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Biochemical characterization of a novel thermostable GH11 xylanase with CBM6 domain from Caldicellulosiruptor kronotskyensis
Alternative TitleJ. Mol. Catal. B-Enzym.
Qiao, Weibo1,2; Tang, Shuge1; Mi, Shuofu2; Jia, Xiaojing2; Peng, Xiaowei2; Han, Yejun2
2014-09-01
Source PublicationJOURNAL OF MOLECULAR CATALYSIS B-ENZYMATIC
ISSN1381-1177
Volume107Issue:SEPPages:8-16
AbstractThe extreme thermophilic bacterium Caldicellulosiruptor kronotskyensis can use hemicelluloses and cellulose as carbohydrate source. The gene Calkro_0081 encoded a novel GH11 xylanase (Xyn11A) with a catalytic domain (GH-CD) and a carbohydrate binding module (CBM6). The native Xyn11A and two corresponded truncations Xyn11A-CD (catalytic domain of Xyn11A) and Xyn11A-CBM (carbohydrate binding module of Xyn11A) were respectively cloned, heterologously expressed, and biochemically characterized. The recombinant Xyn11A is active in a wide temperature range from 40 to 95 degrees C with the highest activity at 75 degrees C. Xyn11A was completely stable at 70 degrees C for 6 h and more than 50% activity was retained after incubation for 6 h at 75 degrees C. The optimum pH of Xyn11A was 6.0, and it retained 100% activity after 15 h incubation in pH 5.5-7.5 at 70 degrees C. As for Xyn11A-CD, the optimal pH value and temperature were 6.0 and 65 degrees C, the residual activity retained 30% after 6h at 60 degrees C. The respective specific activities of Xyn11A, Xyn11A-CD, and Xyn11A-CBM were 1752.0, 986.8, and 0 IU/mg on beechwood xylan (BWX) at optimum conditions. The activity of Xyn11A is the highest among the reported thermostable xylanases at 75 C. Using BWX as substrate, the final products were xylose and xylobiose after hydrolysis with Xyn11A or Xyn11A-CD. No hydrolytic activity of CBM6 was found, while which shows crucial functions on thermostability and activity for Xyn11A. The characteristics of thermostability and high activity make Xyn11A a potential enzyme for industry application. (C) 2014 Elsevier B.V. All rights reserved.; The extreme thermophilic bacterium Caldicellulosiruptor kronotskyensis can use hemicelluloses and cellulose as carbohydrate source. The gene Calkro_0081 encoded a novel GH11 xylanase (Xyn11A) with a catalytic domain (GH-CD) and a carbohydrate binding module (CBM6). The native Xyn11A and two corresponded truncations Xyn11A-CD (catalytic domain of Xyn11A) and Xyn11A-CBM (carbohydrate binding module of Xyn11A) were respectively cloned, heterologously expressed, and biochemically characterized. The recombinant Xyn11A is active in a wide temperature range from 40 to 95 degrees C with the highest activity at 75 degrees C. Xyn11A was completely stable at 70 degrees C for 6 h and more than 50% activity was retained after incubation for 6 h at 75 degrees C. The optimum pH of Xyn11A was 6.0, and it retained 100% activity after 15 h incubation in pH 5.5-7.5 at 70 degrees C. As for Xyn11A-CD, the optimal pH value and temperature were 6.0 and 65 degrees C, the residual activity retained 30% after 6h at 60 degrees C. The respective specific activities of Xyn11A, Xyn11A-CD, and Xyn11A-CBM were 1752.0, 986.8, and 0 IU/mg on beechwood xylan (BWX) at optimum conditions. The activity of Xyn11A is the highest among the reported thermostable xylanases at 75 C. Using BWX as substrate, the final products were xylose and xylobiose after hydrolysis with Xyn11A or Xyn11A-CD. No hydrolytic activity of CBM6 was found, while which shows crucial functions on thermostability and activity for Xyn11A. The characteristics of thermostability and high activity make Xyn11A a potential enzyme for industry application. (C) 2014 Elsevier B.V. All rights reserved.
KeywordXylanase Thermostable Carbohydrate-binding Module (Cbm) Catalytic Domain (Cd) Caldicellulosiruptor Kronotskyensis
SubtypeArticle
WOS HeadingsScience & Technology ; Life Sciences & Biomedicine ; Physical Sciences
DOI10.1016/j.molcatb.2014.05.009
URL查看原文
Indexed BySCI
Language英语
WOS KeywordCELLULOSE-BINDING DOMAINS ; CLOSTRIDIUM-STERCORARIUM ; RECOMBINANT ENZYME ; GENE CLONING ; EXPRESSION ; PURIFICATION ; BACTERIUM ; HYDROLYSIS ; MODULES ; XYNA
WOS Research AreaBiochemistry & Molecular Biology ; Chemistry
WOS SubjectBiochemistry & Molecular Biology ; Chemistry, Physical
WOS IDWOS:000340698300002
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Cited Times:13[WOS]   [WOS Record]     [Related Records in WOS]
Document Type期刊论文
Version出版稿
Identifierhttp://ir.ipe.ac.cn/handle/122111/11507
Collection研究所(批量导入)
Affiliation1.Shenyang Agr Univ, Shenyang 110866, Peoples R China
2.Chinese Acad Sci, Inst Proc Engn, Natl Key Lab Biochem Engn, Beijing 100190, Peoples R China
Recommended Citation
GB/T 7714
Qiao, Weibo,Tang, Shuge,Mi, Shuofu,et al. Biochemical characterization of a novel thermostable GH11 xylanase with CBM6 domain from Caldicellulosiruptor kronotskyensis[J]. JOURNAL OF MOLECULAR CATALYSIS B-ENZYMATIC,2014,107(SEP):8-16.
APA Qiao, Weibo,Tang, Shuge,Mi, Shuofu,Jia, Xiaojing,Peng, Xiaowei,&Han, Yejun.(2014).Biochemical characterization of a novel thermostable GH11 xylanase with CBM6 domain from Caldicellulosiruptor kronotskyensis.JOURNAL OF MOLECULAR CATALYSIS B-ENZYMATIC,107(SEP),8-16.
MLA Qiao, Weibo,et al."Biochemical characterization of a novel thermostable GH11 xylanase with CBM6 domain from Caldicellulosiruptor kronotskyensis".JOURNAL OF MOLECULAR CATALYSIS B-ENZYMATIC 107.SEP(2014):8-16.
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