Cofactor Regeneration at the Lab Scale

2005 ◽  
pp. 225-260 ◽  
Author(s):  
R. Wichmann ◽  
D. Vasic-Racki
Keyword(s):  
Cofactor Regeneration

Improvement of cadaverine production in whole cell system with baker’s yeast for cofactor regeneration

2021 ◽  
Author(s):  
Yeong-Hoon Han ◽  
Hyun Joong Kim ◽  
Tae-Rim Choi ◽  
Hun-Suk Song ◽  
Sun Mi Lee ◽  
...  
Keyword(s):  
Cell System ◽  
Baker’S Yeast ◽  
Cofactor Regeneration ◽  
Baker's Yeast ◽  
Whole Cell

scholarly journals A Redox-Neutral, Two-Enzyme Cascade for the Production of Malate and Gluconate from Pyruvate and Glucose

2021 ◽  
Vol 11 (11) ◽  
pp. 4877
Author(s):  
Ravneet Mandair ◽  
Pinar Karagoz ◽  
Roslyn M. Bill
Keyword(s):  
Malate Dehydrogenase ◽  
Closed System ◽  
Glucose Dehydrogenase ◽  
Sulfolobus Solfataricus ◽  
Cofactor Regeneration ◽  
Triple Mutant ◽  
Thermococcus Kodakarensis ◽  
Platform Chemicals ◽  
Enzyme Cascade

A triple mutant of NADP(H)-dependent malate dehydrogenase from thermotolerant Thermococcus kodakarensis has an altered cofactor preference for NAD+, as well as improved malate production compared to wildtype malate dehydrogenase. By combining mutant malate dehydrogenase with glucose dehydrogenase from Sulfolobus solfataricus and NAD+/NADH in a closed reaction environment, gluconate and malate could be produced from pyruvate and glucose. After 3 h, the yield of malate was 15.96 mM. These data demonstrate the feasibility of a closed system capable of cofactor regeneration in the production of platform chemicals.

scholarly journals Bioelectrocatalytic cofactor regeneration coupled to CO2 fixation in a redox‐active hydrogel for stereoselective C‐C bond formation

2021 ◽  
Author(s):  
Leonardo Castañeda-Losada ◽  
David Adam ◽  
Nicole Paczia ◽  
Darren Buesen ◽  
Fabian Steffler ◽  
...  
Keyword(s):  
Co2 Fixation ◽  
Bond Formation ◽  
Cofactor Regeneration ◽  
Redox Active

Cell-Free Total Biosynthesis of Plant Terpene Natural Products Using an Orthogonal Cofactor Regeneration System

ACS Catalysis ◽  
2021 ◽  
pp. 9898-9903
Author(s):  
Undramaa Bat-Erdene ◽  
John M. Billingsley ◽  
William C. Turner ◽  
Benjamin R. Lichman ◽  
Francesca M. Ippoliti ◽  
...  
Keyword(s):  
Natural Products ◽  
Cofactor Regeneration ◽  
Regeneration System

scholarly journals Construction and characterization of a novel glucose dehydrogenase-leucine dehydrogenase fusion enzyme for the biosynthesis of l-tert-leucine

2021 ◽  
Vol 20 (1) ◽  
Author(s):  
Langxing Liao ◽  
Yonghui Zhang ◽  
Yali Wang ◽  
Yousi Fu ◽  
Aihui Zhang ◽  
...  
Keyword(s):  
Glucose Dehydrogenase ◽  
Catalytic Efficiency ◽  
Space Time ◽  
Cofactor Regeneration ◽  
Enzyme Complex ◽  
Regeneration System ◽  
Regeneration Rate ◽  
Leucine Dehydrogenase ◽  
Fusion Enzyme ◽  
Space Time Yield

Abstract Background Biosynthesis of l-tert-leucine (l-tle), a significant pharmaceutical intermediate, by a cofactor regeneration system friendly and efficiently is a worthful goal all the time. The cofactor regeneration system of leucine dehydrogenase (LeuDH) and glucose dehydrogenase (GDH) has showed great coupling catalytic efficiency in the synthesis of l-tle, however the multi-enzyme complex of GDH and LeuDH has never been constructed successfully. Results In this work, a novel fusion enzyme (GDH–R3–LeuDH) for the efficient biosynthesis of l-tle was constructed by the fusion of LeuDH and GDH mediated with a rigid peptide linker. Compared with the free enzymes, both the environmental tolerance and thermal stability of GDH–R3–LeuDH had a great improved since the fusion structure. The fusion structure also accelerated the cofactor regeneration rate and maintained the enzyme activity, so the productivity and yield of l-tle by GDH–R3–LeuDH was all enhanced by twofold. Finally, the space–time yield of l-tle catalyzing by GDH–R3–LeuDH whole cells could achieve 2136 g/L/day in a 200 mL scale system under the optimal catalysis conditions (pH 9.0, 30 °C, 0.4 mM of NAD+ and 500 mM of a substrate including trimethylpyruvic acid and glucose). Conclusions It is the first report about the fusion of GDH and LeuDH as the multi-enzyme complex to synthesize l-tle and reach the highest space–time yield up to now. These results demonstrated the great potential of the GDH–R3–LeuDH fusion enzyme for the efficient biosynthesis of l-tle.

Design of a cytochrome P450BM3 reaction system linked by two-step cofactor regeneration catalyzed by a soluble transhydrogenase and glycerol dehydrogenase

2009 ◽  
Vol 25 (5) ◽  
pp. 1372-1378 ◽  
Author(s):  
Tsuyoshi Mouri ◽  
Takeshi Shimizu ◽  
Noriho Kamiya ◽  
Masahiro Goto ◽  
Hirofumi Ichinose
Keyword(s):  
Reaction System ◽  
Cofactor Regeneration ◽  
Glycerol Dehydrogenase
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