Abstract

Ubiquitous in nature, lipases represent an example of enzymes with high versatility. Plant seeds are potential sources of lipase, and they are attracting more attention for specific purposes. In this study, coconut lipase was isolated from germinating coconut seed. Biochemical characterization of coconut lipase was undertaken to reveal its substrate specificity and its subunits properties. By using various chromogenic ester of fatty acids, it was demonstrated that lauric acid is the most preferred substrate for coconut lipase esterase reaction. Calcium ions enhance its activity, whereas other metal ions such as magnesium, nickel, sodium, and potassium reduce it. Electrophoresis under native conditions showed that coconut lipase is a single protein. Since electrophoresis under denaturing conditions revealed four subunits, coconut lipase is likely a complex enzyme. It was further revealed that all subunits are active, as evident in an in-gel hydrolysis assay. However, they also hint that they do not have an equal catalytic rate against the 16-carbon-length palmitate derivative. This finding, thus, opens up a notion that those subunits have different substrates specificity yet to be determined.

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