Gene cloning, sequencing, and biochemical characterization of endoxylanase from Thermoanaerobacterium saccharolyticum B6A-RI - PubMed (original) (raw)

Gene cloning, sequencing, and biochemical characterization of endoxylanase from Thermoanaerobacterium saccharolyticum B6A-RI

Y E Lee et al. Appl Environ Microbiol. 1993 Sep.

Abstract

The gene encoding endoxylanase (xynA) from Thermoanaerobacterium saccharolyticum B6A-RI was cloned and expressed in Escherichia coli. A putative 33-amino-acid signal peptide, which corresponded to the N-terminal amino acids, was encoded by xynA. An open reading frame of 3,471 bp, corresponding to 1,157 amino acid residues, was found, giving the xynA gene product a molecular mass of 130 kDa. xynA from T. saccharolyticum B6A-RI had strong similarity to genes from family F beta-glycanases. The temperature and pH optimum for the activity of the cloned endoxylanase were 70 degrees C and 5.5, respectively. The cloned endoxylanase A was stable at 75 degrees C for 60 min and displayed a specific activity of 227.4 U/mg of protein on oat spelt xylan. The cloned xylanase was an endo-acting enzyme.

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References

    1. Appl Environ Microbiol. 1989 May;55(5):1230-3 -PubMed
    1. Eur J Biochem. 1980;108(1):313-21 -PubMed
    1. Appl Environ Microbiol. 1985 Mar;49(3):656-9 -PubMed
    1. J Bacteriol. 1990 Oct;172(10):6098-105 -PubMed
    1. Arch Microbiol. 1984 May;138(1):31-6 -PubMed

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