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

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

doi:10.1002/fsn3.1423

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.

Highlights

In recent years, there is an increasing interest in food protein-derived peptides for their diverse physiological activities such as antioxidant, angiotensin-I-converting enzyme (ACE) inhibitory, and dipeptidyl peptidase-IV (DPP-IV) inhibitory activities
Based on the present limited information in BIOPEP database, fragments with 18 known biological activities were found in quinoa proteins (Figure 1)
Fragments with ACE inhibition, activating ubiquitin-mediated proteolysis, antiamnestic, antioxidative, DPP-IV inhibition, renin inhibition, inhibiting calmodulin-dependent phosphodiesterase (CaMPDE), and stimulating glucose uptake activities existed in all analyzed quinoa protein sequences

Summary

Introduction

There is an increasing interest in food protein-derived peptides for their diverse physiological activities such as antioxidant, angiotensin-I-converting enzyme (ACE) inhibitory, and dipeptidyl peptidase-IV (DPP-IV) inhibitory activities. BIOPEP database, providing collection of sequences (proteins, bioactive peptides, allergenic proteins, and sensory peptides), can be used to predict biological activities about a protein sequence, and to estimate the release of bioactive peptides by proteolysis simulation using certain proteases (Minkiewicz, Dziuba, Iwaniak, Dziuba, & Darewicz, 2008) This in silico tools has been successfully applied in the investigation of bioactive peptides from different sources, including animal products, plant products, and seafood products, such as bovine meat proteins (Minkiewicz, Dziuba, & Michalska, 2011), porcine myofibrillar proteins (Kęska & Stadnik, 2016), yak milk casein (Lin et al, 2018), cereal storage proteins (Cavazos & de Mejia, 2013), oilseed proteins (Han, Maycock, Murray, & Boesch, 2019), giant grouper roe proteins (Panjaitan, Gomez, & Chang, 2018), and portuguese oyster proteins (Gomez, Peralta, Tejano, & Chang, 2019). Online tool PeptideRanker has the function of predicting the potential bioactive index of peptides, and ToxinPred has been developed to predict the toxicity of peptides

Objectives

Results

Conclusion