Production of tert ‐butyl (3 R ,5 S )‐6‐chloro‐3,5‐dihydroxyhexanoate using carbonyl reductase coupled with glucose dehydrogenase with high space–time yield

2019 ◽  
Vol 36 (1) ◽  
Author(s):  
Xiao‐Jian Zhang ◽  
Ling Zheng ◽  
Di Wu ◽  
Rong Zhou ◽  
Zhi‐Qiang Liu ◽  
...  
RSC Advances ◽  
2019 ◽  
Vol 9 (4) ◽  
pp. 2325-2331 ◽  
Author(s):  
Yitong Chen ◽  
Baodi Ma ◽  
Songshuang Cao ◽  
Xiaomei Wu ◽  
Yi Xu

A simple and efficient process for the synthesis of optically active (S)-N-boc-3-hydroxy piperidine was developed using the “designer cells” co-expressing alcohol dehydrogenase and glucose dehydrogenase.


2021 ◽  
Vol 20 (1) ◽  
Author(s):  
Langxing Liao ◽  
Yonghui Zhang ◽  
Yali Wang ◽  
Yousi Fu ◽  
Aihui Zhang ◽  
...  

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.


Author(s):  
Lejian Zhang ◽  
Xiaoxiao Zhu ◽  
Xinping Wang ◽  
Chuan Shi

Anatase-free titanium silicalite-1 (TS-1) zeolite with high framework titanium content is highly required for catalysing selective oxidation reactions, while its synthesis generally suffers from cost, efficiency and environmental issues. Herein,...


2020 ◽  
Author(s):  
Langxing Liao ◽  
Yonghui Zhang ◽  
Yali Wang ◽  
Yousi Fu ◽  
Aihui Zhang ◽  
...  

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 yeild of L-tle by GDH-R3-LeuDH was all enhanced by 2-fold. Finally, the space-time yield of L-tle catalyzing by GDH-R3-LeuDH whole cells could achieve 2136 g/L/d 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.


BioResources ◽  
2020 ◽  
Vol 15 (4) ◽  
pp. 8689-8695
Author(s):  
Huan Liu ◽  
Xiaolan Huang ◽  
Qi Xiao ◽  
Yue Yu ◽  
Li Deng ◽  
...  

Cellulase is a compound enzyme that catalyzes cellulose into monosaccharides or oligosaccharides. Large amounts of cellulase are needed with the development of the lignocellulose processing industry, which necessitates faster methods to produce cellulase. In this work, the marine bacterium Microbulbifer hydrolyticus IRE-31-192 was selected to produce cellulase, due to its fast growth rate and short high space-time yield. Co-fermentation of glucose and xylose to produce cellulase was investigated on the basis of previous work. When the ratio of glucose/xylose was 2:1 (w/w), 294 U/L cellulase activity with highest space-time yield of 12.2 U/L h was obtained. The hydrolytic liquid of lignocellulose prepared from dried distiller’s grains with solubles (DDGS) with the similar ratio of glucose/xylose was used as medium to produce cellulase. The efficiency of cellulase production from processed and unprocessed hydrolysates of DDGS was compared. Unprocessed hydrolysates were more beneficial for the production of cellulase, such that its activity was 261 U/L with a space-time yield of 14.5 U/L h. Thus, commonly used pure glucose and xylose could be replaced by hydrolysates of DDGS, and marine bacteria has potential application for cellulase production.


2014 ◽  
Vol 2 (42) ◽  
pp. 17757-17763 ◽  
Author(s):  
Stéphane Cadot ◽  
Laurent Veyre ◽  
Dominique Luneau ◽  
David Farrusseng ◽  
Elsje Alessandra Quadrelli

Highway to MOF Ni2(dhtp)! 1 hour in boiling water under atmospheric pressure; a cheap synthesis of the linker is also reported.


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