Crosslinking of food proteins mediated by oxidative enzymes – A review

Background With the increase in health awareness and the need to reduce content of sugars, fats, and non-natural food ingredients, as well as increasing demand for food and protein alternatives that do not rely on animal source, researchers have used enzymatic crosslinking as a safe and specific biotechnological tool for modulating food matrix properties while maintaining desired textures. Scope and approach The current manuscript reviews three main oxidative enzymes that were utilized for food protein crosslinking since 2010. Each enzyme is characterized by its reaction mechanism, protein substrates and the effect of the enzymatic reaction on the structure or texture of the matrix. The range of substrates varies from milk proteins, gelatin and collagen to plant proteins such as potato and soy, which are used to formulate gels and emulsions through the formation of extensive protein networks. The influence of enzymatic crosslinking on protein digestibility and allergenicity is also reviewed with respect to protein source, enzyme type and the experimental model used. Key findings and conclusions Laccases, tyrosinases and peroxidases are useful crosslinking agents for generating new textures or for modulating the product formulation while maintaining the desired known texture and mouthfeel. The enzymatic treatments were shown to successfully improve the properties of protein-stabilized emulsions and gels. Commercialization of more oxidative enzymes will enable the increased exploitation of new protein sources and novel combinations of known proteins. Modulating satiety, designing meat replacements, formulating non-dairy cheeses and yogurts with superb consistency are just a few applications of enzyme-mediated crosslinked proteins.