Latest development in the synthesis of ursodeoxycholic acid (UDCA): a critical review

• Fabio Tonin and
• Isabel W. C. E. Arends

Beilstein J. Org. Chem. 2018, 14, 470–483, doi:10.3762/bjoc.14.33

• most used enzymes for the cofactor regeneration are glucose dehydrogenase (glucose to glucuronic acid), lactate dehydrogenase (pyruvate to lactate), glutamate dehydrogenase (α-ketoglutarate to glutamate) and formate dehydrogenase (formate to CO2). In particular, the last enzyme is interesting because

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

• Barış Binay,
• Dilek Alagöz,
• Deniz Yildirim,
• Ayhan Çelik and
• S. Seyhan Tükel

Beilstein J. Org. Chem. 2016, 12, 271–277, doi:10.3762/bjoc.12.29

• 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

• , FDHIGLU and FDHIALD offer feasible potentials for in situ regeneration of NADH. Keywords: biocatalysis; Candida methylica; formate dehydrogenase; Immobead 150; regeneration of NADH; stabilization; Introduction Dehydrogenases are one of the most promising enzymes in biocatalysis since these enzymes have

• decrease operational costs. NAD+-dependent formate dehydrogenase (FDH, EC 1.2.1.2) catalyzes oxidation of formate to carbon dioxide (CO2) [6]. FDH is industrially used as coenzyme for the regeneration of NADH [7][8], as sensor for the determination of formic acid [9], and as catalyst for the production of

Biocatalysis for the application of CO₂ as a chemical feedstock

• Apostolos Alissandratos and
• Christopher J. Easton

Beilstein J. Org. Chem. 2015, 11, 2370–2387, doi:10.3762/bjoc.11.259

• as a renewable chemical feedstock, greatly enabling a sustainable carbon bio-economy. Keywords: biocatalysis; carboxylase; CO2 transformation; formate dehydrogenase; RuBisCO; Introduction Depletion of fossil-fuel feedstocks and pollution resulting from their unsustainable processing and use

• they operate, and as a result there has been little development of their use in synthetic processes. Wood–Ljungdahl pathway The Wood–Ljungdahl pathway, or reductive acetyl-CoA pathway, is used by acetogenic bacteria to reduce CO2 to either formate with formate dehydrogenase (FDH) or CO with CO

Engineering Pichia pastoris for improved NADH regeneration: A novel chassis strain for whole-cell catalysis

• Martina Geier,
• Christoph Brandner,
• Gernot A. Strohmeier,
• Mélanie Hall,
• Franz S. Hartner and
• Anton Glieder

Beilstein J. Org. Chem. 2015, 11, 1741–1748, doi:10.3762/bjoc.11.190

• +-dependent enzyme formaldehyde dehydrogenase (FLD) to S-formylglutathione. S-Formylglutathione hydrolase (FGH) then hydrolyses this compound to formate and glutathione. In a second NAD+-dependent step, formate is oxidized to CO2 by formate dehydrogenase (FDH). Thus, 2 equivalents of the cofactor NADH are

• of methanol. The redesigned Pichia strain, thus, represents a valuable host for whole-cell applications where NADH regeneration is an issue. No additional over-expression of cofactor regenerating enzymes such as formate dehydrogenase, which only yields one molecule of NADH per carbon atom, is

• dehydrogenase; FGH: S-formylglutathione hydrolase; FDH: formate dehydrogenase; CAT: catalase; DAS: dihydroxyacetone synthase; DAK: dihydroxyacetone kinase; DHA: dihydroxyacetone; GAP: D-glyceraldehyde-3-phosphate; DHAP: dihydroxyacetone phosphate; FBP: D-fructose 1,6-bisphosphate; F6P: D-fructose 6-phosphate

An integrated photocatalytic/enzymatic system for the reduction of CO₂ to methanol in bioglycerol–water

• Michele Aresta,
• Angela Dibenedetto,
• Tomasz Baran,
• Antonella Angelini,
• Przemysław Łabuz and
• Wojciech Macyk

Beilstein J. Org. Chem. 2014, 10, 2556–2565, doi:10.3762/bjoc.10.267

• , namely: formate dehydrogenase (FateDH), formaldehyde dehydrogenase (FaldDH), and alcohol dehydrogenase (ADH). These enzymes promote the cascade reduction of CO2 to methanol through formic acid (FateDH), formaldehyde (FaldDH) and aldehyde (ADH). The reduction process is enabled by NADH, which is oxidized

Biosynthesis of rare hexoses using microorganisms and related enzymes

• Zijie Li,
• Yahui Gao,
• Hideki Nakanishi,
• Xiaodong Gao and
• Li Cai

Beilstein J. Org. Chem. 2013, 9, 2434–2445, doi:10.3762/bjoc.9.281

• multi-enzyme system containing DTEase, ribitol dehydrogenase (RDH, EC 1.1.1.56) and formate dehydrogenase (FDH, EC 1.2.1.2) [99]. In this system, NADH is regenerated by an irreversible formate dehydrogenation reaction, promoting the conversion of D-psicose to allitol. As a result, the D-fructose and D

Coupled chemo(enzymatic) reactions in continuous flow

• Ruslan Yuryev,
• Simon Strompen and
• Andreas Liese

Beilstein J. Org. Chem. 2011, 7, 1449–1467, doi:10.3762/bjoc.7.169

• using a coupled parallel enzymatic system [22]. Here, L-leucine dehydrogenase was used for the reductive amination of α-ketoisocaproate (1) to the amino acid 3. The required cofactor NADH was regenerated in a coupled parallel reaction by oxidation of formate (2) catalyzed by formate dehydrogenase

• . Hummel and coworkers similarly described the stereoselective conversion of benzoyl formate (4) to D-mandelic acid (5) by a D-(−)-mandelic acid dehydrogenase from Lactobacillus curvatus in a sterilized enzyme membrane reactor, which was operated continuously (Scheme 2) [23]. Again, formate dehydrogenase

• cofactor was regenerated by coupled formate (2) oxidation catalyzed by formate dehydrogenase (FDH). Due to the high KM value of BFD for 32 an excessive concentration of this compound had to be applied in the first reactor in order to maximize the productivity. Since the aldehyde 32 is also a substrate for