A study to evaluate the potential of an in silico approach for predicting dipeptidyl peptidase-IV inhibitory activity in vitro of protein hydrolysates. (1st November 2017)

• Record Type: Journal Article
• Authors: Wang, Tzu-Yuan; Hsieh, Cheng-Hong; Hung, Chuan-Chuan; Jao, Chia-Ling; Lin, Pei-Yi; Hsieh, You-Liang; Hsu, Kuo-Chiang
• Is Part Of: Food chemistry. Volume 234(2017)
• Page Start: 431
• Page End: 438
• Publication Date: 2017-11-01
• Subjects: In silico analysis -- Dipeptidyl peptidase IV inhibitor -- Dietary protein -- Correlation analysis; Food -- Analysis -- Periodicals; Food -- Composition -- Periodicals; 664
• DOI: 10.1016/j.foodchem.2017.05.035
• Languages: English
• ISSNs: 0308-8146

Abstract

Highlights: The in silico parameter, frequency ( A ), was applied as a screening tool. 294 proteins and 5 proteases listed in the BIOPEP database were analyzed in silico . Numbers of peptides with Xaa-Pro and Xaa-Ala was the key factor of frequency. Frequency and DPP-IV inhibitory activity in vitro showed a strong correlation. Abstract: A total of 294 edible protein sequences and 5 commercial proteases listed in the BIOPEP database were analyzed in silico . The frequency ( A ), a parameter in silico described previously, was examined further to calculating the ratio of truncated peptides with Xaa-proline and/or Xaa-alanine to all peptide fragments in a protein hydrolyzed with a protease, using the BIOPEP database. Then the in vitro DPP-IV inhibitory activity was determined using the same 15 protein and protease combinations to evaluate their relationship. The result shows that A values considering the number of Xaa-proline + Xaa-alanine exhibited a strong correlation with in vitro DPP-IV inhibition rates by Pearson's correlation analysis (r = 0.6993; P < 0.05). Therefore, the in silico approach is effective to predict DPP-IV inhibitory activities in vitro of protein hydrolysates.