TY - JOUR
T1 - A novel organic solvent-stable alkaline protease from organic solvent-tolerant Bacillus licheniformis YP1A
AU - Li, Shuang
AU - He, Bingfang
AU - Bai, Zhongzhong
AU - Ouyang, Pingkai
PY - 2009/2
Y1 - 2009/2
N2 - An organic solvent-stable alkaline protease producing bacterium was isolated from the crude oil contaminant soil and identified as Bacillus licheniformis. The enzyme retained more than 95% of its initial activity after pre-incubation at 40 °C for 1 h in the presence of 50% (v/v) organic solvents such as DMSO, DMF, and cyclohexane. The protease was active in a broad range of pH from 8.0 to 12.0 with the optimum pH 9.5. The optimum temperature for this protease activity was 60 °C, and the enzyme remained active after incubation at 50-60 °C for 1 h. This organic solvent-stable protease could be used as a biocatalyst for organic solvent-based enzymatic synthesis. Crown
AB - An organic solvent-stable alkaline protease producing bacterium was isolated from the crude oil contaminant soil and identified as Bacillus licheniformis. The enzyme retained more than 95% of its initial activity after pre-incubation at 40 °C for 1 h in the presence of 50% (v/v) organic solvents such as DMSO, DMF, and cyclohexane. The protease was active in a broad range of pH from 8.0 to 12.0 with the optimum pH 9.5. The optimum temperature for this protease activity was 60 °C, and the enzyme remained active after incubation at 50-60 °C for 1 h. This organic solvent-stable protease could be used as a biocatalyst for organic solvent-based enzymatic synthesis. Crown
KW - Alkaline protease
KW - Bacillus licheniformis
KW - Organic solvent-tolerant bacteria
KW - Solvent-stable protease
UR - http://www.scopus.com/inward/record.url?scp=57449096150&partnerID=8YFLogxK
U2 - 10.1016/j.molcatb.2008.08.001
DO - 10.1016/j.molcatb.2008.08.001
M3 - 文章
AN - SCOPUS:57449096150
SN - 1381-1177
VL - 56
SP - 85
EP - 88
JO - Journal of Molecular Catalysis - B Enzymatic
JF - Journal of Molecular Catalysis - B Enzymatic
IS - 2-3
ER -