Effect of cyclic and acyclic surfactants on the activity of Candida rugosa lipase
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RESEARCH PAPER
Effect of cyclic and acyclic surfactants on the activity of Candida rugosa lipase Elif Ozyilmaz1 · Filiz Eski2 Received: 8 February 2020 / Accepted: 23 June 2020 © Springer-Verlag GmbH Germany, part of Springer Nature 2020
Abstract The active site of Candida rugosa lipase (CRL) is mainly hydrophilic on its external face and hydrophobic on the internal side, and calix[n]arene-based surfactants form complexes with protein residues or with strong hydrogen bonds to open up the lid. Therefore, the activity of lipase persists for a long time. In this work, a series of cyclic and acyclic anionic surfactants (sodium dodecyl sulfate (SDS), p-sulfonatocalix[4]arene, and p-sulfonatocalix[8]arene) and zwitterionic surfactants (l-proline and l-proline derivative of calix[4]arene) were used to examine the relationship between the surfactants’ molecular structures and their effects on the hydrolytic activity of CRL. We explored the effects of different surfactant concentrations, ring effects, and mixing times on CRL activity and several kinetic parameters. The results demonstrated that cyclic compounds were more effective than linear structures for increasing CRL activity and the highest enzyme activity was obtained by the addition of the calix[4]-l-proline derivative. This zwitterionic compound (calix[4]-l-proline derivative) maintains the active center of enzyme and conformation by enabling electrostatic interactions and hydrogen bonding with both the acidic and basic amino acid groups in the structure of the enzyme. The results indicated that, compared with the other surfactants, activating CRL with calix[4]-l-proline resulted in hyperactivation at all concentrations (a relative increase of 230%). Keywords Surfactant · Lipase · Activity · p-Sulfonatocalix[n]arene
Introduction Lipase (EC 3.1.1.3) is one of the most important industrial biocatalysts and is used to catalyze many different reactions including hydrolysis, esterification, transesterification, alcoholysis, acidolysis and aminolysis.[1–3]. Therefore, this enzyme is among the most widely used enzymes in the chemical, pharmaceutical, and food industries [4, 5]. Lipases carry out their catalytic actions at the substrate–water interface of heterogeneous reaction systems. It is known that the activity of these enzymes depends on the interfacial Electronic supplementary material The online version of this article (https://doi.org/10.1007/s00449-020-02397-3) contains supplementary material, which is available to authorized users. * Elif Ozyilmaz [email protected] 1
Department of Biochemistry, Selcuk University, 42075 Konya, Turkey
Department of Chemistry, Selcuk University, 42075 Konya, Turkey
2
concentration of the substrates [6]. A number of studies have examined enzymes that function at these interfaces and the effects of enzyme activity of surfactants [7]. Surfactants can affect the secondary and tertiary structure and flexibility of lipase and, thus, affect its ability to work as a biocatalyst [6]. Although significant progress has bee
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