Please use this identifier to cite or link to this item: http://hdl.handle.net/11455/68023
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dc.contributor.authorCheng, Y.M.en_US
dc.contributor.authorHong, T.Y.en_US
dc.contributor.authorLiu, C.C.en_US
dc.contributor.authorMeng, M.S.en_US
dc.date2009zh_TW
dc.date.accessioned2014-06-11T05:56:09Z-
dc.date.available2014-06-11T05:56:09Z-
dc.identifier.issn0175-7598zh_TW
dc.identifier.urihttp://hdl.handle.net/11455/68023-
dc.description.abstractA beta-1,3-glucanase gene, encoding a protein of 1,793 amino acids, was cloned from a strain of Paenibacillus sp. in this study. This large protein, designated as LamA, consists of many putative functional units, which include, from N to C terminus, a leader peptide, three repeats of the S-layer homologous module, a catalytic module of glycoside hydrolase family 16, four repeats of the carbohydrate-binding module of family CBM_4_9, and an analogue of coagulation factor Fa5/8C. Several truncated proteins, composed of the catalytic module with various organizations of the appended modules, were successfully expressed and characterized in this study. Data indicated that the catalytic module specifically hydrolyze beta-1,3- and beta-1,3-1,4-glucans. Also, laminaritriose was the major product upon endolytic hydrolysis of laminarin. The CBM repeats and Fa5/8C analogue substantially enhanced the hydrolyzing activity of the catalytic module, particularly toward insoluble complex substrates, suggesting their modulating functions in the enzymatic activity of LamA. Carbohydrate-binding assay confirmed the binding capabilities of the CBM repeats and Fa5/8C analogue to beta-1,3-, beta-1,3-1,4-, and even beta-1,4-glucans. These appended modules also enhanced the inhibition effect of the catalytic module on the growth of Candida albicans and Rhizoctonia solani.en_US
dc.language.isoen_USzh_TW
dc.relationApplied Microbiology and Biotechnologyen_US
dc.relation.ispartofseriesApplied Microbiology and Biotechnology, Volume 81, Issue 6, Page(s) 1051-1061.en_US
dc.relation.urihttp://dx.doi.org/10.1007/s00253-008-1617-9en_US
dc.subjectbeta-1,3-Glucanaseen_US
dc.subjectLaminarinaseen_US
dc.subjectCarbohydrate-binding moduleen_US
dc.subjectDiscoidinen_US
dc.subjectPaenibacillusen_US
dc.subjectAntifungal proteinen_US
dc.subjectacid-sequence similaritiesen_US
dc.subjectcellulose-binding domainen_US
dc.subjectcell-wallen_US
dc.subjectbiochemical-characterizationen_US
dc.subjectcrystal-structureen_US
dc.subjectinsolubleen_US
dc.subjectbeta-1,3-glucanen_US
dc.subjectantifungal activityen_US
dc.subjectlytic activityen_US
dc.subjectfimi cencen_US
dc.subjectendo-1,3-beta-glucanaseen_US
dc.titleCloning and functional characterization of a complex endo-beta-1,3-glucanase from Paenibacillus spen_US
dc.typeJournal Articlezh_TW
dc.identifier.doi10.1007/s00253-008-1617-9zh_TW
item.languageiso639-1en_US-
item.openairetypeJournal Article-
item.cerifentitytypePublications-
item.grantfulltextnone-
item.fulltextno fulltext-
item.openairecristypehttp://purl.org/coar/resource_type/c_18cf-
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