Enzymatic synthesis, characterization and properties of the protein-polysaccharide conjugate: A review

Abstract

Poor solubility of proteins negatively affects their functional properties and greatly limits their application. Enzymatic cross-linking with polysaccharides can improve solubility and functional properties of proteins. The enzymes used include transglutaminase, laccase and peroxidase. Therefore, this work introduces the cross-linking mechanisms of these enzymes and the characterization techniques, the improved properties and the potential applications of the enzymatically-synthesized protein-polysaccharide conjugate. Transglutaminase catalyzes the formation of a new peptide bond and thus works on amino-containing polysaccharides to conjugate with proteins. However, laccase and peroxidase catalyze oxidation of various compounds with phenol and aniline structures. Therefore, these two enzymes can catalyze the conjugate reaction between proteins and feruloylated polysaccharides which are widely distributed in cereal bran. Compared with the unmodified protein, the enzymatically-synthesized protein-polysaccharide conjugate usually has higher solubility and better functional properties. Thus, it is inferred that enzymatic conjugation with polysaccharide molecules can extend the application of proteins.

Keywords: Enzymatic cross-linking; Functional properties; Mechanism; Protein-polysaccharide conjugate; Solubility.