In silico, in vitro and in vivo analyses of dipeptidyl peptidase IV inhibitory activity and the antidiabetic effect of sodium caseinate hydrolysate

The frequency (A), a novel in silico parameter, was developed by calculating the ratio of the number of truncated peptides with Xaa-proline and Xaa-alanine to all peptide fragments from a protein hydrolyzed with a specific protease. The highest in vitro DPP-IV inhibitory activity (72.7%) was observe...

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Bibliographic Details
Published in:Food & function 2016-02, Vol.7 (2), p.1122-1128
Main Authors: Hsieh, Cheng-Hong, Wang, Tzu-Yuan, Hung, Chuan-Chuan, Jao, Chia-Ling, Hsieh, You-Liang, Wu, Si-Xian, Hsu, Kuo-Chiang
Format: Article
Language:English
Subjects:
Animals
Blood Glucose - metabolism
Bromelains - metabolism
Caseins - pharmacology
Diabetes Mellitus, Experimental - drug therapy
Diet, High-Fat
Dipeptidyl Peptidase 4 - metabolism
Dipeptidyl-Peptidase IV Inhibitors - pharmacology
Endopeptidases - metabolism
Hypoglycemic Agents - pharmacology
Male
Peptide Fragments - chemistry
Peptide Fragments - pharmacology
Rats
Rats, Sprague-Dawley
Streptozocin
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Summary:The frequency (A), a novel in silico parameter, was developed by calculating the ratio of the number of truncated peptides with Xaa-proline and Xaa-alanine to all peptide fragments from a protein hydrolyzed with a specific protease. The highest in vitro DPP-IV inhibitory activity (72.7%) was observed in the hydrolysate of sodium caseinate by bromelain (Cas/BRO), and the constituent proteins of bovine casein also had relatively high A values (0.10-0.17) with BRO hydrolysis. 1CBR (the
ISSN:2042-6496
2042-650X
DOI:10.1039/c5fo01324k