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|Title: ||Purification and characterization of extracellular lipases from Pseudomonas monteilii TKU009 by the use of soybeans as the substrate|
|Authors: ||Wang, San-Lang;Lin, Yu-Ting;Liang, Tzu-Wen;Chio, Sau-Hua;Ming, Li-June;Wu, Pei-Chen|
|Issue Date: ||2013-02-27 09:39:31 (UTC+8)|
|Publisher: ||Heidelberg: Springer|
|Abstract: ||A lipase-producing bacterium was isolated and identified as Pseudomonas monteilii TKU009. A lipase (F2) and lipase-like materials (F1) were purified from the culture supernatant of P. monteilii TKU009 with soybean powder as the sole carbon/nitrogen source. The molecular mass of F1 and F2 was estimated to be 44 kDa by SDS-PAGE and gel filtration. The optimum pH, optimum temperature, and pH and thermal stabilities of F2 were 7, 40°C, 8–11, and 50°C; and of F1 were 6, 40°C, 6–7, and 50°C, respectively. F2 was completely inhibited by EDTA and slightly by Mg2+, Fe2+, Mn2+, and SDS. F1 was completely inhibited by EDTA and Fe2+ and strongly by Zn2+, Mn2+, Ca2+, Mg2+, and SDS. The activities of both the enzymes were enhanced by the addition of non-ionic surfactants Triton X–100 and Tween 40, especially for F1. F2 preferably acted on substrates with a long chain (C10–C18) of fatty acids, while F1 showed a broad spectrum on those with chain length of C4–C18. The marked activity of F2 in organic solvents makes it an ideal choice for application in a water-restricted medium including organic synthesis.|
|Relation: ||Journal of Industrial Microbiology and Biotechnology 36(1), pp.65-73|
|Appears in Collections:||[Graduate Institute & Department of Chemistry] Journal Article|
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