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Screening and identification of five peptides from pinto bean with inhibitory activities against α-amylase using phage display technique

Paper ID Volume ID Publish Year Pages File Format Full-Text
16787 42612 2016 9 PDF Available
Title
Screening and identification of five peptides from pinto bean with inhibitory activities against α-amylase using phage display technique
Abstract

•5 novel anti α-amylase peptides were screened from Pinto bean.•SyP9 exhibited the highest α-amylase inhibition activity with IC50 of 1.97 mg ml−1.•His, Pro and Met residues in PBBP were proposed to be critical for the binding.•Binding sites of amylase were predicted to be Tyr54, Leu194, Met195, Asp229, Ala230, His233, Asp326.•The phage display technique had enhanced the bioactive peptide discovery process.

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 20.56 mg ml−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.

Keywords
α-amylase inhibitor; Bioactive peptides; Phage display; Pinto bean
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Screening and identification of five peptides from pinto bean with inhibitory activities against α-amylase using phage display technique
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Publisher
Database: Elsevier - ScienceDirect
Journal: Enzyme and Microbial Technology - Volume 89, July 2016, Pages 76–84
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering
Get Full-Text Now
Don't Miss Today's Special Offer
Price was $35.95
You save - $31
Price after discount Only $4.95
100% Money Back Guarantee
Full-text PDF Download
Online Support
Any Questions? feel free to contact us