News Column

New Findings from Tianjin University of Science and Technology Describe Advances in Carboxylic Ester Hydrolases

June 17, 2014

By a News Reporter-Staff News Editor at Life Science Weekly -- Fresh data on Enzymes and Coenzymes are presented in a new report. According to news reporting from Tianjin, People's Republic of China, by NewsRx journalists, research stated, "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 news correspondents obtained a quote from the research from the Tianjin University of Science and Technology, "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 degrees 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 NaCIO, 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 (ee(s)) was 85.7%."

According to the news reporters, the research concluded: "Thus, the lipase also showed an attractive potency for application in biocatalysis."

For more information on this research see: A high-detergent-performance, cold-adapted lipase from Pseudomonas stutzeri PS59 suitable for detergent formulation. Journal of Molecular Catalysis B-Enzymatic, 2014;102():16-24. Journal of Molecular Catalysis B-Enzymatic can be contacted at: Elsevier Science Bv, PO Box 211, 1000 Ae Amsterdam, Netherlands (see also Enzymes and Coenzymes).

Our news journalists report that additional information may be obtained by contacting X.L. Li, Tianjin Univ Sci & Technol, Key Lab Ind Fermentat Microbiol, Minist Educ, Coll Biotechnol, Tianjin, People's Republic of China. Additional authors for this research include W.H. Zhang, Y.D. Wang, Y.J. Dai, H.T. Zhang, Y. Wang, H.K. Wang and F.P. Lu.

Keywords for this news article include: Asia, Lipase, Tianjin, Detergents, Pseudomonadaceae, Gammaproteobacteria, Pseudomonas stutzeri, Enzymes and Coenzymes, Surface-Active Agents, Gram-Negative Bacteria, People's Republic of China, Carboxylic Ester Hydrolases, Gram-Negative Aerobic Bacteria, Gram-Negative Aerobic Rods and Cocci

Our reports deliver fact-based news of research and discoveries from around the world. Copyright 2014, NewsRx LLC

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Source: Life Science Weekly

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