TY - JOUR
T1 - Purification and characterization of an organic solvent-tolerant lipase from Pseudomonas aeruginosa LX1 and its application for biodiesel production
AU - Ji, Qingchun
AU - Xiao, Sujing
AU - He, Bingfang
AU - Liu, Xiaoning
PY - 2010/10
Y1 - 2010/10
N2 - An organic solvent-tolerant lipase from newly isolated Pseudomonas aeruginosa LX1 has been purified by ammonium sulfate precipitation and ion-exchange chromatography leading to 4.3-fold purification and 41.1% recovery. The purified lipase from P. aeruginosa LX1 was homogeneous as determined by SDS-PAGE, and the molecular mass was estimated to be 56kDa. The optimum pH and temperature for lipase activity were found to be 7.0 and 40°C, respectively. The lipase was stable in the pH range 4.5-12.0 and at temperatures below 50°C. Its hydrolytic activity was found to be highest towards p-nitrophenyl palmitate (C16) among the various p-nitrophenol esters investigated. The lipase displayed higher stability in the presence of various organic solvents, such as n-hexadecane, isooctane, n-hexane, DMSO, and DMF, than in the absence of an organic solvent. The immobilized lipase was more stable in the presence of nhexadecane, tert-butanol, and acetonitrile. The transesterification activity of the lipase from P. aeruginosa LX1 indicated that it is a potential biocatalyst for biodiesel production.
AB - An organic solvent-tolerant lipase from newly isolated Pseudomonas aeruginosa LX1 has been purified by ammonium sulfate precipitation and ion-exchange chromatography leading to 4.3-fold purification and 41.1% recovery. The purified lipase from P. aeruginosa LX1 was homogeneous as determined by SDS-PAGE, and the molecular mass was estimated to be 56kDa. The optimum pH and temperature for lipase activity were found to be 7.0 and 40°C, respectively. The lipase was stable in the pH range 4.5-12.0 and at temperatures below 50°C. Its hydrolytic activity was found to be highest towards p-nitrophenyl palmitate (C16) among the various p-nitrophenol esters investigated. The lipase displayed higher stability in the presence of various organic solvents, such as n-hexadecane, isooctane, n-hexane, DMSO, and DMF, than in the absence of an organic solvent. The immobilized lipase was more stable in the presence of nhexadecane, tert-butanol, and acetonitrile. The transesterification activity of the lipase from P. aeruginosa LX1 indicated that it is a potential biocatalyst for biodiesel production.
KW - Biodiesel
KW - Characteristics
KW - Organic solvent-tolerant lipase
KW - Pseudomonas aeruginosa
KW - Purification
UR - http://www.scopus.com/inward/record.url?scp=77955982720&partnerID=8YFLogxK
U2 - 10.1016/j.molcatb.2010.06.001
DO - 10.1016/j.molcatb.2010.06.001
M3 - 文章
AN - SCOPUS:77955982720
SN - 1381-1177
VL - 66
SP - 264
EP - 269
JO - Journal of Molecular Catalysis - B Enzymatic
JF - Journal of Molecular Catalysis - B Enzymatic
IS - 3-4
ER -