| Autor: |
Silva JC; Departamento de Bioquímica e Imunologia, Faculdade de Medicina de Ribeirão Preto, Universidade de São Paulo, Ribeirão Preto, São Paulo, Brazil., Guimarães LH, Salgado JC, Furriel RP, Polizeli ML, Rosa JC, Jorge JA |
| Jazyk: |
angličtina |
| Zdroj: |
Folia microbiologica [Folia Microbiol (Praha)] 2013 Nov; Vol. 58 (6), pp. 561-8. Date of Electronic Publication: 2013 Apr 07. |
| DOI: |
10.1007/s12223-013-0245-7 |
| Abstrakt: |
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, Mn(2+), 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. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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