文献类型：期刊文献

英文题名：Enhancement of the performance of the GH75 family chitosanases by fusing a carbohydrate binding module and insights into their substrate binding mechanisms

作者：Zhou, Jianli Gu, Qiuya Shen, Yu Harindintwali, Jean Damascene Yang, Wenhua Zou, Shuliang Han, Minghai Ma, Chao Yu, Xiaobin Liu, Xiaobo

第一作者：Zhou, Jianli

通信作者：Yu, XB[1];Liu, XB[2]

机构：[1]Guizhou Univ, Sch Liquor & Food Engn, Guizhou Prov Key Lab Fermentat Engn & Biopharm, Guiyang 550025, Peoples R China;[2]Jiangnan Univ, Key Lab Carbohydrate Chem & Biotechnol, Minist Educ, 1800 Lihu Rd, Wuxi 214122, Peoples R China;[3]Jiangnan Univ, Sch Biotechnol, 1800 Lihu Rd, Wuxi 214122, Peoples R China;[4]Guizhou Inst Technol, Sch Food & Pharmaceut Engn, 1 Caiguan Rd, Guiyang 550003, Peoples R China;[5]Univ Chinese Acad Sci, 19 Yuquan Rd, Beijing 100049, Peoples R China;[6]Nanjing Univ Sci & Technol, Sch Environm & Biol Engn, 200 Xiaolingwei St, Nanjing 210094, Jiangsu, Peoples R China

第一机构：Guizhou Univ, Sch Liquor & Food Engn, Guizhou Prov Key Lab Fermentat Engn & Biopharm, Guiyang 550025, Peoples R China

通信机构：corresponding author), Jiangnan Univ, Sch Biotechnol, 1800 Lihu Rd, Wuxi 214122, Peoples R China;corresponding author), Nanjing Univ Sci & Technol, Sch Environm & Biol Engn, 200 Xiaolingwei St, Nanjing 210094, Jiangsu, Peoples R China.

年份：2022

卷号：163

外文期刊名：LWT-FOOD SCIENCE AND TECHNOLOGY

收录：;EI(收录号：20222112157675);Scopus(收录号：2-s2.0-85130581335);WOS:【SCI-EXPANDED(收录号:WOS:000807492200002)】；

基金：This project was financially supported by the National First-class Discipline Program of the Light Industry Technology and Engineering (LITE2018-11) , the Guizhou Institute of Technology Science Research Project (XJGC20190655) , and the National Natural Science Foundation of China (31760022) .

语种：英文

外文关键词：Chitosan; Chitooligosaccharide; Chitosanase; Carbohydrate-binding module; Thermodynamic analysis

摘要：Chitooligosaccharides (COSs) with relatively higher degrees of polymerization (DP) exhibited better biological properties than COSs with lower DP. Here, we demonstrated a potential strategy to enhance the affinity, activity, and thermostability of the chitosanase Csn75 from Aspergillus fumigatus CJ22-326 through fusion of a carbohydrate binding module (CBM) that can specifically bind to chitosan. Compared with the Csn75, the specific enzyme activity of the Csn75-CBM32 and the Csn75-2CBM32 had increased by 59.18% and 14.29%, respectively. The free energy (Delta G), enthalpy (Delta H), and entropy (-T Delta S) of the three enzymes (Csn75, Csn75-CBM32, and Csn75-2CBM32) toward (GlcN)6 was (-7.19, -7.54, and -8.08 kcal/mol), (-5.37, 1.75, and 0.86 kcal/mol), and (1.45, 9.27, and 8.03 kcal/mol), respectively. The substrate binding of the Csn75 and the fusion enzymes (Csn75-CBM32 and Csn75-2CBM32) were mainly driven by the hydrophobic (entropy effect) and favorable intermolecular forces (enthalpy contribution), respectively. Moreover, the DP of COSs in the final hydrolysate of Csn75 was 2-4, but that of Csn75-CBM32 and Csn75-2CBM32 was 3-5. This strategy provides a potential alternative for the bioproduction of desirable COSs to meet the requirement of application in food systems.