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Screening of solvents for favoring hydrolytic activity of Candida antarctica Lipase B

  • Bartłomiej ZieniukEmail author
  • Agata Fabiszewska
  • Ewa Białecka-Florjańczyk
Research Paper
  • 48 Downloads

Abstract

Lipases are a group of enzymes of considerable significance in organic synthesis, among which Candida antarctica lipase B (CALB) is one of the most widely studied enzymes. The activity of the biocatalyst has been intensively characterized in many organic media, but this paper aimed to compare the effect of 20 different solvents on the activity of CALB in the hydrolysis of p-nitrophenyl laurate. Nonpolar, polar aprotic, and polar protic solvents were used for enzyme pretreatment and then entered the composition of mixed solvents reaction medium. An impact of solvents on solvation processes affecting the catalysis steps, protein denaturation, and changes of its conformation was discussed. Moreover the hydrolytic activity of CALB with partition coefficient (logP) of the solvent used was correlated. It was emphasized that the substrate solubility plays an important role in solvent selection. In the presence of hydrophobic solvents, hydration layer becomes more hydrophobic facilitating the substrate access to the enzyme surface. In turn, polar compounds are good solvents for organic substrates facilitating the penetration of the aqueous layer that surrounds the surface of the enzyme. Two variants proved to be favorable for ester hydrolysis reaction: isooctane or polar solvent such as acetone, tert -butyl methyl ether, tert-butanol or acetonitrile.

Keywords

Candida antarctica lipase B Organic solvent Lipase activity logP 

Notes

Author contributions

BZ and EB-F: conceptualization; BZ: investigation; BZ and AF: methodology; BZ, AF, and EB-F: writing—original draft preparation; EB-F: supervision.

Compliance with ethical standards

Conflict of interest

The authors declare that they have no conflict of interest. This research did not receive any specific grant from funding agencies in the public, commercial, or not-for-profit sectors.

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Copyright information

© Springer-Verlag GmbH Germany, part of Springer Nature 2019

Authors and Affiliations

  1. 1.Department of Chemistry, Institute of Food SciencesWarsaw University of Life SciencesWarsawPoland

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