Please use this identifier to cite or link to this item: http://repositorio.unicamp.br/jspui/handle/REPOSIP/86776
Type: Artigo de periódico
Title: The Characterization Of The Endoglucanase Cel12a From Gloeophyllum Trabeum Reveals An Enzyme Highly Active On β-glucan
Author: Miotto L.S.
De Rezende C.A.
Bernardes A.
Serpa V.I.
Tsang A.
Polikarpov I.
Abstract: The basidiomycete fungus Gloeophyllum trabeum causes a typical brown rot and is known to use reactive oxygen species in the degradation of cellulose. The extracellular Cel12A is one of the few endo-1,4-b-glucanase produced by G. trabeum. Here we cloned cel12A and heterologously expressed it in Aspergillus niger. The identity of the resulting recombinant protein was confirmed by mass spectrometry. We used the purified GtCel12A to determine its substrate specificity and basic biochemical properties. The G. trabeum Cel12A showed highest activity on b-glucan, followed by lichenan, carboxymethylcellulose, phosphoric acid swollen cellulose, microcrystalline cellulose, and filter paper. The optimal pH and temperature for enzymatic activity were, respectively, 4.5 and 50uC on b-glucan. Under these conditions specific activity was 239.269.1 U mg21 and the half-life of the enzyme was 84.663.5 hours. Thermofluor studies revealed that the enzyme was most thermal stable at pH 3. Using b-glucan as a substrate, the Km was 3.260.5 mg mL21 and the Vmax was 0.4160.02 mmol min21. Analysis of the effects of GtCel12A on oat spelt and filter paper by scanning electron microscopy revealed the morphological changes taking place during the process.
Editor: Public Library of Science
Rights: aberto
Identifier DOI: 10.1371/journal.pone.0108393
Address: http://www.scopus.com/inward/record.url?eid=2-s2.0-84907452148&partnerID=40&md5=c643c4d6b6bfdbf2729a9f7c27c9fd89
Date Issue: 2014
Appears in Collections:Unicamp - Artigos e Outros Documentos

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