Alkaline Mannanase from a Novel Species of Alkaliphilic Bacillus
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چکیده
منابع مشابه
Purification and enzymatic properties of a highly alkaline mannanase from alkaliphilic Bacillus sp. strain JAMB-750
An alkaliphilic Bacillus isolate (strain JAMB-750) was found to exoproduce a novel alkaline mannanase (AmA). AmA was purified to homogeneity (about 98% pure) as judged by SDS-polyacrylamide electrophoresis. The molecular mass was approximately 130 kDa. The hydrolysis patterns of various substrates indicated that the enzyme was an endo-type enzyme. The optimal temperature and pH for activity wer...
متن کاملCrystallization and preliminary X-ray study of alkaline mannanase from an alkaliphilic Bacillus isolate.
An alkaline mannanase (EC 3.2.1.78) from the alkaliphilic Bacillus sp. strain JAMB-602 was cloned and sequenced. The deduced amino-acid sequence of the enzyme suggested that the enzyme consists of a catalytic and unknown additional domains. The recombinant enzyme expressed by B. subtilis was crystallized using the hanging-drop vapour-diffusion method at 277 K. X-ray diffraction data were collec...
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Significant progress has been made in isolating novel alkaline β-mannanases, however, there is a paucity of information concerning the structural basis for alkaline tolerance displayed by these β-mannanases. We report the catalytic domain structure of an industrially important β-mannanase from the alkaliphilic Bacillus sp. N16-5 (BSP165 MAN) at a resolution of 1.6 Å. This enzyme, classified int...
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The biochemical and molecular mechanisms used by alkaliphilic bacteria to acquire iron are unknown. We demonstrate that alkaliphilic (pH > 9) Bacillus species are sensitive to artificial iron (Fe³+) chelators and produce iron-chelating molecules. These alkaliphilic siderophores contain catechol and hydroxamate moieties, and their synthesis is stimulated by manganese(II) salts and suppressed by ...
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Xylanase J of alkaliphilic Bacillus sp. strain 41M-1 contains a carbohydrate-binding module family 36 xylan-binding domain (XBD). Mutational analysis of the XBD revealed that Tyr237, Asp313, Trp317, and Asp318 were involved in Ca(2+)-dependent xylan-binding, and that Asp313 and Asp318 were especially important.
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ژورنال
عنوان ژورنال: Journal of Applied Glycoscience
سال: 2004
ISSN: 1344-7882,1880-7291
DOI: 10.5458/jag.51.229