Engineering a lipase B from Candida antactica with efficient perhydrolysis performance by eliminating its hydrolase activity

Wang, Xu Ping; Zhou, Peng; Li, Zhi Gang; Yang, Bo; Hollmann, Frank; Wang, Yong Hua

doi:10.1038/srep44599

Cited by 19 publications

(13 citation statements)

References 24 publications

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“…42 The heterogeneity of the natural substrate [43][44][45][46][47][48] has converted lipases in enzymes with a very broad specificity, accepting substrates very different from glycerides (even amides). Thus, lipases are used in vitro to catalyze reactions different from those of the natural hydrolase function, [49][50][51][52][53][54] such as esterification, [55][56][57][58][59][60][61] acidolysis, [62][63][64][65][66][67] interesterificaton, [68][69][70][71] transesterification, [72][73][74][75][76] aminolysis, [77][78][79][80][81] perhydrolysis, 82,83 etc., together with a collection of the so-called promiscuous reactions. [84][85][86][87][88]...…”

Section: Lipases In Biocatalysismentioning

confidence: 99%

Novozym 435: the “perfect” lipase immobilized biocatalyst?

Ortíz

Ferreira

Barbosa

et al. 2019

Catal. Sci. Technol.

471

360

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Section: Lipases In Biocatalysismentioning

confidence: 99%

Novozym 435: the “perfect” lipase immobilized biocatalyst?

Ortíz

Ferreira

Barbosa

et al. 2019

Catal. Sci. Technol.

471

360

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“…This may be addressed either by protein engineering159 or by solvent engineering 159c, 160. The scope of this reaction is very broad, and many (cyclo)alkanones can be converted in high yields 88b, 161…”

Section: Oxidation Of Aldehydes and Ketonesmentioning

confidence: 99%

Biocatalytic Oxidation Reactions: A Chemist's Perspective

et al. 2018

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Oxidation chemistry using enzymes is approaching maturity and practical applicability in organic synthesis. Oxidoreductases (enzymes catalysing redox reactions) enable chemists to perform highly selective and efficient transformations ranging from simple alcohol oxidations to stereoselective halogenations of non‐activated C−H bonds. For many of these reactions, no “classical” chemical counterpart is known. Hence oxidoreductases open up shorter synthesis routes based on a more direct access to the target products. The generally very mild reaction conditions may also reduce the environmental impact of biocatalytic reactions compared to classical counterparts. In this Review, we critically summarise the most important recent developments in the field of biocatalytic oxidation chemistry and identify the most pressing bottlenecks as well as promising solutions.

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“…Additionally, it has been described that many lipases can use hydrogen peroxide as an oxidant, which is preferred due to its low environmental impact. 16,20,21 One of the best-characterized enzymes in this field is Candida antarctica lipase B (CALB). CALB is widely used in industries and has served as a model to study enzyme promiscuity, either by experimental or theoretical approaches.…”

Section: ■ Introductionmentioning

confidence: 99%

Computational Studies Suggest Promiscuous Candida antarctica Lipase B as an Environmentally Friendly Alternative for the Production of Epoxides

Galmés

Świderek

Moliner

2021

J. Chem. Inf. Model.

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Environmentally friendly processes are nowadays a trending topic to get highly desired chemical compounds and, in this sense, the use of enzyme-catalyzed routes is becoming a promising alternative to traditional synthetic methods. In the present paper, a hybrid quantum mechanics/molecular mechanics (QM/MM) computational study on the epoxidation of alkenes catalyzed by the Ser105Ala variant of the promiscuous Candida antarctica lipase B (CALB) is presented in an attempt to search for alternative paths to get useful intermediates in industries. The catalyzed reaction, described at the atomistic level with a model of the full solvated in a box of water molecules, is compared with the alternative epoxidation of alkenes by peroxy acids in chloroform. Freeenergy profiles obtained at the density functional theory (DFT)/MM level show how Ser105Ala CALB is capable of epoxide short alkenes in a twostep process with free-energy barriers, in agreement with available experimental data, that are significantly lower than those of the single-step reaction in solution. The possible (R)-enantioselectivity dictated by the binding step, explored by means of alchemical QM/MM free-energy perturbation (FEP) methods, and the preference for the (S)-enantiomer derived from the free-energy landscape of the chemical steps would cancel out, thus predicting the lack of enantioselectivity experimentally observed. In general, our results provide general information on the molecular mechanism employed by a highly promiscuous enzyme, with potential applications in biotechnology.

show abstract

Engineering a lipase B from Candida antactica with efficient perhydrolysis performance by eliminating its hydrolase activity

Cited by 19 publications

References 24 publications

Novozym 435: the “perfect” lipase immobilized biocatalyst?

Novozym 435: the “perfect” lipase immobilized biocatalyst?

Biocatalytic Oxidation Reactions: A Chemist's Perspective

Computational Studies Suggest Promiscuous Candida antarctica Lipase B as an Environmentally Friendly Alternative for the Production of Epoxides

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