Linked Life Data

19756576

Source:http://linkedlifedata.com/resource/pubmed/id/19756576

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
2010-2-16
pubmed:abstractText
We engineered a chimeric enzyme (AwFaeA-CBM42) comprising of type-A feruloyl esterase from Aspergillus awamori (AwFaeA) and family 42 carbohydrate-binding module (AkCBM42) from glycoside hydrolase family 54 alpha-L-arabinofuranosidase of Aspergillus kawachii. The chimeric enzyme was successfully produced in Pichia pastoris and accumulated in the culture broth. The purified chimeric enzyme had an apparent relative molecular mass (M(r)) of 53,000. The chimeric enzyme binds to arabinoxylan; this indicates that the AkCBM42 in AwFaeA-CBM42 binds to arabinofuranose side chain moiety of arabinoxylan. The thermostability of the chimeric enzyme was greater than that of AwFaeA. No significant difference of the specific activity toward methyl ferulate was observed between the AwFaeA and chimeric enzyme, but the release of ferulic acid from insoluble arabinoxylan by the chimeric enzyme was approximately 4-fold higher than that achieved by AwFaeA alone. In addition, the chimeric enzyme and xylanase acted synergistically for the degradation of arabinoxylan. In conclusion, the findings of our study demonstrated that the components of the AwFaeA-CBM42 chimeric enzyme act synergistically to bring about the degradation of complex substrates and that the family 42 carbohydrate-binding module has potential for application in the degradation of polysaccharides.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Arabinose, http://linkedlifedata.com/resource/pubmed/chemical/Carboxylic Ester Hydrolases, http://linkedlifedata.com/resource/pubmed/chemical/Coumaric Acids, http://linkedlifedata.com/resource/pubmed/chemical/Fungal Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Glycoside Hydrolases, http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Xylans, http://linkedlifedata.com/resource/pubmed/chemical/alpha-N-arabinofuranosidase, http://linkedlifedata.com/resource/pubmed/chemical/arabinofuranose, http://linkedlifedata.com/resource/pubmed/chemical/arabinoxylan, http://linkedlifedata.com/resource/pubmed/chemical/ferulic acid, http://linkedlifedata.com/resource/pubmed/chemical/feruloyl esterase
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
1432-0614
pubmed:author
pubmed:issnType
Electronic
pubmed:volume
86
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
155-61
pubmed:meshHeading
pubmed:year
2010
pubmed:articleTitle
Characterization of a chimeric enzyme comprising feruloyl esterase and family 42 carbohydrate-binding module.
pubmed:affiliation
Department of Bioresource Engineering, Faculty of Agriculture, Yamagata University, 1-23 Wakaba-machi, Tsuruoka 9978555, Japan. tkoseki@tds1.tr.yamagata-u.ac.jp
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't, Evaluation Studies