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Title: Purification and properties of an endo-1,4-. beta. -glucanase from Clostridium josui

Journal Article · · Journal of Bacteriology; (USA)
OSTI ID:5160930
 [1];  [2]; ; ;  [3]
  1. Nagoya Seiraku Co. Ltd., Tenpaku (Japan)
  2. Thailand Institute of Scientific and Technological Research, Bangkok (Thailand)
  3. Nagoya Univ., Chikusa (Japan)

Recently, cellulolytic anaerobic bacteria have become of great interest because of possible conversion of cellulosic materials from agricultural and forestry wastes, such as rice straw, water hyacinth, and wood chips, to ethanol and other valuable compounds. An enzyme active against carboxymethyl cellulose (CMC) was purified from the stationary-phase-culture supernatant of Clostridium josui grown in a medium containing ball-milled cellulose. The purification in the presence of 6 M urea yielded homogeneous enzyme after an approximately 50-fold increase in specific activity and a 13% yield. The enzyme had a molecular mass of 45 kilodaltons. The optimal temperature and pH of the enzyme against CMC were 60{degree}C and 6.8, respectively. The enzyme hydrolyzed cellotetraose, cellopentaose, and cellohexaose to cellobiose and cellotriose but did not hydrolyze cellobiose or cellotriose. A microcrystalline cellulose, Avicel, was also hydrolyzed significantly, but the extent of hydrolysis was remarkably less than that of CMC. On the basis of these results, the enzyme purified here is one of the endo-1,4-{beta}-glucanases. The N-terminal amino acid sequence of the enzyme is Tyr-Asp-Ala-Ser-Leu-Lys-Pro-Asn-Leu-Gln-Ile-Pro-Gln-Lys-Asn-Ile-Pro-Asn-Asn-Asp-Ala-Val-Asn-Ile-Lys.

OSTI ID:
5160930
Journal Information:
Journal of Bacteriology; (USA), Vol. 171:7; ISSN 0021-9193
Country of Publication:
United States
Language:
English