Purification and properties of two thermostable alkaline xylanases from an alkaliphilic Bacillus sp
Article Abstract:
Research was conducted to examine the purification and properties of two thermostable alkaline xylanases from an alkaliphilic Bacillus sp. Bacillus sp. strain AR-009 was developed at 35 degrees C with rotary shaking in 50-ml baffled flasks containing 100 ml of medium. Mode of action of the two enzymes was measured according to the rate of reducing sugar formation and viscosity reduction of oat spelt xylan. The influence of temperature was determined at different temperatures with pH 8 and 9 buffers. The effect of pH on stability was measured by incubating the enzyme at 50 degrees C.
Publication Name: Applied and Environmental Microbiology
Subject: Biological sciences
ISSN: 0099-2240
Year: 1998
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Purification and some properties of an alkaline xylanase from alkaliphilic Bacillus sp. strain 41M-1
Article Abstract:
Bacillus sp. strain 41M-1 is an alkaliphilic soil bacterium which produces large amounts of multiple xylanases extracellularly. The predominant xylanase from this bacterium was purified and characterized. The results showed that the xylanase, designated xylanase J, is an endoxylanase with a molecular mass of 36-kDa and is most active at a pH of 9.0 and temperature of 50 degrees celsius. Partial sequence analysis showed high N-terminal similarity to xylanases of Bacillus pumilus and Clostridium acetobutylicum.
Publication Name: Applied and Environmental Microbiology
Subject: Biological sciences
ISSN: 0099-2240
Year: 1993
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Purification and properties of a xylan-binding endoxylanase from alkaliphilic Bacillus sp. strain K-1
Article Abstract:
Research was conducted to examine the purification and characteristics of the xylan-binding endoxylanase from an alkaliphilic bacterium, Bacillus sp. strain K-1. The xyland-binding xylanase was purified by specific interaction between the xylan-binding region of the enzyme and insoluble xylan. The characteristics of the purified enzyme suggest that the xylanase activity remained considerable in the alkaline pH range. Results also indicate that the enzyme was an endoxylanase.
Publication Name: Applied and Environmental Microbiology
Subject: Biological sciences
ISSN: 0099-2240
Year: 1999
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