Exploring the Biocatalytic Scope of a Novel Enantioselective Halohydrin Dehalogenase from an Alphaproteobacterium

Xue, Feng; Ya, Xiangju; Xiu, Yuansong; Tong, Qi; Wang, Yuqi; Zhu, Xinhai; Huang, He

doi:10.1007/s10562-019-02659-0

Cited by 9 publications

(3 citation statements)

References 36 publications

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“…As HHDHs were first discovered in the context of enzymes related to the degradation of epihalohydrins, these are the compounds occurring in many studies [14,18e,19,31–32] . Thus, synthesis or degradation of epihalohydrins is by far the most studied system catalysed by HHDH starting from the first papers published by Castro and Bartnicki [13] and Nakamura et al [14,31] .…”

Section: Case Studiesmentioning

confidence: 99%

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Halohydrin Dehalogenases and Their Potential in Industrial Application – A Viewpoint of Enzyme Reaction Engineering

et al. 2020

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At the moment, there are approx. 100 published papers investigating halohydrin dehalogenases from different aspects; enzymology, molecular biology and reactions they can catalyse. Unquestionably, these enzymes are of great importance and hold an immense potential due to the wide spectrum of different compounds that can be synthesized by their action. These compounds, such as chiral epoxides, β‐substituted alcohols, oxazolidinones etc., significantly enrich the chemist's toolbox and, moreover, open the possibility for the synthesis of even more complex compounds. Still, there are many unknowns, and it is the purpose of this work to demonstrate the possibilities and bottlenecks, in scientific sense, that could further help in broadening the applicative potential of these fascinating enzymes.

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Section: Case Studiesmentioning

confidence: 99%

“…and 23.5% yield, was reported. HHDH from alphaproteobacterium was reported [19] to catalyse the stereoselective dehalogenation with the best results for racemic 2‐bromo‐1‐phenylethanol. ( S )‐2‐bromo‐1‐phenylethanol was produced with 99% e.e.…”

Section: Case Studiesmentioning

confidence: 99%

Halohydrin Dehalogenases and Their Potential in Industrial Application – A Viewpoint of Enzyme Reaction Engineering

et al. 2020

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“…In the reverse reaction, which is chemically more interesting, they are also capable of opening epoxide rings with a range of N ‐, C ‐, O ‐ and S ‐nucleophiles resulting in the formation of novel C‐C, C‐N, C‐O, or C‐S bonds (Hasnaoui‐Dijoux et al, 2008; Ma et al, 2022; M. Majerić Elenkov et al, 2006; M. M. Majerić Elenkov et al, 2008; Molinaro et al, 2010; Wang et al, 2022; Zhou et al, 2023). Among a large number of recently discovered new HHDHs (Schallmey et al, 2014; Wang et al, 2022; Xue et al, 2018, 2019, 2020; Zhou et al, 2023), halohydrin dehalogenase G (HheG) from Illumatobacter coccineus , along with other G‐type HHDHs, displays also exceptional activity in the conversion of sterically more demanding cyclic as well as acyclic vicinal di‐substituted epoxides (Calderini et al, 2019; Koopmeiners et al, 2017; Solarczek et al, 2022). Despite this unique substrate profile, HheG's industrial potential is limited by its insufficient stability as indicated by an apparent melting temperature of only 38°C (Solarczek et al, 2019).…”

Section: Introductionmentioning

confidence: 99%

Performance of cross‐linked enzyme crystals of engineered halohydrin dehalogenase HheG in different chemical reactor systems

Staar,

Schallmey

2023

Biotech & Bioengineering

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Halohydrin dehalogenase HheG is an industrially interesting biocatalyst for the preparation of different β‐substituted alcohols starting from bulky internal epoxides. We previously demonstrated that the immobilization of different HheG variants in the form of cross‐linked enzyme crystals (CLECs) yielded stable and reusable enzyme immobilizes with increased resistance regarding temperature, pH, and the presence of organic solvents. Now, to further establish their preparative applicability, HheG D114C CLECs cross‐linked with bis‐maleimidoethane have been successfully produced on a larger scale using a stirred crystallization approach, and their application in different chemical reactor types (stirred tank reactor, fluidized bed reactor, and packed bed reactor) was systematically studied and compared for the ring opening of cyclohexene oxide with azide. This revealed the highest obtained space‐time yield of 23.9 kgproduct gCLEC−1 h−1 Lreactor volume−1 along with the highest achieved product enantiomeric excess [64%] for application in a packed‐bed reactor. Additionally, lyophilization of those CLECs yielded a storage‐stable HheG preparation that still retained 67% of initial activity (after lyophilization) after 6 months of storage at room temperature.

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Synthesis of Enantiopure Vicinal Halohydrins Using a Sequence of Haloperoxidase and Lipase

De Marchi,

Hilberath,

Zippilli

et al. 2024

Adv Synth Catal

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Vicinal halohydrins are key building blocks to produce bioactive molecules and drugs, especially if they can be obtained in enantiomerically pure form. In this study, we present a bi‐enzymatic sequence that allows to obtain vic‐halohydrins through a photochemoenzymatic olefin hydroxy halogenation followed by a lipase catalysed kinetic resolution. The absolute configuration of the resulting products was determined using Mosher’s method.

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Exploring the Biocatalytic Scope of a Novel Enantioselective Halohydrin Dehalogenase from an Alphaproteobacterium

Cited by 9 publications

References 36 publications

Halohydrin Dehalogenases and Their Potential in Industrial Application – A Viewpoint of Enzyme Reaction Engineering

Halohydrin Dehalogenases and Their Potential in Industrial Application – A Viewpoint of Enzyme Reaction Engineering

Performance of cross‐linked enzyme crystals of engineered halohydrin dehalogenase HheG in different chemical reactor systems

Synthesis of Enantiopure Vicinal Halohydrins Using a Sequence of Haloperoxidase and Lipase

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