Phage display of xylan-binding module of xylanase J from alkaliphilic Bacillus sp. strain 41M-1

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منابع مشابه

A calcium-dependent xylan-binding domain of alkaline xylanase from alkaliphilic Bacillus sp. strain 41M-1.

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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Purification and properties of a xylan-binding endoxylanase from Alkaliphilic bacillus sp. strain K-1.

An alkaliphilic bacterium, Bacillus sp. strain K-1, produces extracellular xylanolytic enzymes such as xylanases, beta-xylosidase, arabinofuranosidase, and acetyl esterase when grown in xylan medium. One of the extracellular xylanases that is stable in an alkaline state was purified to homogeneity by affinity adsorption-desorption on insoluble xylan. The enzyme bound to insoluble xylan but not ...

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Improvement of alkaliphily of Bacillus alkaline xylanase by introducing amino acid substitutions both on catalytic cleft and protein surface.

Xylanase J (XynJ) from alkaliphilic Bacillus sp. 41M-1 is an alkaline xylanase. The crystal structure has been solved with XynJ. Improvement of the alkaliphily of XynJ was attempted by amino acid substitutions. Reinforcing the characteristic salt bridge in the catalytic cleft and introducing excess Arg residues on the protein surface shifted the optimum pH of the wild-type enzyme from 8.5 to 9.5.

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An attempt was made to isolate bacterial strains capable of removing strontium biologically. In this study ten different water samples collected from Neydasht spring in the north of Iran and then the bacterial species were isolated from the water samples. The initial screening of a total of 50 bacterial isolates resulted in selection of one strain. The isolated strain showed a maximum adsorptio...

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ژورنال

عنوان ژورنال: Nucleic Acids Symposium Series

سال: 2000

ISSN: 0261-3166,1746-8272

DOI: 10.1093/nass/44.1.165