TY - JOUR
T1 - Influence of Hydrolysis on the Bioactive Properties and Stability of Chickpea-Protein-Based O/W Emulsions
AU - Felix, Manuel
AU - Cermenõ, Maria
AU - Fitzgerald, Richard J.
N1 - Publisher Copyright:
Copyright © 2020 American Chemical Society.
PY - 2020/9/16
Y1 - 2020/9/16
N2 - This study evaluated the effect of enzymatic hydrolysis on the emulsion microstructure and bioactive properties of oil-in-water emulsions generated using chickpea protein concentrate (CP) and its 10 and 210 min Alcalase CP hydrolysates (CPH10 and CPH210, respectively) at three pH values (2.5, 5.0, and 7.5). Chromatographic profiles demonstrated CP protein breakdown following hydrolysis. Increasing the degree of hydrolysis resulted in increased emulsion droplet size and decreased viscoelastic moduli. The antioxidant capacities of the emulsions generated with CPH10 and CPH210 increased significantly compared to those generated with CP and were pH-dependent. Both angiotensin-converting enzyme and dipeptidyl peptidase-IV inhibitory activities were significantly increased in emulsions stabilized with CPH210; however, these results were also pH-dependent. In vitro gastrointestinal digestion of the emulsions resulted in a significant increase in all bioactivities. These results demonstrate the potential for enzymatic hydrolysis to beneficially modulate the emulsifying and bioactive properties of CP proteins.
AB - This study evaluated the effect of enzymatic hydrolysis on the emulsion microstructure and bioactive properties of oil-in-water emulsions generated using chickpea protein concentrate (CP) and its 10 and 210 min Alcalase CP hydrolysates (CPH10 and CPH210, respectively) at three pH values (2.5, 5.0, and 7.5). Chromatographic profiles demonstrated CP protein breakdown following hydrolysis. Increasing the degree of hydrolysis resulted in increased emulsion droplet size and decreased viscoelastic moduli. The antioxidant capacities of the emulsions generated with CPH10 and CPH210 increased significantly compared to those generated with CP and were pH-dependent. Both angiotensin-converting enzyme and dipeptidyl peptidase-IV inhibitory activities were significantly increased in emulsions stabilized with CPH210; however, these results were also pH-dependent. In vitro gastrointestinal digestion of the emulsions resulted in a significant increase in all bioactivities. These results demonstrate the potential for enzymatic hydrolysis to beneficially modulate the emulsifying and bioactive properties of CP proteins.
KW - antioxidant activity
KW - chickpea protein
KW - emulsion
KW - enzyme inhibition
KW - microscopy
KW - protein hydrolysates
UR - http://www.scopus.com/inward/record.url?scp=85091126763&partnerID=8YFLogxK
U2 - 10.1021/acs.jafc.0c02427
DO - 10.1021/acs.jafc.0c02427
M3 - Article
C2 - 32815360
AN - SCOPUS:85091126763
SN - 0021-8561
VL - 68
SP - 10118
EP - 10127
JO - Journal of Agricultural and Food Chemistry
JF - Journal of Agricultural and Food Chemistry
IS - 37
ER -