Inhibition of the in vitro activities of α-amylase, α-glucosidase and pancreatic lipase by yellow field pea (Pisum sativum L.) protein hydrolysates |
| |
Authors: | Temitola O Awosika Rotimi E Aluko |
| |
Affiliation: | Department of Food and Human Nutritional Sciences, University of Manitoba, Winnipeg, MB, R3T 2N2 Canada |
| |
Abstract: | The aim of this work was to produce yellow field pea protein-derived peptides as inhibitors of α-amylase, α-glucosidase and pancreatic lipase activities. A pea protein concentrate was hydrolysed with alcalase, chymotrypsin, pepsin or trypsin and the hydrolysates separated into different fractions (<1, 1–3, 3–5, 5–10 kDa) by membrane ultrafiltration. Peptide sequence analysis showed that the alcalase hydrolysate had higher levels of di- and tripeptides when compared with the chymotrypsin, pepsin and trypsin hydrolysates. The peptide fractions inhibited α-amylase and α-glucosidase activities at levels that were similar to the unfractionated hydrolysates. The peptides were more active against α-amylase (inhibition at μg level) than α-glucosidase (mg level). In contrast, the fractionated peptides had reduced ability (IC50 >4.2 mg mL?1) when compared with the unfractionated hydrolysate (IC50 <4.2 mg mL?1) to inhibit lipase activity. Enzyme kinetic studies revealed that the peptides reduced α-amylase activity through competitive inhibition. However, inhibition of α-glucosidase activity was non-competitive. |
| |
Keywords: | Enzyme inhibition kinetics pancreatic lipase protein hydrolysates ultrafiltration α-Amylase α-glucosidase |
|
|