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Purification and biochemical characterization of glucose–cellobiose-tolerant cellulases from Scytalidium thermophilum

Silva, Jean Carlos Rodrigues ; Guimarães, Luis Henrique Souza ; Salgado, José Carlos Santos ; Furriel, Rosa Prazeres Melo ; Polizeli, Maria Lourdes T. M ; Rosa, José César ; Jorge, João Atilio

Folia microbiologica, 2013-11, Vol.58 (6), p.561-568 [Periódico revisado por pares]

Dordrecht: Springer-Verlag

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Título:
Purification and biochemical characterization of glucose–cellobiose-tolerant cellulases from Scytalidium thermophilum
Autor: Silva, Jean Carlos Rodrigues ; Guimarães, Luis Henrique Souza ; Salgado, José Carlos Santos ; Furriel, Rosa Prazeres Melo ; Polizeli, Maria Lourdes T. M ; Rosa, José César ; Jorge, João Atilio
Assuntos: Applied Microbiology ; Ascomycota - enzymology ; Biochemistry ; Biomedical and Life Sciences ; Biotechnology ; cellobiose ; Cellobiose - metabolism ; Cellulases - chemistry ; Cellulases - isolation & purification ; Cellulases - metabolism ; cellulose ; cysteine ; Electrophoresis, Polyacrylamide Gel ; endo-1,4-beta-glucanase ; Environmental Engineering/Biotechnology ; Enzyme Activators - analysis ; Enzyme Inhibitors - metabolism ; Enzyme Stability ; Enzymes ; Fungi ; Glucose - metabolism ; glucose tolerance ; Hydrogen-Ion Concentration ; hydrolysis ; Immunology ; industrial applications ; Isoelectric Point ; Life Sciences ; manganese ; Mass Spectrometry ; Microbiology ; Molecular Weight ; polyacrylamide gel electrophoresis ; Scytalidium ; sodium dodecyl sulfate ; Temperature
É parte de: Folia microbiologica, 2013-11, Vol.58 (6), p.561-568
Notas: http://dx.doi.org/10.1007/s12223-013-0245-7
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Descrição: Two cellulases from Scytalidium thermophilum were purified and characterized, exhibiting tolerance to glucose and cellobiose. Characterization of purified cellulases I and II by mass spectrometry revealed primary structure similarities with an exoglucanase and an endoglucanase, respectively. Molecular masses were 51.2 and 45.6 kDa for cellulases I and II, respectively, as determined by sodium dodecyl sulfate polyacrylamide gel electrophoresis. Cellulases I and II exhibited isoelectric points of 6.2 and 6.9 and saccharide contents of 11 and 93 %, respectively. Optima of temperature and pH were 60–65 °C and 4.0 for purified cellulase I and 65 °C and 6.5 for purified cellulase II. Both cellulases maintained total CMCase activity after 60 min at 60 °C. Cysteine, Mn²⁺, dithiotreitol and ß-mercaptoethanol-stimulated cellulases I and II. The tolerance to cellulose hydrolysis products and the high thermal stabilities of Scytalidium cellulases suggest good potential for industrial applications.
Editor: Dordrecht: Springer-Verlag
Idioma: Inglês

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Purification and biochemical characterization of glucose–cellobiose-tolerant cellulases from Scytalidium thermophilum

Silva, Jean Carlos Rodrigues ; Guimarães, Luis Henrique Souza ; Salgado, José Carlos Santos ; Furriel, Rosa Prazeres Melo ; Polizeli, Maria Lourdes T. M ; Rosa, José César ; Jorge, João Atilio

Dordrecht: Springer-Verlag

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