Microbial lipases: At the interface of aqueous and non-aqueous media: A review

58Citations
Citations of this article
67Readers
Mendeley users who have this article in their library.

Abstract

In recent times, biotechnological applications of microbial lipases in synthesis of many organic molecules have rapidly increased in non-aqueous media. Microbial lipases are the working horses' in biocatalysis and have been extensively studied when their exceptionally high stability in non-aqueous media has been discovered. Stability of lipases in organic solvents makes them commercially feasibile in the enzymatic esterification reactions. Their stability is affected by temperature, reaction medium, water concentration and by the biocatalyst's preparation. An optimization process for ester synthesis from pilot scale to industrial scale in the reaction medium is discussed. The water released during the esterification process can be controlled over a wide range and has a profound effect on the activity of the lipases. Approaches to lipase catalysis like protein engineering, directed evolution and metagenome approach were studied. This review reports the recent development in the field of non-aqueous microbial lipase catalysis and factors controlling the esterification/transesterification processes in organic media. © 2008 Akadémiai Kiadó.

Cite

CITATION STYLE

APA

Verma, M. L., Azmi, W., & Kanwar, S. S. (2008). Microbial lipases: At the interface of aqueous and non-aqueous media: A review. Acta Microbiologica et Immunologica Hungarica, 55(3), 265–294. https://doi.org/10.1556/AMicr.55.2008.3.1

Register to see more suggestions

Mendeley helps you to discover research relevant for your work.

Already have an account?

Save time finding and organizing research with Mendeley

Sign up for free