4.7 Article

Development of a workflow for screening and identification of α-amylase inhibitory peptides from food source using an integrated Bioinformatics-phage display approach: Case study - Cumin seed

Journal

FOOD CHEMISTRY
Volume 214, Issue -, Pages 67-76

Publisher

ELSEVIER SCI LTD
DOI: 10.1016/j.foodchem.2016.07.069

Keywords

alpha-Amylase inhibition; Bioactive peptide discovery; Bioinformatics; Phage display

Funding

  1. Universiti Sains Malaysia RUT Grant [1001/CAATS/814257]
  2. MyPhD scholarship

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The main objective of this study was to develop an efficient workflow to discover alpha-amylase inhibitory peptides from cumin seed. A total of 56 unknown peptides was initially found in the cumin seed protein hydrolysate. They were subjected to 2 different in silico screenings and 6 peptides were shortlisted. The peptides were then subjected to in vitro selection using phage display technique and 3 clones (CSP3, CSP4 and CSP6) showed high affinity in binding alpha-amylase. These clones were subjected to the inhibitory test and only CSP4 and CSP6 exhibited high inhibitory activity. Therefore, these peptides were chemically synthesized for validation purposes. CSP4 exhibited inhibition of bacterial and human salivary alpha-amylases with IC50 values of 0.11 and 0.04 mu mol, respectively, whereas CSP6 was about 0.10 and 0.15 mu mol, respectively. Results showed that the strength of each protocol has been successfully combined as deemed fit to enhance the alpha-amylase inhibitor peptide discovery. (C) 2016 Elsevier Ltd. All rights reserved.

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