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Study of a Lipase fromCandida rugosa Diddens and Lodder

✍ Scribed by Ratomahenina, R. ;Riaublanc, A. ;Galzy, P.

Publisher
John Wiley and Sons
Year
1993
Weight
351 KB
Volume
95
Category
Article
ISSN
0931-5985

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✦ Synopsis

B y A . R i a u b l a n c , R. R a r o m a h e n i n a andf! G a l z y *

Lipasic system of Cnndida rugosn (CBS 613) strain was studied. The enzyme was purified in one step by hydrophobic chromatography. The properties of this lipase were determined. It is an oligomeric enzyme composed of five identical monomers of 46 kg . rnol-'. Its optimum reaction conditions are p H = 7 and temperature = 40Β°C. This enzyme presents a rapid thermal denaturation and then a more stable form. It is a cell-bound lipase which is induced by triacyl glycerols. This enzyme presents a high specificity for external positions on glycerol.

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