Xylan is the highest content of hemicellulose in plant cells and important microbial resources, it is also one of abundant content of polysaccharides in Nature. Xylanase contains a series of enzymes that can hydrolyze xylan into xylo-oligosaccharides, according to the domain can be divided into different families, of which most of the wooden xylanase belongs to glycoside hydrolase family 10 and 11; And xylanase of family 11 have draw much attention due to the smaller molecular weight, high specific enzyme activity and many other advantages and make it possessing a broad application prospect in the forage, papermaking, food, energy industries. However, the commercialization of xylanase must be easy to produce, have higher enzyme activity, and suitable to the strict industrial processes in various conditions, such as in forage and papermaking industrial processes, sometimes need instantaneous increasing reaction temperature, and these require xylanase to have fairly high specific activity and thermostability under high temperature. But in ordinary conditions, many microorganisms secrete xylanase can not meet this requirement. Therefore, improving the thermostability of xylanase by some reasonable molecular biology methods is people′s constant pursuit of the goal. This paper focuses on explanation of the important properties of the protein, such as the disulfide bond, glycosylation and hydrophobic interaction, and expaciate the effect of these factors on xylanase thermostability of family 11 combined with the author′s personal experiment results. It will have great significance to further deepen understand the mechanism of xylanase and direct the molecular modification of xylanase. |