Characteristics of lipase‐catalyzed hydrolysis of olive oil in AOT–isooctane reversed micelles
- 31 July 1986
- journal article
- research article
- Published by Wiley in Biotechnology & Bioengineering
- Vol. 28 (8), 1250-1255
- https://doi.org/10.1002/bit.260280817
Abstract
Candida rugosa lipase solubilized in organic solvents in the presence of both surfactant and water could catalyze the hydrolysis of triglycerides, and kinetic analysis of the lipase-catalyzed reaction was found to be possible in this system. Among eight organic solvents tested, isooctane was most effective for the hydrolysis of olive oil in reversed micelles. Temperature effect, pH profile, Km,app and Vmax,app were determined. Among various chemical compounds, Cu2+, Hg2+, and Fe3+ inhibited lipase severely. But the enzyme activity was restorable partially by adding histidine or glycine to the system containing these metal ions. The enzyme activity was dependent on R (molar ratio of water to surfactant) and maximum activity was obtained at R = 10.5. Upon addition of glycerol to the reversed micelles, lipase activity was affected in a different fashion depending on the R values. Stability of the lipase in reversed micelles was also dependent on R, and it was most stable at R = 5.5.This publication has 23 references indexed in Scilit:
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