Selective oxidation and reduction reactions with cofactor regeneration mediated by galactitol-, lactate-, and formate dehydrogenases immobilized on magnetic nanoparticles

Demir, Ayhan S.; Talpur, Farah Naz; Sopacı, Ş. Betül; Kohring, Gert‐Wieland; Çelik, Ayhan

doi:10.1016/j.jbiotec.2011.03.002

Cited by 27 publications

(14 citation statements)

References 31 publications

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“…The purification of FDH was performed according to Demir et al [32]. Briefly, 7 g of wet E. coli BL21 (DE3) cell paste containing the expressed FDH protein was suspended in 10 mL buffer solution (20 mM Tris–HCl, pH 7.8, 0.5 M NaCl, 5 mM imidazole) at 4 °C.…”

Section: Methodsmentioning

confidence: 99%

Highly stable and reusable immobilized formate dehydrogenases: Promising biocatalysts for in situ regeneration of NADH

Bi̇nay

Alagöz

Yıldırım

et al. 2016

Beilstein J. Org. Chem.

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SummaryThis study aimed to prepare robust immobilized formate dehydrogenase (FDH) preparations which can be used as effective biocatalysts along with functional oxidoreductases, in which in situ regeneration of NADH is required. For this purpose, Candida methylica FDH was covalently immobilized onto Immobead 150 support (FDHI150), Immobead 150 support modified with ethylenediamine and then activated with glutaraldehyde (FDHIGLU), and Immobead 150 support functionalized with aldehyde groups (FDHIALD). The highest immobilization yield and activity yield were obtained as 90% and 132%, respectively when Immobead 150 functionalized with aldehyde groups was used as support. The half-life times (t 1/2) of free FDH, FDHI150, FDHIGLU and FDHIALD were calculated as 10.6, 28.9, 22.4 and 38.5 h, respectively at 35 °C. FDHI150, FDHIGLU and FDHIALD retained 69, 38 and 51% of their initial activities, respectively after 10 reuses. The results show that the FDHI150, FDHIGLU and FDHIALD offer feasible potentials for in situ regeneration of NADH.

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Section: Methodsmentioning

confidence: 99%

Highly stable and reusable immobilized formate dehydrogenases: Promising biocatalysts for in situ regeneration of NADH

Bi̇nay

Alagöz

Yıldırım

et al. 2016

Beilstein J. Org. Chem.

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“…Alternatively, specific cofactor regeneration systems can be employed when isolated enzymes are to be used (Fig. 5) [17,40].…”

Section: Enzymes For Rare Sugar Productionmentioning

confidence: 99%

Enzymes for the biocatalytic production of rare sugars

Beerens

Desmet

Soetaert

2012

Journal of Industrial Microbiology and Biotechnology

168

109

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Carbohydrates are much more than just a source of energy as they also mediate a variety of recognition processes that are central to human health. As such, saccharides can be applied in the food and pharmaceutical industries to stimulate our immune system (e.g., prebiotics), to control diabetes (e.g., low-calorie sweeteners), or as building blocks for anticancer and antiviral drugs (e.g., L: -nucleosides). Unfortunately, only a small number of all possible monosaccharides are found in nature in sufficient amounts to allow their commercial exploitation. Consequently, so-called rare sugars have to be produced by (bio)chemical processes starting from cheap and widely available substrates. Three enzyme classes that can be used for rare sugar production are keto-aldol isomerases, epimerases, and oxidoreductases. In this review, the recent developments in rare sugar production with these biocatalysts are discussed.

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“…A typical biotechnological use of FDH is in the determination of formic and oxalic acid in solution, but it can also be used as a NAD + regeneration system [6][7][8], especially after immobilization, e.g. on silica matrixes [9], agaroses [1,10], membranes [11] and magnetic nanoparticles [12]. The best recyclability performance has been obtained using alginate gels as supports [13].…”

Section: Introductionmentioning

confidence: 99%

Improving the catalytic activity of formate dehydrogenase from Candida boidinii by using magnetic nanoparticles

Netto¹,

Nakamura²,

Andrade³

et al. 2012

Journal of Molecular Catalysis B: Enzymatic

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Selective oxidation and reduction reactions with cofactor regeneration mediated by galactitol-, lactate-, and formate dehydrogenases immobilized on magnetic nanoparticles

Cited by 27 publications

References 31 publications

Highly stable and reusable immobilized formate dehydrogenases: Promising biocatalysts for in situ regeneration of NADH

Highly stable and reusable immobilized formate dehydrogenases: Promising biocatalysts for in situ regeneration of NADH

Enzymes for the biocatalytic production of rare sugars

Improving the catalytic activity of formate dehydrogenase from Candida boidinii by using magnetic nanoparticles

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