A high-detergent-performance, cold-adapted lipase from Pseudomonas stutzeri PS59 suitable for detergent formulation

• A novel method to isolate novel lipase-producing strains for formulation detergent.
• The lipase produced from Pseudomonas stutzeri PS59 keeps high activity at lower temperature.
• The better stability of the lipase to metal ions and detergent additives.
• The lipase showed superior washing performance.
• The lipase also showed an attractive potency for application in biocatalysis.

A high-detergent-performance and cold-adapted lipase was purified and characterised from Pseudomonas stutzeri PS59, which was isolated from Daqing oil fields (Heilongjiang, PR China). The lipase was purified to homogeneity using ammonium sulphate precipitation, dialysis, freeze–drying, ion exchange chromatography and gel filtration chromatography. The molecular weight of the lipase was approximately 55 kDa, as measured by SDS-PAGE. The lipase showed optima activity at pH 8.5 and 20 °C. The lipase activity was activated by metal ions, such as Ca2+ and Mn2+, and surfactants, such as Tween 80, Tween 20, sodium dodecyl benzene sulfonate and urea. Oxidising agents, such as H2O2 and NaClO, were found to have little effect on the activity of the lipase, and most organic solvents can enhance the activity of the lipase. The broad substrate specificity and the compatibility of the lipase in the presence of surfactants, oxidising agents, and other detergent additives clearly indicate its potential application in the laundry industry. The hydrolysis resolution of (R,S)-ethyl 2-methylbutyrate by P. stutzeri PS59 lipase was carried out with the yield of 31.2% for R-ethyl 2-methylbutyrate, the enantiomeric excess of residual substrate (ees) was 85.7%. Thus, the lipase also showed an attractive potency for application in biocatalysis.

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