JOURNAL OF ORGANIC CHEMISTRY
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2022
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IF 4.198
Ge Liu,Yuzhen Gao,Weiping Su
An efficient protocol was proposed for the preparation of secondary alcohols in good to excellent yields via photoredox-catalyzed decarboxylative couplings between readily available arylacetic acids and a variety of less reactive (hetero)aromatic aldehydes. The formation of carbanion is the key intermediate in this reaction. Various substituted arylacetic acids and aldehydes were all compatible with this transformation under mild reaction conditions. Furthermore, the current protocol was successfully applied to the direct alcoholization of several drug acids.
研究领域:
有机化学
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合成化学
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DOI
PubMed
高影响因子
MOLECULES
·
2019
·Vol. 24
·期 3
·490
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IF 3.06
Xiu Xing,Jun-Qi Jia,Jing-Fan Zhang,Zi-Wen Zhou,Jun Li,Na Wang,Xiao-Qi Yu
In this study, an immobilization strategy for magnetic cross-linking enzyme aggregates of lipase B fromCandida antarctica(CALB) was developed and investigated. Magnetic particles were prepared by conventional co-precipitation. The magnetic nanoparticles were modified with 3-aminopropyltriethoxysilane (APTES) to obtain surface amino-functionalized magnetic nanoparticles (APTES–Fe3O4) as immobilization materials. Glutaraldehyde was used as a crosslinker to covalently bind CALB to APTES–Fe3O4. The optimal conditions of immobilization of lipase and resolution of racemic 1-phenylethanol were investigated. Under optimal conditions, esters could be obtained with conversion of 50%, enantiomeric excess of product (eep) > 99%, enantiomeric excess of substrate (ees) > 99%, and enantiomeric ratio (E) > 1000. The magnetic CALB CLEAs were successfully used for enzymatic kinetic resolution of fifteen secondary alcohols. Compared with Novozym 435, the magnetic CALB CLEAs exhibited a better enantioselectivity for most substrates. The conversion was still greater than 49% after the magnetic CALB CLEAs had been reused 10 times in a 48 h reaction cycle; both eesand eepwere close to 99%. Furthermore, there was little decrease in catalytic activity and enantioselectivity after being stored at −20 °C for 90 days.Keywords:CALB;magnetic nanoparticles;cross-linked enzyme aggregates;resolution;secondary alcohols
研究领域:
生物化学
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材料科学
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酶工程
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DOI
PubMed
高影响因子
CATALYSIS LETTERS
·
2025
·Vol. 155
·期 4
·1-10
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IF 2.4
Cao Songshuang,Wu Xiaomei,Ma Baodi,Xu Yi
Aliphatic chiral secondary alcohols are important chiral intermediates widely used in the synthesis of drugs and fine chemicals. The whole cells of recombinant E. coli co-expressing alcohol dehydrogenase and glucose dehydrogenase were used to catalyze the asymmetric reduction of three fatty ketones without the addition of exogenous cofactors. The reaction medium and reaction conditions were systematically studied. As expected, the kinds of co-solvents, the molar ratio of glucose/substrate, temperature, pH and cell amount have important influence on the reaction. Under the optimal condition (glucose at 1.5 times substrate concentration, isopropanol at 2%, PBS (0.1 M, pH 8.0), and 45℃), the cells co-expressing both enzymes efficiently catalyzed the asymmetric reduction of three fatty ketones to the corresponding ( S )-fatty alcohols. The conversion and ee value of the products were both greater than 99% after 8 h reaction at 1 M of substrate concentration, and the space-time yield was between 346 ~ 470 g/(L·d). All the products can be obtained on gram scale. The results indicated that this method has potential application value in the efficient and green synthesis of aliphatic chiral secondary alcohols. Graphical
研究领域:
生物化学
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合成生物学
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DOI
高影响因子
BIORESOURCE TECHNOLOGY
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2017
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IF 5.651
Guochao Xu,Yaping Zhang,Yue Wang,Ye Ni
In this work, genome hunting strategy was adopted in screening for reductases from Candida glabrata . A total of 37 putative reductases were successfully expressed in E. coli BL21(DE3). A substrate library containing 32 substrates was established for characterization of each reductase by average specific activity and Shannon-Wiener index. Among them, Cg26 was identified with the highest efficiency and wider substrate spectrum in the reduction of prochiral ketones, with average activity and Shannon-Wiener index of 8.95 U·mg −1 and 2.82. Cg26 is a member of ‘extended’ short chain dehydrogenase/reductase superfamily. Ni 2+ could improve its activity. As much as 150 g·L −1 ethyl 2-oxo-4-phenylbutyrate could be completely converted by 10 g·L −1 Cg26. This study provides evidence for this newly identified Cg26 in the preparation of chiral secondary alcohols.
研究领域:
生物化学
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酶工程
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合成生物学
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DOI
PubMed
高影响因子
INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES
·
2024
·
IF 7.7
Wenwen Pei,Xuewen Zhang,Yan Zeng,Jiao Li,Ziyi Li,Jiangang Yang,Xinjun Du,Yueming Zhu,Yuanxia Sun
α-Hydroxyketones, which have significant industrial applications, can be sustainably synthesized through the oxidation of secondary alcohols using secondary alcohol dehydrogenase (SADH). However, the activity of the SADH oxidation reaction is generally low, making it unsuitable for large-scale production. In this study, a rational design approach was employed to computationally engineer SADH derived from Ogataea parapolymorpha ( Op SADH), significantly enhancing its oxidation activity towards ( R )-1,2-propanediol (PDO). The mutant M2 (S222T/S316A) exhibited a 14.2-fold increase in specific enzyme activity compared to the wild type (WT) and was employed as a catalyst for high-concentration hydroxyacetone production, facilitated by an NAD + regeneration system. By applying an appropriate Zn 2+ ion force field in molecular dynamics (MD) simulations, it was found that two mutation sites could stabilize the conformations of NAD + and PDO, thereby revealing the molecular mechanism behind the enhanced activity of this metalloenzyme mutant. Notably, we first uncovered the dynamic mechanism by which four key residues (Cys39, His75, Glu76, and Glu175) and PDO within the active pocket contribute to the formation of coordination bonds with Zn 2+ . The findings of this study provide robust support for researching the catalytic mechanisms and dynamics processes of metalloenzymes.
研究领域:
生物化学
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酶工程
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计算生物学
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DOI
PubMed
高影响因子
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