The extracellular endo--1,4-xylanase with multidomain from the extreme thermophile Caldicellulosiruptor lactoaceticus is specific for insoluble xylan degradation
文献类型：期刊论文
| 作者 | Jia, Xiaojing1,2,3; Han, Yejun2 |
| 刊名 | BIOTECHNOLOGY FOR BIOFUELS
 |
| 出版日期 | 2019-06-08 |
| 卷号 | 12页码:14 |
| 关键词 | Endo--1 4-xylanase Carbohydrate-binding module Multi-modularity Thermostability Substrate specificity Caldicellulosiruptor lactoaceticus |
| ISSN号 | 1754-6834 |
| DOI | 10.1186/s13068-019-1480-1 |
| 英文摘要 | BackgroundThe extremely thermophilic bacterium Caldicellulosiruptor lactoaceticus can degrade and metabolize untreated lignocellulosic biomass containing xylan. The mechanism of the bacterium for degradation of insoluble xylan in untreated biomass has not been revealed.ResultsIn the present study, the only annotated extracellular endo--1,4-xylanase (Xyn10B) with multidomain structures in C. lactoaceticus genome was biochemically characterized. Xyn10B contains three N-terminal consecutive family 22 carbohydrate-binding modules (CBMs), one GH10 catalytic domain (CD), two family 9 CBMs and two S-layer homology (SLH) modules in the C-terminal. CBM22a shares 27.1% and 27.2% sequence homology with CBM22b and CBM22c, respectively. The sequence homology between two CBM9s and two SLHs is 26.8% and 25.6%, respectively. To elucidate the effect of multiple domains on the enzymatic properties of Xyn10B, the truncated variants of which (Xyn10B-TM1: CBM22a-CBM22b-CBM22c-CD10; Xyn10B-TM2: CBM22c-CD10; Xyn10B-TM3: CBM22c-CD10-CBM9a; and Xyn10B-TM4: CD10-CBM9a) were separately reconstructed, recombinantly expressed and biochemically characterized. Enzymatic properties studies showed that the optimal temperature for all four Xyn10B truncations was 65 degrees C. Compared to Xyn10B-TM3 and Xyn10B-TM4, Xyn10B-TM1 and Xyn10B-TM2 had higher hydrolytic activity, thermostability and affinity on insoluble substrates. It is noteworthy that Xyn10B-TM1 and Xyn10B-TM2 have higher enzymatic activity on insoluble xylan than the soluble counterparts, whereas Xyn10B-TM3 and Xyn10B-TM4 showed opposite characteristics. The kinetic parameters analysis of Xyn10B-TM1 on xylan showed V-max was 5740, 1300, 1033, and 3925 U/mol on insoluble oat spelt xylan (OSX), soluble beechwood xylan (BWX), soluble sugar cane xylan (SCX), and soluble corncob xylan (CCX), respectively. The results indicated that CBM22s especially CBM22c promoted the hydrolytic activity, thermostability and affinity on insoluble substrates of the Xyn10B truncations. The functions of CBM22, CBM9, CD and SLH are different, while contribute synergetically to the thermostability, protein structure integrity, substrate binding, and high hydrolytic activity on insoluble xylan of untreated lignocellulosic biomass. The domains of CBM22, CBM9, CD and SLH have different characteristics, which synergistically promote the thermostability, protein structure integrity, affinity on insoluble substrates and enzymatic activity properties of Xyn10B.ConclusionsThe extracellular endo--1,4-xylanase with multidomain structures of CBM, CD and SLH promote the biodegradation of insoluble xylan in untreated lignocellulosic biomass by thermophilic C. lactoaceticus. |
| WOS关键词 | CARBOHYDRATE-BINDING MODULE ; THERMOSTABILIZING DOMAINS ; THERMOTOGA-NEAPOLITANA ; CLONING ; DECONSTRUCTION ; EXPRESSION ; XYN10B ; GENE ; PROTEINS ; GH10 |
| 资助项目 | Beijing Advanced Innovation Center for Food Nutrition and Human Health ; National Key Laboratory of Biochemical Engineering |
| WOS研究方向 | Biotechnology & Applied Microbiology ; Energy & Fuels |
| 语种 | 英语 |
| WOS记录号 | WOS:000470784800003 |
| 出版者 | BMC |
| 资助机构 | Beijing Advanced Innovation Center for Food Nutrition and Human Health ; National Key Laboratory of Biochemical Engineering |
| 源URL | [http://ir.ipe.ac.cn/handle/122111/29799]  |
| 专题 | 中国科学院过程工程研究所 |
| 通讯作者 | Han, Yejun |
| 作者单位 | 1.Beijing Technol & Business Univ, Beijing Adv Innovat Ctr Food Nutr & Human Hlth, Beijing 100048, Peoples R China 2.Chinese Acad Sci, Inst Proc Engn, Natl Key Lab Biochem Engn, Beijing 100190, Peoples R China 3.Univ Chinese Acad Sci, Beijing 100049, Peoples R China |
| 推荐引用方式 GB/T 7714 | Jia, Xiaojing,Han, Yejun. The extracellular endo--1,4-xylanase with multidomain from the extreme thermophile Caldicellulosiruptor lactoaceticus is specific for insoluble xylan degradation[J]. BIOTECHNOLOGY FOR BIOFUELS,2019,12:14. |
| APA | Jia, Xiaojing,&Han, Yejun.(2019).The extracellular endo--1,4-xylanase with multidomain from the extreme thermophile Caldicellulosiruptor lactoaceticus is specific for insoluble xylan degradation.BIOTECHNOLOGY FOR BIOFUELS,12,14. |
| MLA | Jia, Xiaojing,et al."The extracellular endo--1,4-xylanase with multidomain from the extreme thermophile Caldicellulosiruptor lactoaceticus is specific for insoluble xylan degradation".BIOTECHNOLOGY FOR BIOFUELS 12(2019):14. |
入库方式： OAI收割
来源：过程工程研究所
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