Five thermostable xylanases from microtetraspora flexuosa for us

Details Five thermostable xylanases from microtetraspora flexuosa for us Five thermostable xylanases from microtetraspora flexuosa for us

1994-04-28

1995-08-01

Naff, David M.

Chemistry: molecular biology and microbiology

Enzyme , proenzyme; compositions thereof; process for...

Hydrolase

435278, 4352521, 435822, 536124, C12N 924, C12N 112, D21C 300, C07G 1700

Patent

active

054379920

ABSTRACT:
Five xylanases are purified from the microorganism, Microtetraspora flexuosa,preferably strain ATCC 35864. Each biochemically unique xylanase is thermostable and has optimal activity in alkaline conditions. These enzymes are excellent candidates for enhancing the delignification and bleaching of pulp. Furthermore, treating the pulp with the above enzymes prior to bleaching may reduce the amount of chlorine containing and/or peroxide chemicals required in the bleaching process.

REFERENCES:
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Speth et al., Biol. Chem. Hoppe-Seyler, vol. 370, 591-9, 1989.
Chenglin et al., Acta Microbiol. Sin., 29(1), 7-14, 1989.
Miyadoh et al., Int'l. J. of Syst. Bacteriol., 39(2), 152-158, 1989.
Toda et al., J. of Antibiot., 46(6), 875-883, 1993.
Athalye et al., J. of General Microbiol., 130, 817-23, 1984.
Ghangas, et al., "Cloning of a Thermomonospora fusca Xylanase Gene and Its Expression in Escherichia coli and Streptomyces lividans", J. Bacteriology, 171(6):2963-2969 (Jun. 1989).
Holtz, et al., "Production and properties os xylanases from thermophilic actinomycete", Antonie van Leeuwenhoek, 59:1-7 (1991).

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