Abstract
A simple, rapid and precise method has been developed for determination of lipase activity in microbial media. The method is based on using phenyl acetate as substrate for lipase and determination of liberated phenol by Folin Ciocalteu reagent. Reaction mixture containing substrate 2.4 ml of phenyl acetate 165 μM in Tris HCl buffer, 0.1 M and pH 7, with 1% (v/v) Triton X-100) and 0.1 ml lipase is incubated at 40?C during 10 minutes and the absorbance was measured at 750 nm. Linearity was observed in the concentration range 0-0.8 g/L lipase.
Highlights
Lipases are one of the most important classes in biotechnology that can catalyze the hydrolysis of ester bond at the lipid and water interface [1]
Reaction mixture containing substrate 2.4 ml of phenyl acetate 165 μM in Tris HCl buffer, 0.1 M and pH 7, with 1% (v/v) Triton X-100) and 0.1 ml lipase is incubated at 40 ̊C during 10 minutes and the absorbance was measured at 750 nm
We investigated a new method to determine the lipase activity starting with phenyl acetate that is low price commercially available
Summary
Lipases (triacylglycerol acylhydrolases, E.C. 3.1.1.3) are one of the most important classes in biotechnology that can catalyze the hydrolysis of ester bond at the lipid and water interface [1]. It is important to determine the lipase activity by a simple and rapid method to select the best condition for the production. Several methods have been developed for the determination of lipase activity, only two methods are commonly used in the literatures. The first one is the titrimetric method using olive oil as substrate. This method depends on the determination of the liberated fatty acids by titration against potassium hydroxide [3]. The second method is the colorimetric method using p-nitrophenyl palimitate as a substrate and determines the lipase activity by measuring the amount of the yellow chromogen (p-nitrophenol) resulting from the hydrolysis of the substrate [4]
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