TY - JOUR
T1 - Cloning and Characterizing the Thermophilic and Detergent Stable Cellulase CelMytB from Saccharophagus sp. Myt-1
AU - Sakatoku, Akihiro
AU - Tanaka, Daisuke
AU - Kamachi, Hiroyuki
AU - Nakamura, Shogo
N1 - Funding Information:
Acknowledgments This study was partly supported by grants from the Japan Society for the Promotion of Science (Grant-in Aid for JSPS Research Fellows No. 10085 (to AS).
PY - 2014/3
Y1 - 2014/3
N2 - We previously isolated and reported a second species of the Saccharophagus genus, Saccharophagus sp. strain Myt-1. In the present study, a cellulase gene (celMytB) from the genomic DNA of Myt-1 was cloned and characterized. The DNA sequence fragment contained an open reading frame of 1,893 bp that encoded a protein of 631 amino acids with an estimated molecular mass of 66.8 kDa. The deduced protein, CelMytB, had a catalytic domain that contained a conserved signature sequence (VIYEIYNEPL) of glycosyl hydrolase family 5 and a CBM6 cellulose binding module. CelMytB showed optimal activity at 55 °C and pH 6.5, which is similar to the optimal temperature and pH profile of cel5H, an endoglucanase from the closely related S. degradans 2-40. However, the cellulase (degradation of soluble cellulose) and avicelase (degradation of crystalline cellulose) activities of CelMytB were about 3-fold and 100-fold higher, respectively, than the equivalent activities of cel5H. Moreover, CelMytB could degrade xylan. From the zymogram results, we speculated that the catalytic domain of CelMytB had high activity even without the cellulose binding module. The presence of some detergents stimulated the cellulase activity of CelMytB.
AB - We previously isolated and reported a second species of the Saccharophagus genus, Saccharophagus sp. strain Myt-1. In the present study, a cellulase gene (celMytB) from the genomic DNA of Myt-1 was cloned and characterized. The DNA sequence fragment contained an open reading frame of 1,893 bp that encoded a protein of 631 amino acids with an estimated molecular mass of 66.8 kDa. The deduced protein, CelMytB, had a catalytic domain that contained a conserved signature sequence (VIYEIYNEPL) of glycosyl hydrolase family 5 and a CBM6 cellulose binding module. CelMytB showed optimal activity at 55 °C and pH 6.5, which is similar to the optimal temperature and pH profile of cel5H, an endoglucanase from the closely related S. degradans 2-40. However, the cellulase (degradation of soluble cellulose) and avicelase (degradation of crystalline cellulose) activities of CelMytB were about 3-fold and 100-fold higher, respectively, than the equivalent activities of cel5H. Moreover, CelMytB could degrade xylan. From the zymogram results, we speculated that the catalytic domain of CelMytB had high activity even without the cellulose binding module. The presence of some detergents stimulated the cellulase activity of CelMytB.
KW - Cellulase
KW - Detergent stable
KW - Saccharophagus sp. Myt-1
KW - Thermophilic
KW - Xylanase
UR - http://www.scopus.com/inward/record.url?scp=84891660356&partnerID=8YFLogxK
U2 - 10.1007/s12088-013-0421-0
DO - 10.1007/s12088-013-0421-0
M3 - 学術論文
C2 - 24426162
AN - SCOPUS:84891660356
SN - 0046-8991
VL - 54
SP - 20
EP - 26
JO - Indian Journal of Microbiology
JF - Indian Journal of Microbiology
IS - 1
ER -