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KMID : 0545119990090060832
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Journal of Microbiology and Biotechnology
1999 Volume.9 No. 6 p.832 ~ p.838
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Extracellular Triacylglycerol Lipases Secreted by New Isolate of Filamentous Fungus
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Lusta, Konstantin A.
Woo, Sahng Young/Chung, Il Kyung/Sul, Ill Whan/Park, Hee Sung/Shin, Dong Ill
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Abstract
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Two different types of lipases (lipase Ⅰ and lipase Ⅱ) secreted into culture medium by Rhizopus sp. L-1 were purified using a hydrophobic chromatography and were partially characterized. Both enzymes were monomeric as revealed by SDS-PAGE and gel filtration. The molecular masses of the enzymes were identified as 45kDa (lipase Ⅰ) and 69kDa (lipase Ⅱ). The isoelectric points were estimated to be 3.6 and 5.2 for lipase Ⅰ and lipase Ⅱ, respectively. pH and temperature activity optima for lipase I were as 7.5 and 50℃, respectively, whereas the corresponding parameters for lipase Ⅱ were 6.0 and 45℃. The amino terminal sequences of lipase Ⅰ and lipase Ⅱ, determined by Edman degradation, were found to be Leu-Val-Met-Ile-Gln-Arg and Leu-Val-Met-Lys-Gln-Arg, respectively. By western blotting analysis, the two lipases were found to have a common antigenic determinant. Immuno-electron cytochemistry conducted with polyclonal anti-lipase I antibody indicated the enzyme located in both the periplasm and the adjacent vesicles of fungal hyphae. Fortunately, the sites on the cell envelope where lipase was exported into the culture medium was also identified.
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