h) produced bioactive peptides that inhibited dipeptidyl peptidase-IV (DPP-IV) (IC50=1.2mgSP/mL); however, the IC50 was not improved by either germination or alcalase hydrolysis. Insulin secretion by glucose stimulated (20mM) INS-1E pancreatic β-cells, increased 45% from the basal state with 2mgSP/mL of G0-0h. Germination did not improve the stimulation of insulin. Computational modeling showed that the peptide RGPLVNPDPKPFL obtained after 48h germination and 1h alcalase-hydrolysis was able to inhibit DPP-IV by interacting with its S1, S2, and S3 pockets of the active site. Germination and alcalase hydrolysis can be applied to improve some markers related to the management of T2D. Furthermore, simulated gastrointestinal digestion of common bean proteins without any treatment produced bioactive peptides with the ability to inhibit DPP-IV, resulting in increased insulin released from pancreatic cells in vitro.
AB - The aim of this study was to evaluate the effect of germination and alcalase hydrolysis of common bean proteins on the generation of bioactive peptides with potential to reduce parameters related to the risk of developing type-2 diabetes (T2D) in vitro. Germination (25°C up to 72h) and alcalase hydrolysis (up to 4h) produced peptides with high antioxidant capacity (1085μmolTE/g soluble protein, SP). After 24h of germination, there was an increase of 44% in α-amylase inhibitory capacity of the peptides relative to acarbose (1mM). Simulated gastrointestinal digestion of the non-germinated and non-hydrolyzed sample (G0-0h) produced bioactive peptides that inhibited dipeptidyl peptidase-IV (DPP-IV) (IC50=1.2mgSP/mL); however, the IC50 was not improved by either germination or alcalase hydrolysis. Insulin secretion by glucose stimulated (20mM) INS-1E pancreatic β-cells, increased 45% from the basal state with 2mgSP/mL of G0-0h. Germination did not improve the stimulation of insulin. Computational modeling showed that the peptide RGPLVNPDPKPFL obtained after 48h germination and 1h alcalase-hydrolysis was able to inhibit DPP-IV by interacting with its S1, S2, and S3 pockets of the active site. Germination and alcalase hydrolysis can be applied to improve some markers related to the management of T2D. Furthermore, simulated gastrointestinal digestion of common bean proteins without any treatment produced bioactive peptides with the ability to inhibit DPP-IV, resulting in increased insulin released from pancreatic cells in vitro.
KW - Alcalase
KW - Common bean
KW - Germination
KW - Pancreatin
KW - Pepsin
KW - Type-2 diabetes
UR - https://www.scopus.com/pages/publications/84938749232
UR - https://www.scopus.com/pages/publications/84938749232#tab=citedBy
U2 - 10.1016/j.foodres.2015.04.041
DO - 10.1016/j.foodres.2015.04.041
M3 - Article
AN - SCOPUS:84938749232
SN - 0963-9969
VL - 76
SP - 150
EP - 159
JO - Food Research International
JF - Food Research International
IS - P1
ER -