Review
Enhancing enzymatic hydrolysis of food proteins and production of bioactive peptides using high hydrostatic pressure technology

https://doi.org/10.1016/j.tifs.2018.08.013Get rights and content

Highlights

  • Advantages and challenges of HHP techniques are presented.

  • HHP assisted enzymatic hydrolysis improves protein digestibility.

  • Production of bioactive peptides depends on HHP parameters and protein source.

  • Simultaneous HHP and hydrolysis could be an interesting alternative approach.

Abstract

Background

Bioactive peptides (BPs) generated by hydrolysis of food proteins exhibit a broad spectrum of biological properties (antihypertensive, hypocholesterolemic, antimicrobial, antioxidant, etc.) in both in vitro and in vivo models. Initially obtained from milk and egg products, BPs have now largely been obtained from food byproducts such as marine, animal and plant biomasses. Amongst the various strategies being developed for BPs production, enzymatic hydrolysis (EH) is the most widely preferred due to its GRAS nature. However, the main challenge of EH is to decrease the time and quantity of enzyme, and improve yield and bioactivity of BPs.

Scope and approach

Consequently, innovative and efficient food technologies have been developed to satisfy these needs. High hydrostatic pressure (HHP) processing, a non-thermal technology, initially developed to extend food shelf-life, is being considered as a promising tool to improve the efficiency of EH and generate high value-added peptide fractions from various complex biomasses.

Findings and conclusions

This innovative and emerging technology enhances EH by inducing protein unfolding/denaturation, as well as activating the enzymes used while maintaining their nutritional and functional properties. This review discusses the state of the art of HHP technique, its applications in combination with EH, and potential challenges for the production of BPs from food-derived protein sources.

Introduction

Over the last decade, many studies have described the role of proteins as a source of biologically active peptides and different strategies to improve their production. Bioactive peptides (BPs), generally composed of 2–20 amino acid residues and inactive in the sequence of their native protein, have been investigated extensively as they have positive effects on physiological functions, improving health (Kitts & Weiler, 2003; H; Korhonen & Pihlanto, 2003). Hence, BPs can be added to many products or ingredients and labeled as “functional foods” or “nutraceuticals” (Hartmann & Meisel, 2007). Different strategies are used to produce BPs. Microbial fermentation and enzyme-catalyzed proteolysis is the most widely studied and applied, while autolysis and acid hydrolysis are less common. Although there have been many studies on the production and optimization of the BPs production process, there are still many challenges to developing an industrial-scale production system with higher peptide yields and lower cost. Recently, the in-silico approach allowed researchers to predict the production of BPs from food proteins using bioinformatics and databases. Combined with classical approaches this method can determine the best BPs production parameters, such as the type of enzyme to be used (Fu, Wu, Zhu, & Xiao, 2016; Udenigwe, 2014). Other issues include demonstrating effective bioactivity and health benefits through in vitro and in vivo experiments as well as clinical trials for pharmaceutical applications (Government, 2003). Finally, safety assessments must be completed and efficient regulatory guidelines for the use of BPs must be developed. Nevertheless, a few products are already supplemented with BPs and are available in international markets (Hartmann & Meisel, 2007; H; Korhonen & Pihlanto, 2003).

Bioactive peptide production benefits from the increasing application of novel and emerging food processing technologies. In this regard, technologies such as high hydrostatic pressure (HHP), microwave, and pulsed electric field have been recognized as three of the most promising emerging technologies with growing commercial interest (Jermann, Koutchma, Margas, Leadley, & Ros-Polski, 2015). More specifically, HHP applications have attracted considerable research attention for their ability to increase food product shelf-life (J.-C. Cheftel, 1992; J. C. Cheftel, 1995) and modulate food proteins. Diverse fields are increasingly turning to HHP processing since it is regarded as one of the most sustainable and green technologies. Functional and nutritional properties, as well as the organoleptic quality of food products, are generally maintained after HHP treatment but modifications to protein structure and conformation may be induced (Rastogi, Raghavarao, Balasubramaniam, Niranjan, & Knorr, 2007). Indeed, HHP treatment affects significantly on hydrophobic and electrostatic bonds, but a very little on covalent bonds causing the proteins to unfold or denature (Lullien-Pellerin & Balny, 2002; Vadim V; Mozhaev, Heremans, Frank, Masson, & Balny, 1996; V. V.; Mozhaev, Lange, Kudryashova, & Balny, 1996; Rivalain, Roquain, & Demazeau, 2010). Thereupon, using HHP can alter enzyme-substrate (protein) interaction and hydrolysis rate. Over the last decade, many studies have evaluated the impact of HHP on protein denaturation and aggregation. These studies have demonstrated that HHP treatment can improve enzymatic hydrolysis of a food-derived protein (from plant to dairy and meat proteins) and enhance generation of BPs by using a large spectrum of enzymes (Bamdad, Shin, Suh, Nimalaratne, & Sunwoo, 2017; Boukil, Suwal, Chamberland, Pouliot, & Doyen, 2018; Guan, Diao, Jiang, Han, & Kong, 2018; Homma, Ikeuchi, & Suzuki, 1994). This critical review discusses the potential application of HHP as an emerging technology to improve food-derived protein digestibility and generation of BPs.

Section snippets

Bioactive peptides

Bioactive peptides are composed of 2–20 amino acid residues, generated from parent proteins where their native structure is inactive. According to their structural properties, amino acid composition, charge and sequence, these low molecular weight molecules exhibit many biological properties (Hartmann & Meisel, 2007; Hannu Korhonen & Pihlanto, 2006). Bioactive peptides have been generated from a wide range of food proteins. Milk and egg proteins (Clare & Swaisgood, 2000; Mine, 2007) are the

Autolysis

Autolysis is the cleavage of proteins by endogenous proteases. In this context, the term autolysate is preferred to hydrolysate. Numerous studies have clearly demonstrated the utility of autolysis for BPs production, mostly from marine byproducts due to their high endogenous enzyme content. Depending on the protein source used, a large number of digestive enzymes were characterized, such as pepsin, trypsin, chymotrypsin or cathepsin (Song, Zhang, & Wei, 2016). For instance, autolysate

Fundamental aspects

High hydrostatic pressure, also called “pascalization” or “cold pasteurization”, is a non-thermal and eco-efficient technology governed by Le Chatelier's principle, which states that any phenomenon leading to a decrease in volume is enhanced by pressure (Vadim V Mozhaev, Heremans, Frank, Masson, & Balny, 1994). While HHP was first applied at a laboratory-scale by Hite in 1989 to destroy microorganisms in milk in order to improve its shelf-life, the technology was considered an emerging process

Conclusions

Bioactive peptides have been largely recognized as high value-added compounds for the nutraceutical and pharmaceutical industries. Food-derived BPs are commonly produced by enzymatic hydrolysis even though new strategies, such as in silico approaches, are being developed. Producing BPs at a commercial scale, however, involves many challenges. Optimization of hydrolysis parameters to generate and recover the maximum amount of BPs from a complex food matrix with use of minimum enzyme is crucial

Acknowledgements

This research did not receive any specific grant from funding agencies in the public, commercial, or not-for-profit sectors.

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