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Applied and Environmental Microbiology, April 2000, p. 1532-1537, Vol. 66, No. 4
Department of Biological Sciences, Macquarie
University, Sydney New South Wales, Australia,1
and Centre for Gene Technology, University of
Auckland,2 and Department of Molecular
Medicine, University of Auckland Medical
School,3 Auckland, New Zealand
Received 19 October 1999/Accepted 10 January 2000
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°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.
0099-2240/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.
Sequencing and Expression of Additional Xylanase
Genes from the Hyperthermophile Thermotoga maritima
FjSS3B.1
*
Corresponding author. Mailing address: Research Office,
Macquarie University, Sydney, NSW 2109, Australia. Phone:
61-2-9850-8614. Fax: 61-2-9850-8799. E-mail:
peter.bergquist{at}mq.edu.au.
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