A study to evaluate the potential of an in silico approach for predicting dipeptidyl peptidase-IV inhibitory activity in vitro of protein hydrolysates

Tzu-Yuan Wang; Cheng-Hong Hsieh; Chuan-Chuan Hung; Chia-Ling Jao; Pei-Yi Lin; You-Liang Hsieh; Kuo-Chiang Hsu

doi:10.1016/j.foodchem.2017.05.035

A study to evaluate the potential of an in silico approach for predicting dipeptidyl peptidase-IV inhibitory activity in vitro of protein hydrolysates

Food Chem. 2017 Nov 1:234:431-438. doi: 10.1016/j.foodchem.2017.05.035. Epub 2017 May 8.

Authors

Tzu-Yuan Wang¹, Cheng-Hong Hsieh², Chuan-Chuan Hung³, Chia-Ling Jao⁴, Pei-Yi Lin⁵, You-Liang Hsieh², Kuo-Chiang Hsu⁶

Affiliations

¹ Division of Endocrine and Metabolism, China Medical University Hospital, 2 YuDe Road, Taichung 40447, Taiwan.
² Department of Health and Nutrition Biotechnology, Asia University, 500, Lioufeng Road, Taichung 41354, Taiwan.
³ Food Safety and Inspection Center, Asia University, 500, Lioufeng Road, Taichung 41354, Taiwan; Department of Nutrition, China Medical University, 91, Hsueh-Shih Road, Taichung 40402, Taiwan.
⁴ Department of Food and Beverage Management, Tung Fang Design University, 110, Tung-Fang Road, Kaohsiung 82941, Taiwan.
⁵ Department of Nutrition, China Medical University, 91, Hsueh-Shih Road, Taichung 40402, Taiwan.
⁶ Department of Health and Nutrition Biotechnology, Asia University, 500, Lioufeng Road, Taichung 41354, Taiwan; Food Safety and Inspection Center, Asia University, 500, Lioufeng Road, Taichung 41354, Taiwan; Department of Nutrition, China Medical University, 91, Hsueh-Shih Road, Taichung 40402, Taiwan. Electronic address: kchsu@mail.cmu.edu.tw.

PMID: 28551257
DOI: 10.1016/j.foodchem.2017.05.035

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.

Keywords: Correlation analysis; Dietary protein; Dipeptidyl peptidase IV inhibitor; In silico analysis.

MeSH terms

Amino Acid Sequence
Computer Simulation
Dipeptidyl Peptidase 4 / metabolism
Dipeptidyl-Peptidase IV Inhibitors / pharmacology*
Protein Hydrolysates / metabolism*

Substances

Dipeptidyl-Peptidase IV Inhibitors
Protein Hydrolysates
Dipeptidyl Peptidase 4