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    Please use this identifier to cite or link to this item: http://tkuir.lib.tku.edu.tw:8080/dspace/handle/987654321/18866

    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
    Contributors: 淡江大學生命科學研究所
    Date: 2009-01
    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
    DOI: 10.1007/s10295-008-0473-z
    Appears in Collections:[化學學系暨研究所] 期刊論文

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