Researchers from State Key Laboratory of Materials-Oriented Chemical Engineering Describe Findings in Carboxylic Ester Hydrolases (Chemical modification with functionalized ionic liquids: a novel method to improve the enzymatic properties of ...)
By a News Reporter-Staff News Editor at Life Science Weekly -- Research findings on Enzymes and Coenzymes are discussed in a new report. According to news reporting originating from Nanjing, People's Republic of China, by NewsRx correspondents, research stated, "Chemical modification of lysine residues in Candida rugosa lipase (CRL) was carried out using five different functional ionic liquids, and about 15.4-25.0 % of the primary amino groups of lysine were modified. Enzymatic properties of the native and modified CRLs were investigated in olive oil hydrolysis reaction."
Our news editors obtained a quote from the research from the State Key Laboratory of Materials-Oriented Chemical Engineering, "Improved thermal stability, catalytic activity in organic solvents, and adaptability to temperature and pH changes were achieved compared with the native enzyme. CRL modified by [choline][H2PO4] showed the best results, bearing a maximum improvement of 16.7 % in terms of relative activity, 5.2-fold increase in thermostability (after incubation at 45 A degrees C for 5 h), and 2.3-fold increase in activity in strong polar organic solvent (80 % dimethyl sulfoxide) compared with the native enzyme. The results of ultraviolet, circular dichroism and fluorescence spectroscopy suggested that the change of the secondary and tertiary structures of CRL caused by the chemical modification resulted in the enhancement of enzymatic performance."
According to the news editors, the research concluded: "The modification of CRL with functional ionic liquids was proved to be a novel and efficient method for improving the enzymatic properties of CRL."
For more information on this research see: Chemical modification with functionalized ionic liquids: a novel method to improve the enzymatic properties of Candida rugosa lipase. Bioprocess and Biosystems Engineering, 2014;37(8):1617-1626. Bioprocess and Biosystems Engineering can be contacted at: Springer, 233 Spring St, New York, NY 10013, USA. (Springer - www.springer.com; Bioprocess and Biosystems Engineering - www.springerlink.com/content/1615-7591/)
The news editors report that additional information may be obtained by contacting Y. Hu, Nanjing Technical Univ, Coll Biotechnol & Pharmaceut Engn, State Key Lab Mat Oriented Chem Engn, Nanjing 210009, People's Republic of China. Additional authors for this research include J. Yang, R. Jia, Y. Ding, S. Li and H. Huang (see also Enzymes and Coenzymes).
Keywords for this news article include: Asia, Lipase, Nanjing, Solvents, Ionic Liquids, Enzymes and Coenzymes, People's Republic of China, Carboxylic Ester Hydrolases
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