Author： Khanongnuch C. Ooi T. Kinoshita S.
Publisher： Springer Publishing Company
ISSN： 0959-3993
Source： World Journal of Microbiology and Biotechnology, Vol.15, Iss.2, 1999-04, pp. : 249-258
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Abstract
The two genes for β-mannanase and cellulase of Bacillus sp. 5H have been cloned in Escherichia coli JM 109 by a shotgun method, though the cellulase gene was not expressed in Bacillus sp. 5H. The nucleotide sequences of the β-mannanase gene and the cellulase gene revealed open reading frames of 1,086 and 1,503 base pairs, respectively, coding for a proteins of M_r 40,803 Da (β-mannanase) and 55,420 Da (cellulase). The deduced primary structure of β-mannanase comprised 362 amino acids which had a mature protein of 336 amino acids and a signal peptide of 26 amino acids and that of cellulase comprised 501 amino acid residues.
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