Literature DB >> 10742238

Sequencing and expression of additional xylanase genes from the hyperthermophile Thermotoga maritima FjSS3B.1.

R A Reeves1, M D Gibbs, D D Morris, K R Griffiths, D J Saul, P L Bergquist.   

Abstract

Two genes, xynB and xynC, coding for xylanases were isolated from Thermotoga maritima FjSS3B.1 by a genomic-walking-PCR technique. Sequencing of the genes showed that they encode multidomain family 10 xylanases. Only XynB exhibited activity against xylan substrates. The temperature optimum (87 degrees C) and pH optimum (pH 6.5) of XynB are different from the previously reported xylanase, XynA (also a family 10 enzyme), from this organism. The catalytic domain expressed without other domains has a lower temperature optimum, is less thermostable, and has optimal activity at pH 6.5. Despite having a high level of sequence similarity to xynB, xynC appears to be nonfunctional since its encoded protein did not show significant activity on xylan substrates.

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Year:  2000        PMID: 10742238      PMCID: PMC92019          DOI: 10.1128/AEM.66.4.1532-1537.2000

Source DB:  PubMed          Journal:  Appl Environ Microbiol        ISSN: 0099-2240            Impact factor:   4.792


  17 in total

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Authors:  D D Morris; R A Reeves; M D Gibbs; D J Saul; P L Bergquist
Journal:  Appl Environ Microbiol       Date:  1995-06       Impact factor: 4.792

6.  Sequence and expression of a xylanase gene from the hyperthermophile Thermotoga sp. strain FjSS3-B.1 and characterization of the recombinant enzyme and its activity on kraft pulp.

Authors:  D J Saul; L C Williams; R A Reeves; M D Gibbs; P L Bergquist
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8.  Hyperthermostable Thermotoga maritima xylanase XYN10B shows high activity at high temperatures in the presence of biomass-dissolving hydrophilic ionic liquids.

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  8 in total

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