Novel dipeptidyl peptidase-IV and angiotensin-I-converting enzyme inhibitory peptides released from quinoa protein by in silico proteolysis

通过计算机蛋白水解从藜麦蛋白中释放出新型二肽基肽酶-IV和血管紧张素-I转换酶抑制肽

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作者:Huimin Guo, Aurore Richel, Yuqiong Hao, Xin Fan, Nadia Everaert, Xiushi Yang, Guixing Ren

Abstract

Quinoa protein has been paid more and more attention because of its nutritional properties and beneficial effects. With the development of bioinformatics, bioactive peptide database and computer-assisted simulation provide an efficient and time-saving method for the theoretical estimation of potential bioactivities of protein. Therefore, the potential of quinoa protein sequences for releasing bioactive peptides was evaluated using the BIOPEP database, which revealed that quinoa protein, especially globulin, is a potential source of peptides with dipeptidyl peptidase-IV (DPP-IV) and angiotensin-I-converting enzyme (ACE) inhibitory activities. Three plant proteases, namely papain, ficin, and stem bromelain, were employed for the in silico proteolysis of quinoa protein. Furthermore, four tripeptides (MAF, NMF, HPF, and MCG) were screened as novel promising bioactive peptides by PeptideRanker. The bioactivities of selected peptides were confirmed using chemical synthesis and in vitro assay. The present work suggests that quinoa protein can serve as a good source of bioactive peptides, and in silico approach can provide theoretical assistance for investigation and production of functional peptides.

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