Xylooligosaccharides have shown good prebiotic effects in improving intestinal microecology,and good health care effects in lowering blood glucose, blood pressure, and preventing constipation and so on. In recent years, studies on the preparation of functional xylooligosaccharides using bioenzyme technology have attracted much attention. The features of high specificity and catalytic efficiency of the glycoside hydrolase (GH) 11 xylanase had obvious advantages for xylooligosaccharide production. However, poor stability of most natural GH11 xylanase made it unable to meet the requirements of extreme conditions such as high temperature, strong acid and alkali in industrial production. Molecular modification of natural xylanase by enzyme engineering technology could make xylanase with good substrate specificity and high catalytic efficiency applicable to extreme industrial conditions such as high temperature, strong acid and alkali,which was important and practical for the industrial production of functional xylooligosaccharides. According to the molecular structure of the GH11 xylanase and its characteristics, disulfide bonds have been found to be of great advantage in improving the stability of the enzyme by comparing their intramolecular interaction forces on the thermal stability of the enzyme. Based on the analysis of the structure of the GH11 xylanase, the common strategies for constructing disulfide bonds was summarized, and the effects of constructing single or multiple disulfide bonds in different regions of the enzyme on improving the stability of the GH11 xylanase were compared. Several regions that showed significant changes in enzyme stability after construction of disulfide bonds were localized, and the mode of action of multiple disulfide bonds on improving enzyme stability was introduced. It was expected to provide valuable information for relevant studies on the improvement of stability by enzyme molecular modification, and to broaden the range of industrial applications of GH11 xylanase.