Purification and biochemical characterization of glucose-cellobiose-tolerant cellulases from Scytalidium thermophilum
Jazyk angličtina Země Spojené státy americké Médium print-electronic
Typ dokumentu časopisecké články, práce podpořená grantem
- MeSH
- aktivátory enzymů analýza MeSH
- Ascomycota enzymologie MeSH
- celobiosa metabolismus MeSH
- celulasy chemie izolace a purifikace metabolismus MeSH
- elektroforéza v polyakrylamidovém gelu MeSH
- glukosa metabolismus MeSH
- hmotnostní spektrometrie MeSH
- inhibitory enzymů metabolismus MeSH
- izoelektrický bod MeSH
- koncentrace vodíkových iontů MeSH
- molekulová hmotnost MeSH
- stabilita enzymů MeSH
- teplota MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
- Názvy látek
- aktivátory enzymů MeSH
- celobiosa MeSH
- celulasy MeSH
- glukosa MeSH
- inhibitory enzymů MeSH
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.
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