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Thermostable pectate lyase from Caldicellulosiruptor kronotskyensis provides an efficient addition for plant biomass deconstruction
Su, Hong1,2; Qiu, Weihua1; Kong, Qing3; Mi, Shuofu1; Han, Yejun1
2015-11-01
Source PublicationJOURNAL OF MOLECULAR CATALYSIS B-ENZYMATIC
ISSN1381-1177
Volume121Issue:NOVPages:104-112
AbstractTo 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.
KeywordPectate Lyase Caldicellulosiruptor Thermostable Degumming Biomass Deconstruction
SubtypeArticle
WOS HeadingsScience & Technology ; Life Sciences & Biomedicine ; Physical Sciences
DOI10.1016/j.molcatb.2015.08.013
Indexed BySCI
Language英语
WOS KeywordCATALYZED PROTON ABSTRACTION ; ERWINIA-CHRYSANTHEMI 3937 ; CARBON ACIDS ; FAMILY 3 ; ESCHERICHIA-COLI ; CLONING ; RECOMBINANT ; MECHANISMS ; EXPRESSION ; PECTINASES
WOS Research AreaBiochemistry & Molecular Biology ; Chemistry
WOS SubjectBiochemistry & Molecular Biology ; Chemistry, Physical
Funding OrganizationNational "863" High-Tech Research and Development Program of China(2014AA021905) ; 100 Talents Program of Institute of Process Engineering, Chinese Academy of Sciences
WOS IDWOS:000365050800015
Citation statistics
Cited Times:1[WOS]   [WOS Record]     [Related Records in WOS]
Document Type期刊论文
Identifierhttp://ir.ipe.ac.cn/handle/122111/19836
Collection生化工程国家重点实验室
Affiliation1.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
Recommended Citation
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.
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