Linked Life Data

20541570

Source:http://linkedlifedata.com/resource/pubmed/id/20541570

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
2010-7-23
pubmed:abstractText
Endo beta-1,4-mannanases (beta-mannanases, EC 3.2.1.78), belonging to CAZy GH5 and GH26 families, catalyze the hydrolysis of structurally different mannans. In this study, the mannanase encoding gene of Aspergillus aculeatus VN was expressed in Aspergillus niger D15#26 using pAN 52-4 vector, under the control of PgpdA promoter and TtrpC terminator. In order to improve the hydrolytic capacity of this GH5 on lignocellulosic substrate, the family 1 carbohydrate-binding module (CBM1) of Aspergillus niger cellobiohydrolase B was artificially fused at the C-terminal end of this enzyme with a natural linker. Both mannanase and mannanase-CBM genes were successfully expressed in A. niger D15#26, producing proteins with molecular masses of 54 and 79 kDa, respectively. The Michaelis-Menten constants, pH activity profiles and temperature optima of three enzymes (wild-type mannanase, recombinant mannanase and recombinant mannanase-CBM) were similar, but the fused mannanase-CBM enzyme was more thermostable. Cross-comparison of the three enzymes for softwood hydrolysis in association with Trichoderma reesei enzymatic cocktail showed that mannanase-CBM improved the glucose yield compared to wild-type and recombinant mannanases.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
1873-4863
pubmed:author
pubmed:copyrightInfo
Copyright 2010 Elsevier B.V. All rights reserved.
pubmed:issnType
Electronic
pubmed:day
2
pubmed:volume
148
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
163-70
pubmed:meshHeading
pubmed:year
2010
pubmed:articleTitle
Hydrolysis of softwood by Aspergillus mannanase: role of a carbohydrate-binding module.
pubmed:affiliation
INRA, UMR1163, Université Aix-Marseille I, II, Marseille, France. pta_bk@yahoo.com
pubmed:publicationType
Journal Article