scholarly journals Efficient synthesis of Ibrutinib chiral intermediate in high space-time yield by recombinant E. coli co-expressing alcohol dehydrogenase and glucose dehydrogenase

RSC Advances ◽  
2019 ◽  
Vol 9 (4) ◽  
pp. 2325-2331 ◽  
Author(s):  
Yitong Chen ◽  
Baodi Ma ◽  
Songshuang Cao ◽  
Xiaomei Wu ◽  
Yi Xu
Keyword(s):  
Alcohol Dehydrogenase ◽  
Glucose Dehydrogenase ◽  
Space Time ◽  
Optically Active ◽  
Efficient Synthesis ◽  
E Coli ◽  
Efficient Process ◽  
High Space ◽  
Space Time Yield

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.

Efficient synthesis of a statin precursor in high space-time yield by a new aldehyde-tolerant aldolase identified from Lactobacillus brevis

2015 ◽  
Vol 5 (8) ◽  
pp. 4048-4054 ◽  
Author(s):  
Xue-Cheng Jiao ◽  
Jiang Pan ◽  
Guo-Chao Xu ◽  
Xu-Dong Kong ◽  
Qi Chen ◽  
...  
Keyword(s):  
High Activity ◽  
Lactobacillus Brevis ◽  
Space Time ◽  
High Tolerance ◽  
Efficient Synthesis ◽  
High Space ◽  
Space Time Yield

A novel 2-deoxyribose-5-phosphate aldolase (LbDERA) was identified from Lactobacillus brevis, with high activity, excellent thermostability and high tolerance against aldehyde substrates.

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.

Synthesis of pure and uniform nano-sized TS-1 crystal with high titanium content and high space-time yield

2021 ◽  
Author(s):  
Lejian Zhang ◽  
Xiaoxiao Zhu ◽  
Xinping Wang ◽  
Chuan Shi
Keyword(s):  
Selective Oxidation ◽  
Cost Efficiency ◽  
Environmental Issues ◽  
Titanium Content ◽  
Space Time ◽  
Titanium Silicalite ◽  
Oxidation Reactions ◽  
High Space ◽  
Space Time Yield ◽  
Selective Oxidation Reactions

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,...

Highly Efficient Synthesis of (R)-3-Quinuclidinol in a Space–Time Yield of 916 g L–1 d–1 Using a New Bacterial Reductase ArQR

2013 ◽  
Vol 15 (19) ◽  
pp. 4917-4919 ◽  
Author(s):  
Wen-Xia Zhang ◽  
Guo-Chao Xu ◽  
Lei Huang ◽  
Jiang Pan ◽  
Hui-Lei Yu ◽  
...  
Keyword(s):  
Space Time ◽  
Efficient Synthesis ◽  
Highly Efficient ◽  
Space Time Yield

ChemInform Abstract: Efficient Synthesis of an ε-Hydroxy Ester (II) in a Space-Time Yield of 1580 gL-1d-1by a Newly Identified Reductase RhCR.

ChemInform ◽  
2015 ◽  
Vol 46 (18) ◽  
pp. no-no
Author(s):  
Rui-Jie Chen ◽  
Gao-Wei Zheng ◽  
Yan Ni ◽  
Bu-Bing Zeng ◽  
Jian-He Xu
Keyword(s):  
Space Time ◽  
Hydroxy Ester ◽  
Efficient Synthesis ◽  
Space Time Yield

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

2020 ◽  
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 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.

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