Purification and Characterization of a Lipase from Candida curvata Lodder and Kreger — van Rij CBS 570
✍ Scribed by Montet, D. ;Ratomahenina, R. ;Pina, M. ;Graille, J. ;Galzy, P.
- Publisher
- John Wiley and Sons
- Year
- 1985
- Weight
- 474 KB
- Volume
- 87
- Category
- Article
- ISSN
- 0931-5985
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✦ Synopsis
Kregervan Rij CBS 570
ByD. M o n t e t , R . R a t o m a h e n i n a , M . P i n a , J . G r a i l l e andR G a l s y *
The purification of the lipase from Condido curvatu CBS 570 was achieved in three steps. Its optimum pH is 6 and its optimum temperature range is 500Cto600 C.Thisenzyme is thermoresistantandonlyloses20%ofitsactivity when heated at 500 C during 30 minutes. Its activation energy is 14.4 kcal/mole and its inactivation energy 22 kcal/mole. Its molecular weight was determined to be 195000. EDTA, pchloromemri benzoate, N-ethylmdeimide and iodoacetamide have no influence on the activity of this enzyme, whereas Cu++ and Zn++ show strong inhibitory effects.The lipase activity is induced by the presence of triglycerides and inhibited by the presence of glucose. This enzyme strongly attacks triolein and trilinolein molecules, however it only hydrolyzes a little tristearin and trilinolenin.