A novel endoglucanase (Cel9P) from a marine bacterium Paenibacillus sp. BME-14.
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 degrees C. The metal ions of Ca(2+), Mg(2+), and Mn(2+) had a positive effect on the activity while Hg(2+), Cu(2+), and EDTA had a negative effect. Notably, Cel9P had 65% of the maximal activity at 5 degrees C. Based on the special characteristic of Cel9P, it had a potential significance for study of cold-active mechanism and industry applications.
Fu
Xiaoyu
X
State Key Laboratory of Agricultural Microbiology, College of Life Science and Technology, Huazhong Agricultural University, Wuhan, 430070, People's Republic of China.
Liu
Pengfu
P
Lin
Ling
L
Hong
Yuzhi
Y
Huang
Xiaoluo
X
Meng
Xin
X
Liu
Ziduo
Z
D000595:Amino Acid Sequence; D002480:Cellulase / Q000737:chemistry / Q000235:genetics* / Q000302:isolation & purification / Q000378:metabolism; D002855:Chromatography, Thin Layer; D003001:Cloning, Molecular; D006863:Hydrogen-Ion Concentration / Q000187:drug effects; D007477:Ions; D008670:Metals / Q000494:pharmacology; D008969:Molecular Sequence Data; D056507:Paenibacillus / Q000187:drug effects / Q000201:enzymology* / Q000235:genetics*; D012623:Seawater / Q000382:microbiology*; D016415:Sequence Alignment; D017422:Sequence Analysis, DNA; D013379:Substrate Specificity / Q000187:drug effects
D007477:Ions; D008670:Metals; D002480:Cellulase