A convenient test for lipase activity in aqueous-based solutions

Enzyme and Microbial Technology
Jin GuoXiao-Jun Huang

Abstract

We proposed a convenient and accurate method for the measurement of lipase activity in a uniform aqueous-based substrate solution. In this work, lipase from Candida rugosa was used as the model lipase to test its catalytic ability toward p-nitrophenyl palmitate (p-NPP), which was suspended in a mixture of p-NPP ethanol solution and buffer. An ultraviolet-visible spectrophotometer was used to efficiently measure the liberated p-nitrophenol without extraction or centrifugation. Several factors that affected lipase activity were investigated, such as the ratio of p-NPP ethanol solution to buffer, the concentrations of p-NPP and lipase, as well as the temperature, reaction time, pH and agitation rate. Additionally, enzyme catalytic parameters such as Km, Vm and "activation energy" were also assessed. We determined the optimal conditions for lipase in this homogeneous system and demonstrated lipase's catalytic performance in this condition followed Michealis-Menten kinetics.

References

Jul 19, 2000·Enzyme and Microbial Technology·A L PaivaF X Malcata
Feb 14, 2013·Chemical Society Reviews·Patrick Adlercreutz

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Citations

May 19, 2017·The Journal of Biological Chemistry·Khundrakpam Herojit SinghBichitra Kumar Biswal
Feb 3, 2021·Daru : Journal of Faculty of Pharmacy, Tehran University of Medical Sciences·Saeid GhofraniDariush Norouzian
Dec 14, 2018·Organic Letters·Emese FarkasLászló Poppe
Nov 18, 2021·Journal of Agricultural and Food Chemistry·Lei KuangHuafeng Tian

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