中国科学院机构知识库网格
Chinese Academy of Sciences Institutional Repositories Grid
Thermostable pectate lyase from Caldicellulosiruptor kronotskyensis provides an efficient addition for plant biomass deconstruction

文献类型:期刊论文

作者Su, Hong1,2; Qiu, Weihua1; Kong, Qing3; Mi, Shuofu1; Han, Yejun1
刊名JOURNAL OF MOLECULAR CATALYSIS B-ENZYMATIC
出版日期2015-11-01
卷号121期号:NOV页码:104-112
关键词Pectate lyase Caldicellulosiruptor Thermostable Degumming Biomass deconstruction
ISSN号1381-1177
英文摘要To understand the enzymological basis for extremely thermophilic, biomass-degrading genus Caldicellulosiruptor metabolize pectin, a thermostable pectate lyase Pel-863 encoded by a gene cluster for hexose-containing polysaccharide metabolism in genome of C. kronotskyensis was studied. The pectate lyase of Caldicellulosiruptor was highly conserved and the representative Pel-863 was biochemically characterized, and the application for pectin containing biomass degradation was also studied. Pel-863 exhibited an optimal activity at 70 degrees C and pH 9.0 with Ca2+ as cofactor. It degraded polygalacturonic acid (PGA), methylated pectin and pectic biomass through endo-cleaving action. The respective V-max and K-m for Pel-863 were 172.8 U/mg and 0.60 g/L on PGA. FTIR and SEM analysis indicated that Pel-863 could remove most of pectin in hemp fiber with less damage compared to alkaline degumming. In addition, pre-digestion with Pel-863 improved glucose and xylose yield by 14.2% and 311.6% respectively for corn stalk, 6.5% and 55% for rice stalk compared with sole action of Novozymes Cellic CTec2. (C) 2015 Elsevier B.V. All rights reserved.
WOS标题词Science & Technology ; Life Sciences & Biomedicine ; Physical Sciences
类目[WOS]Biochemistry & Molecular Biology ; Chemistry, Physical
研究领域[WOS]Biochemistry & Molecular Biology ; Chemistry
关键词[WOS]CATALYZED PROTON ABSTRACTION ; ERWINIA-CHRYSANTHEMI 3937 ; CARBON ACIDS ; FAMILY 3 ; ESCHERICHIA-COLI ; CLONING ; RECOMBINANT ; MECHANISMS ; EXPRESSION ; PECTINASES
收录类别SCI
语种英语
WOS记录号WOS:000365050800015
源URL[http://ir.ipe.ac.cn/handle/122111/19836]  
专题过程工程研究所_生化工程国家重点实验室
作者单位1.Chinese Acad Sci, Natl Key Lab Biochem Engn, Inst Proc Engn, Beijing, Peoples R China
2.Univ Chinese Acad Sci, Beijing, Peoples R China
3.Ocean Univ China, Coll Food Sci & Engn, Qingdao, Peoples R China
推荐引用方式
GB/T 7714
Su, Hong,Qiu, Weihua,Kong, Qing,et al. Thermostable pectate lyase from Caldicellulosiruptor kronotskyensis provides an efficient addition for plant biomass deconstruction[J]. JOURNAL OF MOLECULAR CATALYSIS B-ENZYMATIC,2015,121(NOV):104-112.
APA Su, Hong,Qiu, Weihua,Kong, Qing,Mi, Shuofu,&Han, Yejun.(2015).Thermostable pectate lyase from Caldicellulosiruptor kronotskyensis provides an efficient addition for plant biomass deconstruction.JOURNAL OF MOLECULAR CATALYSIS B-ENZYMATIC,121(NOV),104-112.
MLA Su, Hong,et al."Thermostable pectate lyase from Caldicellulosiruptor kronotskyensis provides an efficient addition for plant biomass deconstruction".JOURNAL OF MOLECULAR CATALYSIS B-ENZYMATIC 121.NOV(2015):104-112.

入库方式: OAI收割

来源:过程工程研究所

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