Interfacial Activation of Candida antarctica Lipase B: Combined Evidence from Experiment and Simulation

Biochemistry
Themistoklis ZisisKerstin Blank

Abstract

Lipase immobilization is frequently used for altering the catalytic properties of these industrially used enzymes. Many lipases bind strongly to hydrophobic surfaces where they undergo interfacial activation. Candida antarctica lipase B (CalB), one of the most commonly used biocatalysts, is frequently discussed as an atypical lipase lacking interfacial activation. Here we show that CalB displays an enhanced catalytic rate for large, bulky substrates when adsorbed to a hydrophobic interface composed of densely packed alkyl chains. We attribute this increased activity of more than 7-fold to a conformational change that yields a more open active site. This hypothesis is supported by molecular dynamics simulations that show a high mobility for a small "lid" (helix α5) close to the active site. Molecular docking calculations confirm that a highly open conformation of this helix is required for binding large, bulky substrates and that this conformation is favored in a hydrophobic environment. Taken together, our combined approach provides clear evidence for the interfacial activation of CalB on highly hydrophobic surfaces. In contrast to other lipases, however, the conformational change only affects large, bulky substrates, leading t...Continue Reading

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Citations

Feb 19, 2016·Chemical Reviews·Elena PapaleoRuth Nussinov
Jul 13, 2016·Molecular Simulation·Jayangika N DahanayakeKatie R Mitchell-Koch
May 18, 2016·Applied Biochemistry and Biotechnology·Viviane ChiaradiaClaudia Sayer
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