Isolation and partial characterization of a lipase from jackfruit (Artocarpus heterophyllus Lam.) latex

Date

4-2005

Degree

Bachelor of Science in Chemistry

College

College of Arts and Sciences (CAS)

Adviser/Committee Chair

Eugenia M. Castillo

Abstract

Using ammonium sulfate fractionation at 90% saturation, a lipase from jackfruit (Artocarpus heterophyllus Lam.) latex was isolated and further purification was done using Sephadex G-100 gel filtration chromatography.  The partially purified lipase was then characterized in terms of pH, temperature, incubation time and kinetic parameters.  The optimum pH and temperature was observed at 5.0 and 45 oC, respectively and the lipase showed the highest activity at an incubation fold of time of 20 minutes.  The partially purified lipase has purification fold of 39 times that that of the crude extract and a specific activity of 35.058 U/mg.

Kinetic studies using the Lineweaver-Burk plot of the partially purified lipase showed a maximal velocity (Vmax) of 14.13 molar/min and Michaelis-Menten (km) equal to 20.02 molar.

Language

English

Location

UPLB Main Library Special Collections Section (USCS)

Call Number

Thesis

Document Type

Thesis

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