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Partial purification and some properties of the lipase present in oil palm ( Elaeis guineensis ) mesocarp
Author(s) -
Abigor Doye R.,
Opute Fred I.,
Opoku Andy R.,
Osagie Anthony U.
Publication year - 1985
Publication title -
journal of the science of food and agriculture
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.782
H-Index - 142
eISSN - 1097-0010
pISSN - 0022-5142
DOI - 10.1002/jsfa.2740360711
Subject(s) - lipase , chemistry , elaeis guineensis , chromatography , glycerol , fractionation , lecithin , size exclusion chromatography , ammonium , palm oil , food science , enzyme , biochemistry , organic chemistry
The fatty layer obtained by centrifuging a homogenate of oil palm fruit mesocarp contains an active lipase. The lipase which was partially purified using a combination of ammonium sulphate fractionation, ion exchange and gel filtration chromatography, indicated an optimum activity at pH 4.5 and a temperature of 30°C. The enzyme exhibited good activity towards its natural substrate, palm oil as well as glycerol trioleate and glycerol tripalmitate. It also showed a linear reaction rate for the first 20 min of incubation. Sodium cyanide, resorcinol, cholesterol, lecithin and glycylglycine strongly inhibited its activity while phenol, L‐cysteine and EDTA enhanced its activity. It is suggested that the lipase is associated with the membrane of the oil droplets.