Affiliations 

  • 1 Analytical Biochemistry Research Centre, Universiti Sains Malaysia, 11800 Penang, Malaysia
  • 2 Institute for Research in Molecular Medicine, Universiti Sains Malaysia, 11800 Penang, Malaysia
  • 3 Analytical Biochemistry Research Centre, Universiti Sains Malaysia, 11800 Penang, Malaysia. Electronic address: mattgan81@yahoo.com
Enzyme Microb Technol, 2016 Jul;89:76-84.
PMID: 27233130 DOI: 10.1016/j.enzmictec.2016.04.001

Abstract

The objective of this study was to screen and identify α-amylase inhibitor peptides from Pinto bean. Five Pinto bean bioactive peptides were successfully identified: PPHMLP (P1), PLPWGAGF (P3), PPHMGGP (P6), PLPLHMLP (P7) and LSSLEMGSLGALFVCM (P9). Based on ELISA results, their promising optical density values were 1.27; 3.71, 1.67, 3.20 and 1.03, respectively, which indicated the binding interaction between the peptide and α-amylase occurred. The highest inhibitory activity (66.72%) of the chemically synthesized peptide was shown in SyP9 followed by SyP1 (48.86%), SyP3 (31.17%), SyP7 (27.88%) and SyP6 (23.96%). The IC50 values were 1.97, 8.96, 14.63, 18.45 and 20.56mgml(-1), respectively. Structure activity relationship study revealed that α-amylase was inhibited due to its residues of Ala230, Asp229, Asp326, Tyr54, Met195, Leu194 and His233 were bound. On the other hand, the residues of PBBP (i.e. histidine, proline and methionine) were found to have the highest potency in the binding interaction.

* Title and MeSH Headings from MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.