期刊
APPLIED BIOCHEMISTRY AND BIOTECHNOLOGY
卷 160, 期 6, 页码 1627-1636出版社
SPRINGER
DOI: 10.1007/s12010-009-8648-2
关键词
Paenibacillus sp.; Sea bacteria; Endoglucanase; Glycoside hydrolase family 9; Alkali tolerant
资金
- National Natural Sciences Foundation of China [30770021, 30570057]
- 111 project [B07041]
By constructing a genomic library, an endoglucanase gene (cel9P) was cloned from Paenibacillus sp. BME-14 which was isolated from the sea. It had an open-reading frame of 1,629 bp, encoding a peptide of 542-amino acid residue with a calculated molecular mass of 60 kDa. The enzyme showed the highest amino acid identity of 52% with other known endoglucanases and had a C-terminal catalytic domain belonging to the glycosyl hydrolases family 9. The optimum pH and temperature for enzymatic activity was pH 6.5 and 35 A degrees C. The metal ions of Ca2+, Mg2+, and Mn2+ had a positive effect on the activity while Hg2+, Cu2+, and EDTA had a negative effect. Notably, Cel9P had 65% of the maximal activity at 5 A degrees C. Based on the special characteristic of Cel9P, it had a potential significance for study of cold-active mechanism and industry applications.
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