Lipase assays for conventional and molecular screening: an overview
- 1 February 2003
- journal article
- review article
- Published by Wiley in Biotechnology and Applied Biochemistry
- Vol. 37 (1) , 63-71
- https://doi.org/10.1042/ba20020059
Abstract
Lipases are versatile biocatalysts that can perform innumerable different reactions. Their enantio‐, chemo‐ and stereo‐selective nature makes them an important tool in the area of organic synthesis. Unlike other hydrolases that work in aqueous phase, lipases are unique as they act at the oil/water interface. Besides being lipolytic, lipases also possess esterolytic activity and thus have a wide substrate range. Hence, the lipase assay protocols hold a significant position in the field of lipase research. Lipase activity can be estimated using a wide range of assay protocols that differ in terms of their basic principle, substrate selectivity, sensitivity and applicability. As the value of these enzymes continues to grow and new markets are exploited, development of new or improved enzymes will be a key element in the emerging realm of biotechnology. Hence, development of faster and simpler protocols incorporating newer and more specific substrates is the need of the hour. In this endeavour, methods that could be adopted for molecular screening occupy an important position. Here, an overview of the lipase assay protocols is presented with emphasis on the assays that can be adopted for the molecular screening of these biocatalysts.Keywords
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