Open AccessPeptide Fractions from Chymotrypsin-hydrolyzed Moringa oleifera Seed Proteins Inhibit α-amylase and α-glucosidase in vitro
Author(s) -
Oluwafemi Emmanuel Ekun,
Augustine O Olusola,
Joseph Adaviruku Sanni,
Feyisayo Ishola
Publication year - 2022
Publication title -
biology, medicine and natural product chemistry/biology, medicine, and natural product chemistry
Language(s) - English
Resource type - Journals
eISSN - 2540-9328
pISSN - 2089-6514
DOI - 10.14421/biomedich.2022.111.7-16
Subject(s) - chymotrypsin , moringa , isoelectric point , hydrolysate , hydrolysis , chemistry , peptide , amylase , biochemistry , enzyme , trypsin , chromatography , food science
This study attempts to investigate the activities of chymotrypsin-digested M. oleifera seed proteins and their peptide fractions on carbohydrate-hydrolyzing enzymes. Proteins from M. oleifera seeds were isolated using isoelectric point precipitation and hydrolyzed using chymotrypsin. The hydrolysates obtained were fractionated into peptide fractions of