博文
云师大生命科学学院周峻沛课题组在国际top期刊《J. Agric. Food Chem. 》上发表最新研究成果
||
2024年3月7日，ACS旗下国际著名期刊《JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY》在线发表了云南师范大学生命科学学院周峻沛教授课题组的最新研究成果《Critical Roles of Acidic Residues in Loop Regions of the Structural Surface for the Salt Tolerance of a GH39 β-d-Xylosidase》。云南师范大学生命科学学院周峻沛教授为通讯作者。
Abstract
Xylan is the main component of hemicellulose. Complete hydrolysis of xylan requires synergistically acting xylanases, such as β-d-xylosidases. Salt-tolerant β-d-xylosidases have significant application benefits, but few reports have explored the critical amino acids affecting the salt tolerance of xylosidases. Herein, the site-directed mutation was used to demonstrate that negative electrostatic potentials generated by 19 acidic residues in the loop regions of the structural surface positively correlated with the improved salt tolerance of GH39 β-d-xylosidase JB13GH39P28. These mutants showed reduced negative potentials on structural surfaces as well as a 13–43% decrease in stability in 3.0–30.0% (w/v) NaCl. Six key residue sites, D201, D259, D297, D377, D395, and D474, were confirmed to influence both the stability and activity of GH39 β-d-xylosidase. The activity of the GH39 β-d-xylosidase was found promoting by SO42– and inhibiting by NO3–. Values of Km and Kcat/Km decreased aggravatedly in 30.0% (w/v) NaCl when mutation operated on residues E179 and D182 in the loop regions of the catalytic domain. Taken together, mutation on acidic residues in loop regions from catalytic and noncatalytic domains may cause the deformation of catalytic pocket and aggregation of protein particles then decrease the stability, binding affinity, and catalytic efficiency of the β-d-xylosidase.
扩展阅读：
周峻沛 生物化学与分子生物学专业，教授，硕士导师，博士生导师
学术任职及兼职：
主要招生专业： 微生物学；生物化学与分子生物学
主要研究方向： 酶 | |
学历及研究简历:（从本科起正序） 2000年9月-2004年7月 云南大学 本科 生物科学专业； 2004年9月-2007年7月 云南大学 硕士 微生物专业； 2007年9月-2010年7月 中国农业科学院 博士 生物化学与分子生物学专业
近三年代表论文和著作： [1]. Zhang R, Li N, Liu Y, Han XW, Tu T, Shen JD, Xu SJ, Qian W, Zhou JP*, Huang ZX. Biochemical and structural properties of a low-temperature-active glycoside hydrolase family 43 β-xylosidase: Activity and instability at high neutral salt concentrations. Food Chemistry, 2019, 301: 125266. [2]. Zhang R, Li N, Xu SJ, Han XW, Li CY, Wei X, Liu Y, Tu T, Tang XH, Zhou JP*, Huang ZX. Glycoside hydrolase family 39 β-xylosidases exhibit β-1,2-xylosidase activity for transformation of notoginsenosides: a new EC subsubclass. Journal of Agricultural and Food Chemistry, 2019, 67: 3220–3228. [3]. Li N, Han XW, Xu SJ, Li CY, Wei X, Liu Y, Zhang R, Tang XH, Zhou JP*, Huang ZX. Glycoside hydrolase family 39 β-xylosidase of Sphingomonas showing salt/ethanol/trypsin tolerance, low-pH/low-temperature activity, and transxylosylation activity. Journal of Agricultural and Food Chemistry, 2018, 66: 9465–9472. [4]. Zhang R, Zhou JP*, Song ZF, Huang ZX. Enzymatic properties of β-N-acetylglucosaminidases. Applied Microbiology and Biotechnology, 2018, 102: 93–103. [5]. Zhou JP, Lu Q, Zhang R, Wang YY, Wu Q, Li JJ, Tang XH, Xu B, Ding JM, Huang ZX. Characterization of two glycoside hydrolase family 36 α-galactosidases: novel transglycosylation activity, lead–zinc tolerance, alkaline and multiple pH optima, and low-temperature activity. Food Chemistry, 2016, 194: 156–166.
近五年获奖成果和名誉称号： 全国专利信息实务人才； 云南省中青年学术技术带头人后备人才； 云南省万人计划青年拔尖人才
近三年主持的国家级或百万以上其他项目： 国家自然科学基金地区项目，31660445，低温外切菊粉酶的低温适应机理研究； 国家自然科学基金地区项目，31960459，双结构域必需木糖苷酶HJ14GH43和JB13GH39的耐盐性突变及适应机理研究
近三年主持的省级以上教学质量工程项目：
近三年主讲课程（研究生，本科）： 蛋白质结构与功能；工业酶制剂与应用；微生物学实验
| |
https://blog.sciencenet.cn/blog-454141-1424675.html
上一篇：云师大生科学院郭锡汉副教授在《AGING CELL》发表最新研究成果
下一篇：Output Styles
