Light-Harvesting Dye–Alginate Hydrogel for Solar-Driven, Sustainable Biocatalysis of Asymmetric Hydrogenation

Yoon, Jaeho; Lee, Sahng Ha; Tieves, Florian; Rauch, Marine; Hollmann, Frank; Park, Chan Beum

doi:10.1021/acssuschemeng.9b01075

Cited by 39 publications

(24 citation statements)

References 43 publications

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“…The TsOYE encapsulated in alginate hydrogel exhibited enhanced stability against external stresses (e.g., heat, organic solvents), also on a repeated use. However, the long-term reusability of TsOYE alginate hydrogel was hampered by photobleaching and leakage of the dye used [18].…”

Section: Introductionmentioning

confidence: 99%

Immobilization of Old Yellow Enzymes via Covalent or Coordination Bonds

et al. 2020

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Ene-reductases (ERs) belonging to the old yellow enzyme (OYE) family have been thoroughly investigated for the stereospecific reduction of activated prochiral C=C double bonds. In this work, OYE3 was immobilized both by covalent binding on glyoxyl-agarose (OYE3-GA), and by affinity-based adsorption on EziGTM particles (OYE3-EziG). The immobilized OYE3-GA was demonstrated to be active (activity recovery = 52%) and to retain almost 100% of its activity under the enzymatic assay conditions (50 mM phosphate buffer pH 7, 28 °C) for six days, whereas the activity of the non-immobilized enzyme dropped to 50% after two days. In the case of EziGTM, the highest activity recovery (54%) was achieved by using the most hydrophilic carrier (EziGTM Opal) that was selected for the full characterization of this type of enzyme preparation (stability, recycling, re-use, enzyme leakage). OYE3-EziG was slightly less stable than OYE3-GA under the same experimental conditions. OYE3-GA could be recycled and re-used for up to 12 reaction cycles in the bioreduction of α-methyl-trans-cinnamaldehyde; after 12 runs, the highest conversion achieved was 40%. In the case of the co-immobilized OYE3/GDH-EziG, the conversion dropped to 56% after two reaction cycles. No enzyme leakage was detected over 48 h for both OYE3-GA and OYE3/GDH-EziG (50 mM phosphate buffer pH 7, 28 °C). These seed results pave the way for a true optimization of the immobilization of OYE3, as well as for the use of immobilized OYE3 for preparative applications both in batch and continuous flow conditions.

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Section: Introductionmentioning

confidence: 99%

Immobilization of Old Yellow Enzymes via Covalent or Coordination Bonds

et al. 2020

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“…Exhibit Agar-agar [208], agarose [209], albumin [210], alginate [211], carrageenan [212], cellulose, chitin/chitosan [213], collagen [214], gelatin [215], pectin [216], Sepharose (crosslinked agarose) [217], alginate/starch [217] Sinthetic polymers Polymeric chain assembled using selected monomers to fit the requirements of enzyme and process where the catalyst will be used -Diversity of functional groups, e.g., alkyl, amine, carbonyl, carboxyl, epoxy, hydroxyl, in the structure of the polymer that ease enzyme binding and polymer surface functionalization -Tailored hydrophobic/hydrophilic nature of the carrier -Often available as highly porous, ion-exchange resins…”

Section: Natural Polymersmentioning

confidence: 99%

Enzyme Immobilization and Co-Immobilization: Main Framework, Advances and Some Applications

et al. 2022

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Enzymes are outstanding (bio)catalysts, not solely on account of their ability to increase reaction rates by up to several orders of magnitude but also for the high degree of substrate specificity, regiospecificity and stereospecificity. The use and development of enzymes as robust biocatalysts is one of the main challenges in biotechnology. However, despite the high specificities and turnover of enzymes, there are also drawbacks. At the industrial level, these drawbacks are typically overcome by resorting to immobilized enzymes to enhance stability. Immobilization of biocatalysts allows their reuse, increases stability, facilitates process control, eases product recovery, and enhances product yield and quality. This is especially important for expensive enzymes, for those obtained in low fermentation yield and with relatively low activity. This review provides an integrated perspective on (multi)enzyme immobilization that abridges a critical evaluation of immobilization methods and carriers, biocatalyst metrics, impact of key carrier features on biocatalyst performance, trends towards miniaturization and detailed illustrative examples that are representative of biocatalytic applications promoting sustainability.

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“…Yoon et al. co‐immobilized an ene‐reductase from Thermus scotoductus SA‐01 ( Ts OYE) and rose bengal (RB, a light‐harvesting dye) together in alginate hydrogel capsules [ 109 ]. With these hydrogel beads, the authors performed a cofactor‐free asymmetric reduction of 2‐methylcyclohexenone to enantiopure ( R )‐2‐methylcyclohexanone with high enantioselectivities (> 99%) and a maximal conversion of 70.4% (Figure 2(vii) ).…”

Section: Enzyme Immobilization In Hydrogel Materialsmentioning

confidence: 99%