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PURIFICATION AND SUBSTRATE SPECIFICITIES OF LIPASES FROM GEOTRICHUM CANDIDUM
Charton, E. Davies, C. Sidebottom, C. M. Sutton, J. L. Dunn, P. P. J. Slabas, A. R. Macrae, A. R.
Charton, E.
Davies, C.
Sidebottom, C. M.
Sutton, J. L.
Dunn, P. P. J.
Slabas, A. R.
Macrae, A. R.
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Issue Date
1991
Submitted date
2024-03-27
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Abstract
Two strains of the mould Geotrichum candidum (ATCC 34614 and CMICC 335426) each produce two extracellular lipases. We have purified the four lipases to electrophoretic homogeneity and each is a single species when analysed by isoelectric focusing. The enzymes are glycosylated and have similar molecular weights and isoelectric points. Peptide mapping and Western blotting shows that the lipases are related and this has been confirmed by amino acid analysis. We have examined the substrate specificities of the two lipases using triacylglycerols and fatty acid methyl esters as substrates. One lipase is highly specific for the release of cis-A9-fatty acids from these substrates. In contrast, the other 3 lipases are not specific, releasing both saturated and unsaturated fatty acids.
Citation
Lipases : structure, mechanism and genetic engineering, 335 - 338
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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