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.

蛋白质溶解性差会对它们的功能特性产生负面影响，并极大地限制了它们的应用。与多糖的酶促交联可以提高蛋白质的溶解性和功能特性。使用的酶包括转谷氨酰胺酶、漆酶和过氧化物酶。因此，这项工作介绍了这些酶的交联机制和表征技术，酶法合成的蛋白质-多糖缀合物的改进特性和潜在应用。转谷氨酰胺酶催化新肽键的形成，从而作用于含氨基的多糖与蛋白质结合。然而，漆酶和过氧化物酶催化各种具有苯酚和苯胺结构的化合物的氧化。所以，这两种酶能催化蛋白质与广泛分布于谷麸中的阿魏酰化多糖之间的共轭反应。与未修饰的蛋白质相比，酶法合成的蛋白质-多糖缀合物通常具有更高的溶解度和更好的功能特性。因此，推断与多糖分子的酶促偶联可以扩展蛋白质的应用。