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

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.

SUBMITTER: Zisis T 

PROVIDER: S-EPMC4697882 | biostudies-literature | 2015 Sep

REPOSITORIES: biostudies-literature