Creating Proteins with Novel Functionality via the Maillard Reaction: A Review

Abstract

Proteins are widely utilized to add functional properties, such as gelling and emulsification to foods. These attributes depend on a number of factors such as molecular structure of the protein, the pH, and the composition of its chemical environment. There is substantial evidence to suggest that the functional properties of food proteins can be further improved by derivatization. Covalent bonding of proteins to polysaccharides and smaller reducing sugars via the Maillard reaction has been shown to alter the functionality of proteins without requiring the addition of chemical reagents. Establishment of a technologically feasible method for preparing the conjugates and optimization of the processing conditions, however, is needed to promote their development as functional food ingredients. This paper provides a state-of-the-art contribution to the impact of the Maillard reaction on protein functionality. It presents a deeper understanding of the influence of processing conditions and reactant formulation on improving desirable properties of proteins. In particular attention is given to how potential improvements could be achieved in the emulsifying, textural, and solubility properties of proteins to add value to commodity food ingredients. Elements that are considered to be critical to the design of functional Maillard conjugates are highlighted and suggestions proposed to facilitate progress in this area.

Effects of caseinate deamidation on transglutaminase-induced glucosamine conjugation and cross-linking as well as properties of the treated caseinates

“…In recent years, the Maillard-type glycation has been widely used to generate new glycoproteins, by conjugating carbohydrates covalently into food proteins (Zhu, Damodaran, & Lucey, 2008). Past studies have shown that the generated glycoproteins had improved functional properties including emulsifying properties (Diftis & Kiosseoglou, 2003) and solubility (Oliver, Melton, & Stanley, 2006). However, the Maillard-type glycation of the proteins might have some adverse effects that cannot be ignored both in practical applicability and safety, such as a difficulty in reaction control, a longer reaction time, the undesired color and flavor of products, and the formation of some potential mutagenic compounds (Brands, Alink, Van-Boekel, & Jongen, 2000).…”

In vitro immuno-modulatory ability of tryptic caseinate hydrolysate affected by prior caseinate glycation using the Maillard reaction or transglutaminase

“…Caseinate is one of these protein ingredients with good nutritive values and desired functional properties, and thus often used in food processing (Oliver, Melton, & Stanley, 2006). However, chemical modifications of proteins can lead to both structure and property innate and adaptive immunity and their roles in phagocytosis (Kim et al, 2013).…”

Structure and property changes of soybean protein isolates resulted from the glycation and cross-linking by transglutaminase and a degraded chitosan

“…The well-known chemical modifications of proteins include acetylation, succinylation, esterification, amidation, and other reactions, have been used in the past studies, and are not introduced here. In addition, protein glycation has become an area of considerable research interest in recent years (Oliver, Melton, & Stanley, 2006). The well-known Maillard reaction is able to glycate proteins (Martins, Jongen, & Van Boekel, 2000), via the formation of protein-saccharide conjugates.…”