Excessive calorie intake in the form of glucose and fatty acids is a causative factor in the development of obesity and diabetes. Therefore, agents that reduce the activities of carbohydrases and lipases could be used to prevent or treat these chronic diseases. In this work, enzymatic hydrolysis of pea proteins was used to produce peptides that inhibited activities of lipase, α-amylase, α-glucosidase. The protein hydrolysates were obtained using each of the following enzymes: alcalase, chymotrypsin, pepsin or trypsin. Each hydrolysate was then fractionated into peptides of different sizes (&lt;1, 1-3, 3-5, 5-10 kDa) using membrane ultrafiltration and their activities compared with those of the protein hydrolysates. Results showed alcalase hydrolysis produced the highest protein hydrolysate yield (58.2%) while trypsin yielded the least (44.0%). Alcalase was also the most efficient in producing small (&lt;5 kDa) peptides while pepsin was the least. The higher proteolytic efficiency of alcalase was confirmed with identification of the most content of di- and tripeptides when compared to the chymotrypsin, pepsin and trypsin hydrolysates. The protein hydrolysates inhibited in vitro activities of α-amylase and α-glucosidase activities at levels that were similar to the peptide fractions. However, the protein hydrolysates and peptide fractions had stronger (µg concentrations) inhibitions of α-amylase activity than α-glucosidase (mg concentrations). For lipase inhibition, the unfractionated hydrolysates (IC<sub>50</sub> &lt;4.2 mg/mL) were more potent than the fractionated peptides (IC<sub>50</sub> &gt;4.2 mg/mL). Double reciprocal plots revealed competitive and non-competitive inhibitions of α-amylase and α-glucosidase activities, respectively by the pea protein-derived peptides. The results suggest that the pea peptides may serve as useful ingredients to formulate functional foods that reduce the release of calories from diets.

Pea protein-derived peptides as inhibitory agents against carbohydrate and lipid-digesting enzymes

2019 Fall National Meeting

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