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New Carboxylic Ester Hydrolases Study Findings Recently Were Reported by Researchers at Beijing University of Chemical Technology

June 24, 2014



By a News Reporter-Staff News Editor at Life Science Weekly -- Investigators discuss new findings in Enzymes and Coenzymes. According to news originating from Beijing, People's Republic of China, by NewsRx correspondents, research stated, "Candida sp. 99-125 lipase immobilized on surface hydrophobic modified support and appropriate substrate feeding methods were used to improve the synthesis of tri-substituted trimethylolpropane (TMP) esters, which can be used as raw materials for biodegradable lubricants. The proposed novel production method is environmentally friendly."

Our news journalists obtained a quote from the research from the Beijing University of Chemical Technology, "Lipase was adsorbed on surface hydrophobic silk fibers that were pretreated by amino-modified polydimethylsiloxane. A 5-level-4-factors central composite model, including reaction time, temperature, enzyme amount, and molar ratio of fatty acid to TMP, was designed to evaluate the interaction of process variables in the enzymatic esterification. The water activity was kept constant using a LiCI-saturated salt solution. Under the optimum conditions with 30% enzyme amount and substrates molar ratio 8.4 at 45 degrees C for 47 h, the total conversion of caprylic acid is 97.3% and the yield of tri-substituted TMP esters is 95.5%. The surface hydrophobic treatment resulted in less cluster water accumulated on the surface immobilized lipase, which was demonstrated by near-infrared spectra. Consequently, the optimum temperature and water tolerance of immobilized lipase were increased."

According to the news editors, the research concluded: "Two TMP-feeding methods were used to maintain high molar ratio of fatty acid to TMP, and increase the final tri-substituted TMP esters content exceeding 85% (w/w) in reactant."

For more information on this research see: Enhancing trimethylolpropane esters synthesis through lipase immobilized on surface hydrophobic modified support and appropriate substrate feeding methods. Enzyme and Microbial Technology, 2014;58-59():60-67. Enzyme and Microbial Technology can be contacted at: Elsevier Science Inc, 360 Park Ave South, New York, NY 10010-1710, USA. (Elsevier - www.elsevier.com; Enzyme and Microbial Technology - www.elsevier.com/wps/product/cws_home/525004)

The news correspondents report that additional information may be obtained from Y.F. Tao, Beijing University of Chemical Technology, Minist Educ, Beijing Key Lab Bioproc, Biorefinery Res & Engn Center, Beijing 100029, People's Republic of China. Additional authors for this research include C.X. Cui, H.Q. Shen, L. Liu, B.Q. Chen and T.W. Tan (see also Enzymes and Coenzymes).

Keywords for this news article include: Asia, Lipase, Beijing, Carboxylic Acids, Enzymes and Coenzymes, People's Republic of China, Carboxylic Ester Hydrolases

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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