Cellulomonas flavigena: characterization of an endo-1,4-xylanase tightly induced by sugarcane bagasse
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چکیده
منابع مشابه
Complete genome sequence of Cellulomonas flavigena type strain (134T)
Cellulomonas flavigena (Kellerman and McBeth 1912) Bergey et al. 1923 is the type species of the genus Cellulomonas of the actinobacterial family Cellulomonadaceae. Members of the genus Cellulomonas are of special interest for their ability to degrade cellulose and hemicellulose, particularly with regard to the use of biomass as an alternative energy source. Here we describe the features of thi...
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In present research exploration, sugar cane bagasse an indigenous waste/by product carbon source was tested as substrate for optimum biosynthesis of xylanase by Aspergillus niger using the submerged fermentation technique. The for xylanase production, thee concentration levels (2.5, 3.0 and 3.5%) of sugar cane bagasse, four different fermentation temperatures (i.e. 25.0, 27.5, 30.0 and 32.5C) a...
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The bacteria in the genus Cellulomonas are known for their ability to degrade plant cell wall biomass. Cellulomonas fimi ATCC 484 and C. flavigena ATCC 482 have been the subject of much research into secreted cellulases and hemicellulases. Recently the genome sequences of both C. fimi ATCC 484 and C. flavigena ATCC 482 were published, and a genome comparison has revealed their full spectrum of ...
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Three-step extraction of lignin fractions from ball-milled sugarcane bagasse (SCB) was studied with 96% dioxane, 50% dioxane, and 80% dioxane containing 1% NaOH at boiling temperature followed by purification to remove hemicelluloses. The total yields of hemicelluloses and lignin were 15.8% and 7.2% based on dried SCB, respectively. In the first step, 5.1% lignin (70.8% of the total extracted l...
متن کاملCharacterization of CenC, an enzyme from Cellulomonas fimi with both endo- and exoglucanase activities.
The cenC gene, encoding beta-1,4-glucanase C (CenC) from Cellulomonas fimi, was overexpressed in Escherichia coli with a tac-based expression vector. The resulting polypeptide, with an apparent molecular mass of 130 kDa, was purified from the cell extracts by affinity chromatography on cellulose followed by anion-exchange chromatography. N-terminal sequence analysis showed the enzyme to be prop...
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ژورنال
عنوان ژورنال: FEMS Microbiology Letters
سال: 2002
ISSN: 0378-1097
DOI: 10.1016/s0378-1097(02)00876-5