Substrate-induced stability of the lipase from Candida cylindracea in reversed micelles

Activity of lipase (candida cylindracea) in reversed micelles was found to be sustained over extended periods of time in the presence of amphiphilic substrates. Esterification of palmitic or oleic acid and octanol was studied to characterize the lipase activity in AOT/isooctane reversed micelles. Co...

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Bibliographic Details
Published in:Biotechnology letters 1995-02, Vol.17 (2), p.177-182
Main Authors: Ayyagari, M.S, John, V.T
Format: Article
Language:English
Subjects:
alcohols
Bioconversions. Hemisynthesis
Biological and medical sciences
Biotechnology
Candida cylindracea
enzyme activity
esterification
Fundamental and applied biological sciences. Psychology
Methods. Procedures. Technologies
micelles
octanol
oleic acid
palmitic acid
stability
triacylglycerol lipase
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Summary:Activity of lipase (candida cylindracea) in reversed micelles was found to be sustained over extended periods of time in the presence of amphiphilic substrates. Esterification of palmitic or oleic acid and octanol was studied to characterize the lipase activity in AOT/isooctane reversed micelles. Complete conversion was possible even in the presence of stoichiometric excess of water. In the absence of acyl substrates, the enzyme lost all its activity within a few hours in reversed micelles. Thermal effects on the enzyme activity were studied, and the enzyme stability in reversed micelles was compared to that in a bulks organic solvent.
ISSN:0141-5492
1573-6776
DOI:10.1007/BF00127984