FOOD SCIENCE ›› 2019, Vol. 40 ›› Issue (3): 293-299.doi: 10.7506/spkx1002-6630-20171020-219

• Reviews • Previous Articles     Next Articles

Recent Advances in Improvement of GH11 Xylanases Thermostability by N-Terminal Modification

HOU Jie1,2, JIANG Yuefeng1,2, XIONG Ke2,3, YANG Ran2,3, LI Xiuting1,2,*   

  1. (1. Beijing Advanced Innovation Center for Food Nutrition and Human Health, Beijing Technology and Business University, Beijing 100048, China; 2. School of Food and Chemical Engineering, Beijing Technology and Business University, Beijing 100048, China; 3. Beijing Engineering and Technology Research Center of Food Additives, Beijing Technology and Business University, Beijing 100048, China)
  • Online:2019-02-15 Published:2019-03-05

RichHTML

9

PDF (PC)

72

Abstract: Xylanases have great potential industrial applications and are promising in the food, feed and paper-making industries. The application of xlanases in different fields is due to their versatile enzymatic properties, especially the outstanding thermostability. Therefore, the heat resistance mechanism of xylanases attracts much research interest. The thermostability of GH11 xylanases has been closely related to their N-terminal region, and many researchers have successfully constructed thermophilic xylanases by N-terminal modification. This paper reviews the factors influencing the thermostability of GH11 xylanases and the different techniques and methods used for N-terminal modification of xylanase for improving heat resistance, and prospects for possible?future applications are discussed. This review is expected to provide valuable information for improving the thermostability of GH11 family xylanases.

Key words: GH11 xylanases, thermostability, factors, N-terminal modification

CLC Number: