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Biotechnology and Applied Biochemistry (2003) 37, (63–71) (Printed in Great Britain)

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Review

Lipase assays for conventional and molecular screening: an overview

Rani Gupta¹, Pooja Rathi, Namita Gupta and Sapna Bradoo²

Department of Microbiology, University of Delhi South Campus, Benito Juarez Road, New Delhi 110 021, India

Key words: esterolytic, fatty acid, hydrolase, lipid, lipolytic.

¹To whom correspondence should be addressed (e-mail microzyme@123india.com).

²Present address: Biotechnology Department, Center for Chemistry and Chemical Engineering, Lund University, Box 124, SE 22100, Lund, Sweden.

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.

Received 17 June 2002/22 October 2002; accepted 31 October 2002

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