Biosynthesis of optically pure chiral alcohols by a substrate coupled and biphasic system with a short-chain dehydrogenase from Streptomyces griseus

Tan, Zhuotao; Ma, Hongmin; Li, Qing; Pu, Lingling; Cao, Yang; Qu, Xudong; Zhu, Chenjie; Ying, Hanjie

doi:10.1016/j.enzmictec.2016.08.015

Cited by 24 publications

(11 citation statements)

References 32 publications

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“…The first approach is a substrate-coupled reaction systems, in which one enzyme that uses both the reduced and oxidized forms of a cofactor is applied to catalyse both the synthesis of the product from one substrate and the cofactor regeneration reaction with a second substrate [50]. An example of substrate coupled regeneration is described by Tan and coworkers [53] using Streptomyces griseus carbonyl reductase for the conversion of prochiral ketones into highly optically active alcohols. Isopropanol was used as the co-substrate for the NADH recycling in the substrate-coupled reaction (Figure 2A).…”

Section: Cofactor Recyclingmentioning

confidence: 99%

Using enzyme cascades in biocatalysis: Highlight on transaminases and carboxylic acid reductases

Cutlan

Rose²,

Isupov³

et al. 2020

Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics

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Section: Cofactor Recyclingmentioning

confidence: 99%

Using enzyme cascades in biocatalysis: Highlight on transaminases and carboxylic acid reductases

Cutlan

Rose²,

Isupov³

et al. 2020

Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics

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“…2016) and SgCR from Streptomyces griseus (Tan et al . 2016), have been developed as biocatalysts in the asymmetric biocatalytic reduction reactions, but most of them are difficult or low catalytic efficacies for the synthesis of bulky prochiral carbonyl compounds with commercial application value. Furthermore, the scale‐up of asymmetric bioreduction reactions has been restricted due to the limited commercially available biocatalysts, the low volumetric productivity, narrow substrate specificity, expensive cofactor dependency and low initial substrate concentration and insolubility.…”

Section: Introductionmentioning

confidence: 99%

Identification of a newly isolated Rhodotorula mucilaginosa NQ1 and its development for the synthesis of bulky carbonyl compounds by whole‐cell bioreduction

Wang

Peng

et al. 2020

Lett Appl Microbiol

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A strain NQ1, which showed efficient asymmetric reduction of 3,5‐bis(trifluoromethyl) acetophenone (BTAP) to enantiopure (S)‐[3,5‐bis(trifluoromethyl)phenyl]ethanol ((S)‐BTPE), which is the key intermediate for the synthesis of a receptor antagonist and antidepressant, was isolated from a soil sample. Based on its morphological and internal transcribed spacer sequence, the strain NQ1 was identified to be Rhodotorula mucilaginosa NQ1. Some key reaction parameters involved in the bioreduction catalyzed by whole cells of R. mucilaginosa NQ1 were subsequently optimized, and the optimized conditions for the synthesis of (S)‐BTPE were determined to be as follows: 5·0 ml phosphate buffer (200 mmol l−1, pH 7·0), 80 mmol l−1 of BTAP, 250 g (wet weight) l−1 of resting cell, 35 g l−1 of glucose and a reaction for 18 h at 30°C and 180 rev min−1. The strain NQ1 exhibited a best yield of 99% and an excellent enantiomeric excess of 99% for the preparation of (S)‐BTPE under the above optimal conditions, and could also asymmetrically reduce a variety of bulky prochiral carbonyl compounds to their corresponding optical hydroxyl compound with excellent enantioselectivity. These results indicated that R. mucilaginosa NQ1 had a good capacity to reduce BTAP to its corresponding (S)‐BTPE, and might be a new potential biocatalyst for the production of valuable chiral hydroxyl compounds in industry.

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“…Currently, enantiomerically pure alcohols are important building blocks that are widely used as intermediates in the chemical and pharmaceutical industries for synthesis of ne products with chiral centers such as, avourings, agrochemicals, drugs, liquid crystals and specialty materials. 1,2 Thus, their synthesis is continuously of great interest to researchers. Considering that the traditional synthetic methods predominantly use toxic metals or expensive complex ligands, enzyme-catalysed syntheses offer signicant advantages to these methods, such as remarkable chemo-, regio-, and stereoselectivity, environmentally benign processes and energyefficient operations.…”

Section: Introductionmentioning

confidence: 99%

Enzymatic synthesis of enantiopure alcohols: current state and perspectives

Chen

Souza

2019

RSC Adv.

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Biosynthesis of optically pure chiral alcohols by a substrate coupled and biphasic system with a short-chain dehydrogenase from Streptomyces griseus

Cited by 24 publications

References 32 publications

Using enzyme cascades in biocatalysis: Highlight on transaminases and carboxylic acid reductases

Using enzyme cascades in biocatalysis: Highlight on transaminases and carboxylic acid reductases

Identification of a newly isolated Rhodotorula mucilaginosa NQ1 and its development for the synthesis of bulky carbonyl compounds by whole‐cell bioreduction

Enzymatic synthesis of enantiopure alcohols: current state and perspectives

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