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Kinetic studies of Mucor miehei lipase in phosphatidylcholine microemulsions

✍ Scribed by A. C. Oliveira; J. M. S. Cabral

Publisher
Wiley (John Wiley & Sons)
Year
2007
Tongue
English
Weight
495 KB
Volume
56
Category
Article
ISSN
0268-2575

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✦ Synopsis

Ethanol-oleic acid esterification by a free and microencapsulated lipase from Mucor miehei, using dodecane as solvent and phosphatidylcholine as surfactant, was studied.

The initial esterification rate was influenced by the water content in the biphasic system. Kinetic studies with free and microencapsulated enzyme showed that the microencapsulation led to an increase of the kinetic parameters (V,,, and K,), probably due to an increase of the interfacial area. The reaction rate was also affected by the shaking rate, the temperature and the pH. The optimal temperature and pH achieved were, respectively, 40°C and 4.5 using free enzyme, and 50°C and 6 using microencapsulated enzyme.

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