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PROPERTIES AND PARTIAL PURIFICATION OF A PSEUDOMONAS CEPACIA LIPASE
Dünhaupt, A. Lang, S. Wagner, Fritz
Dünhaupt, A.
Lang, S.
Wagner, Fritz
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Issue Date
1991
Submitted date
2024-03-27
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Abstract
A high lipolytic activity (65 umol/ml min.) was observed in the supernatant of Pseudomonas cepacia DSM 50181 after growth on olive oil. The crude lipase was investigated with respect to substrate specifity, pH- and temperature optima. The hydrolysis of short chain triglycerides and of the unsaturated triolein indicated a higher lipolytic activity than in the case of long chain substances (37°C). The p-nitrophenyl- esters of fatty acids showed maximum activity for the palmitate. This was the same maximum which was observed for triglycerides in the range from C12 to C18 at 75°C. An inhibition of lipolytic activity was noticed by adding oleic acid during the hydrolysis of olive oil. Furthermore an inactivation of the lipase occured when the interface liquid/gaseous was increased. The addition of an inert lipophilic substance or of detergents could neutralize this effect. A partial purification of the lipolytic enzyme could be achieved by liquid/liquid extraction and ionexchangechromatography. This enrichment procedures led to a purification factor of 55 with a recovery of 30%. Isoelectric focussing showed a main protein band at pl 7.1.
Citation
Lipases : structure, mechanism and genetic engineering, 389 - 392
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Book chapter
conference paper
conference paper
Language
en
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Series/Report no.
GBF monographs ; Volume 16
ISSN
0930-4320
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ISBN
156081165X
3527283323
3527283323
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Attribution-NonCommercial-ShareAlike 4.0 International