Albizia lebbeck Seed Protein Hydrolysates Inhibit α-Amylase and α-Glucosidase in vitro

Authors

  • Oluwafemi Ekun Adekunle Ajasin University, Akungba-Akoko
  • Adedoyinsola David Ojajuni Institute of Agriculture and Animal Science, Lamjung Campus, Kathmandu, Bagmati Province, Nepal
  • Tomilola Grace Laoye Department of Biochemistry, Faculty of Science, Adekunle Ajasin University, Akungba Akoko, Ondo State, Nigeria
  • Deborah Motunrayo Amusan Department of Biochemistry, Faculty of Science, Adekunle Ajasin University, Akungba Akoko, Ondo State, Nigeria
  • Adedolapo Adeola Bakinde Department of Biochemistry, Faculty of Science, Adekunle Ajasin University, Akungba Akoko, Ondo State, Nigeria
  • Racheal Gift Ekun Department of Biochemistry, Faculty of Science, Adekunle Ajasin University, Akungba Akoko, Ondo State, Nigeria
  • Deborah Oluwafunbi Ajewole Department of Biochemistry, Faculty of Science, Adekunle Ajasin University, Akungba Akoko, Ondo State, Nigeria
  • Precious Yemi Ashogbon Department of Biochemistry, Faculty of Science, Adekunle Ajasin University, Akungba Akoko, Ondo State, Nigeria
  • Opeyemi Glory Akinsulu Department of Biochemistry, Faculty of Science, Adekunle Ajasin University, Akungba Akoko, Ondo State, Nigeria

Keywords:

Albizia lebbeck, hydrolysates, α-amylase, α-glucosidase, diabetes mellitus

Abstract

Albizia lebbeck seeds have been found to contain a high proportion of proteins, which on hydrolysis have yielded hydrolysates which contained bioactive peptides that possessed antioxidant activities in earlier studies. Hence, this study investigated the potentials of these hydrolysates in inhibiting two carbohydrate – hydrolyzing enzymes, α-amylase and α-glucosidase. Albizia lebbeck seed proteins were hydrolyzed using the proteinases trypsin, chymotrypsin and papain. The hydrolysates obtained were evaluated for their inhibitory effects against α-amylase and α-glucosidase. The results revealed that Albizia lebbeck seed proteins were most susceptible to chymotrypsin hydrolysis (degree of hydrolysis of 62.43±1.685%) when compared to those of trypsin and papain. However, hydrolysates obtained from papain hydrolysis exhibited the highest inhibitory activities against α-amylase (70.453±1.619%) whereas tryptic digests inhibited α-glucosidase better than chymotrypsin and papain hydrolysates (55.354±0.808%). The result also suggest that proteinase specificity influenced the relative enzyme-inhibitory activities of the resulting hydrolysates, in terms of the nature of peptides released. The study concludes that Albizia lebbeck seed proteins, on proteolysis with appropriate enzymes, possess potentially therapeutic peptides which can be further characterized towards the development of provide peptide-based alternatives in the management of diabetes mellitus.

Downloads

Published

2024-06-30

Issue

Vol. 8 No. 1 (2024): International Journal of Applied Biology

Section

Articles

License

Copyright Notice

 

This is an open access journal which means that all contents is freely available without charge to the user or his/her institution. Users are allowed to read, download, copy, distribute, print, search, or link to the full texts of the articles in this journal without asking prior permission from the publisher or the author. This is in accordance with the BOAI definition of open access. 

Submission of an article implies that the work described has not been published previously (except in the form of an abstract or as part of a published lecture or academic thesis), that it is not under consideration for publication elsewhere, that its publication is approved by all authors and tacitly or explicitly by the responsible authorities where the work was carried out, and that, if accepted, will not be published elsewhere in the same form, in English or in any other language, without the written consent of the Publisher. An article based on a section from a completed graduate dissertation may be published in International Journal of Applied Biology, but only if this is allowed by author's(s') university rules. The Editors reserve the right to edit or otherwise alter all contributions, but authors will receive proofs for approval before publication. 

International Journal of Applied Biology operates a CC-BY 4.0 © license for journal papers. Copyright remains with the author, but International Journal of Applied Biology is licensed to publish the paper, and the author agrees to make the article available with the CC-BY 4.0 license. Reproduction as another journal article in whole or in part would be plagiarism.