Screening, purification and characterization of a novel cold-active and organic solvent-tolerant lipase from Stenotrophomonas maltophilia CGMCC 4254.
An extracellular organic solvent-tolerant and cold-active lipase producing bacterium was isolated from oil-contaminated soil samples, and identified taxonomically as Stenotrophomonas maltophilia. The lipase from S. maltophilia CGMCC 4254 (SML) was purified 60.5-fold to homogeneity with 38.9 U/mg specific activity. Partially purified SML displayed remarkable stability in 50% and 100% (v/v) hydrophobic organic solvents after incubation for 7 days. The enzyme also retained more than 50% of its residual activity in several pure hydrophilic organic solvents after incubation for 7 days. SML showed 57% maximum activity at 5°C, and had optimal activity at 35°C. These unique properties of SML make it promising as a biocatalyst for industrial processes.
Institute of Bioengineering, Department of Chemical and Biological Engineering, Zhejiang University, Hangzhou 310027, China.
Mu
M
Li
Li-Rong
LR
Yang
Gang
G
Xu
Jian-Ping
JP
Wu
D003080:Cold Temperature; D004795:Enzyme Stability / Q000187:drug effects; D006863:Hydrogen-Ion Concentration / Q000187:drug effects; D008049:Lipase / Q000096:biosynthesis / Q000302:isolation & purification* / Q000378:metabolism*; D009930:Organic Chemicals / Q000494:pharmacology*; D010802:Phylogeny; D012997:Solvents / Q000494:pharmacology*; D020615:Stenotrophomonas maltophilia / Q000187:drug effects / Q000201:enzymology*; D013379:Substrate Specificity / Q000187:drug effects
D009930:Organic Chemicals; D012997:Solvents; D008049:Lipase
Cold-active; Lipase; Non-aqueous; Solvent tolerant; Stenotrophomonas maltophilia