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

Article Abstract:

Researchers used a genomic-walking-PCR technique to isolate the xynB and xynC xylanase genes from Thermota maritima FjSS3B.1. Xylanases are used to reduce the amount of chlorine needed to bleach wood pulp during the manufacture of paper.

Thermophilic bacteria

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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

Article Abstract:

The nucleotide sequence of the gene that encodes the hyperthermophillic bacterium Thermotoga sp. strain FjSS3-B.1 xylanase reveals that it encodes only a single domain. That domain is family 10 xylanase. The enzyme, when encoded by a recombinant gene, is thermally stable and has a broad range of optimal pH. The enzyme acts on xylan in Pinus radiata kraft pulp. Activity parameters of the enzyme are akin to industrial atmosphere and hence it has an edge over other processes of enzymatic pulp degradation.

Wood pulp industry, Nucleotide sequence, Base sequence, Pulp industry

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Cloning, sequence, and expression of a xylanase gene from the extreme thermophile Dictyoglomus thermophilum Rt46B.1 and activity of the enzyme on fiber-bound substrate

Article Abstract:

The subcloning of a xylanase gene from the thermophile Dictyoglomus thermophilum Rt46B.1 suggests that xylanase activity is present only in an internal 1,507-bp PstI-HindIII region. Sequencing of this fragment confirms that it has an open reading frame coding for a single-domain xylanase, XynA. XynA is an endo-acting xylanase with 352 amino acids that hydrolyzes xylan to xylotriose and xylobiose. XynA capable of hydrolyzing xylan in kraft pulp and may be useful as an aid in pulp bleaching.

Genetic aspects, Observations, Enzymes, Thermophiles

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