Engineering of Candida antarctica lipase B for hydrolysis of bulky carboxylic acid esters

Juhl, P. Benjamin; Doderer, Kai; Hollmann, Frank; Thum, Oliver; Pleiss, Jürgen

doi:10.1016/j.jbiotec.2010.09.951

Cited by 58 publications

(33 citation statements)

References 43 publications

(53 reference statements)

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“…Gene cloning in heterologous overexpressing hosts (Parra et al 2008;Xuezheng et al 2010;Novototskaya-Vlasova et al 2013), crystal studies (Uppenberg et al 1995;Juhl et al 2010;Durmaz et al 2013) and molecular modelling studies (Maraite et al 2013;Mohamad Ali et al 2013) strongly supports the structural attributes of cold-adapted lipases for cold habitation discussed above.…”

Section: Structural Features and Cold Adaptionmentioning

confidence: 57%

Cold active lipases – an update

Kavitha

2016

Frontiers in Life Science

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Cold active lipases (CLPs) are gaining importance nowadays as they are increasingly used in fine chemical synthesis, bioremediation, food processing and as detergent additive. These enzymes exhibit high catalytic activity at low temperatures and flexibility to act at low water medium. Since they are active at low temperatures consume less energy and also stabilize fragile compounds in the reaction medium. CLPs are commonly obtained from psychrophilic microorganisms which thrive in cold habitats. Compared to mesophilic and thermophilic lipases, only a few CLPs were studied and industrially exploited so far. CLPs (C. antarctica lipase-A and C. antarctica lipase-B) from Candida antarctica isolated from Antarctic region are the well studied and industrially employed, and many are being followed up. This review updates the CLPs reported recently and the industrial applications of CLPs. ARTICLE HISTORY

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Section: Structural Features and Cold Adaptionmentioning

confidence: 57%

Cold active lipases – an update

Kavitha

2016

Frontiers in Life Science

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“…18 More importantly, it has enabled the rational redesign of the CalB active site with the goal of altering its substrate specificity. 19-22 …”

Section: Introductionmentioning

confidence: 99%

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

et al. 2015

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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 to the conclusion that CalB acts like an esterase for small substrates and as a lipase for substrates with large alcohol substituents.

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“…Among the nine predicted variants only one displayed higher activity than the wild type against branched acids but not against sterically demanding acids. This work shows the potential of in silico approaches to predict mutant variants, thus reducing the time-consuming high throughput screening assays [87]. …”

Section: Substrate Scopementioning

confidence: 99%