Enzymatic Catalytic Promiscuity and the Design of New Enzyme Catalyzed Reactions

Bornscheuer, Uwe T.; Kazlauskas, Romas J.

doi:10.1002/9783527639861.ch41

Cited by 7 publications

(6 citation statements)

References 178 publications

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“…Interestingly, lipase capability for working in solvents different from water was described as a "promiscuous behavior" (Arora et al, 2014;Asler et al, 2010;Babtie et al, 2010;Bornscheuer and Kazlauskas, 2012;Brodzka et al, 2018;Busto et al, 2010;Carbonell and Faulon, 2010;Copley, 2017;Gatti-Lafranconi and Hollfelder, 2013;Gerlt, 2004;Green et al, 2010;Hult and Berglund, 2007;Humble and Berglund, 2011;Kapoor and Gupta, 2012;Kazlauskas, 2005;Khersonsky et al, 2006;Khersonsky and Tawfik, 2010;Lathe et al, 2015;Lopez-Iglesias and Gotor-Fernandez, 2015;O'Brien and Herschlag, 1999;Ondari and Walker, 2009;Sheldon and Brady, 2018;Xu and Lin, 2007).…”

Section: Accepted Manuscriptmentioning

confidence: 99%

Immobilization of lipases on hydrophobic supports: immobilization mechanism, advantages, problems, and solutions

Rodrigues

Virgen-Ortíz

Santos

et al. 2019

Biotechnology Advances

451

291

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Lipases are the most widely used enzymes in biocatalysis, and the most utilized method for enzyme immobilization is using hydrophobic supports at low ionic strength. This method allows the one step immobilization, purification, stabilization, and hyperactivation of lipases, and that is the main cause of their popularity. This review focuses on these lipase immobilization supports. First, the advantages of these supports for lipase immobilization will be presented and the likeliest immobilization mechanism (interfacial activation on the support surface) will be revised. Then, its main shortcoming will be discussed: enzyme desorption under certain conditions (such as high temperature, presence of cosolvents or detergent molecules). Methods to overcome this problem include physical or chemical crosslinking of the immobilized enzyme molecules or using heterofunctional supports. Thus, supports containing hydrophobic acyl chain plus epoxy, glutaraldehyde, ionic, vinylsulfone or glyoxyl groups have been designed. This prevents enzyme desorption and improved enzyme stability, but it may have some limitations, that will be discussed and some additional solutions will be proposed (e.g., chemical amination of the enzyme to have a full covalent enzyme-support reaction). These immobilized lipases may be subject to unfolding and refolding strategies to reactivate inactivated enzymes. Finally, these biocatalysts have been used in new strategies for enzyme coimmobilization, where the most stable enzyme could be reutilized after desorption of the least stable one after its inactivation.

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Section: Accepted Manuscriptmentioning

confidence: 99%

Immobilization of lipases on hydrophobic supports: immobilization mechanism, advantages, problems, and solutions

Rodrigues

Virgen-Ortíz

Santos

et al. 2019

Biotechnology Advances

451

291

View full text Add to dashboard Cite

show abstract

“…[9] In principle, however, the mechanism of silicatein activity on SiÀ O bonds proposed by Zhou et al is transferable to the active site of lipases; the condensation of silyl ethers proceeds analogously to ester formation with silanol serving as the nucleophile. [3] Therefore, we concluded from our previous results that the turnover of silyl-protected alcohols occurs in the active site of lipases, but is limited by the molecular size. This agreed with the observation, that the studied enzymes also converted bulky esters with no or very low activity.…”

Section: Introductionmentioning

confidence: 86%

“…The ability of some enzymes to interact with SiÀ O bonds has been reported for quite some time: [3] In 1989, Michel Therisod described the transesterification of a silyl ether and butyric acid ethyl ester to ethoxy-trimethylsilane in the presence of lipases. [4] Ten years later, Cha et al isolated the cathepsin-L-like silicateine-α from marine sponges and showed its ability to polymerize silica.…”

Section: Introductionmentioning

confidence: 99%

Lipase‐Mediated Conversion of Protecting Group Silyl Ethers: An Unspecific Side Reaction

Pick,

Wenzlaff,

Yousefi

et al. 2023

ChemBioChem

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Silyl ether protecting groups are important tools in organic synthesis, ensuring selective reactions of hydroxyl functional groups. Enantiospecific formation or cleavage could simultaneously enable the resolution of racemic mixtures and thus significantly increase the efficiency of complex synthetic pathways. Based on reports that lipases, which today are already particularly important tools in chemical synthesis, can catalyze the enantiospecific turnover of trimethylsilanol (TMS)‐protected alcohols, the goal of this study was to determine the conditions under which such a catalysis occurs. Through detailed experimental and mechanistic investigation, we demonstrated that although lipases mediate the turnover of TMS‐protected alcohols, this occurs independently of the known catalytic triad, as this is unable to stabilize a tetrahedral intermediate. The reaction is essentially non‐specific and therefore most likely completely independent of the active site. This rules out lipases as catalysts for the resolution of racemic mixtures of alcohols through protection or deprotection with silyl groups.

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“…Enzymes in nature use their bespoke binding environments to catalyse reactions with extreme selectivity; however, there are only a limited number of reactions that occur in nature where this is possible [166]. One method to extend their reactivity is to use them in combination with photocatalysis.…”

Section: Enzyme Catalysismentioning

confidence: 99%

Recent developments in enantioselective photocatalysis

Prentice¹,

Morrisson²,

Smith³

et al. 2020

Beilstein J. Org. Chem.

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Enantioselective photocatalysis has rapidly grown into a powerful tool for synthetic chemists. This review describes the various strategies for creating enantioenriched products through merging enantioselective catalysis and photocatalysis, with a focus on the most recent developments and a particular interest in the proposed mechanisms for each. With the aim of understanding the scope of each strategy, to help guide and inspire further innovation in this field.

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Enzymatic Catalytic Promiscuity and the Design of New Enzyme Catalyzed Reactions

Cited by 7 publications

References 178 publications

Immobilization of lipases on hydrophobic supports: immobilization mechanism, advantages, problems, and solutions

Immobilization of lipases on hydrophobic supports: immobilization mechanism, advantages, problems, and solutions

Lipase‐Mediated Conversion of Protecting Group Silyl Ethers: An Unspecific Side Reaction

Recent developments in enantioselective photocatalysis

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