Stereoselective synthesis of caffeic acid amides via enzyme-catalyzed asymmetric aminolysis reaction

Xiao, Peiliang; Zhang, Suoqin; Ma, Huayu; Zhang, Aijun; Lv, Xiaoli; Zheng, Liangyu

doi:10.1016/j.jbiotec.2013.09.004

Cited by 23 publications

(10 citation statements)

References 36 publications

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“…The role of organic solvents in the enzymatic reaction is to increase the solubility of the substrates and to ensure sufficient contact between the enzyme active sites and the substrates (Fernandez-Perez and Otero, 2003;Levinson et al, 2005;Xiao et al, 2013). However, the organic solvents and temperature also showed great influence on the enzyme activity, stability and selectivity (Zaks and Klibanov, 1984;Ragupathy et al, 2012;Garcia-Alles and Gotor, 2015).…”

Section: Effect Of Solvents and Temperature On The Amidation Reactionmentioning

confidence: 99%

Optimization of the Lipase-Catalyzed Selective Amidation of Phenylglycinol

Sun

Nie

Wang

et al. 2020

Front. Bioeng. Biotechnol.

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Ceramides and their analogs have a regulatory effect on inflammatory cytokines expression. It was found that a kind of ceramides analog synthesized from phenylglycinol could inhibit the production of cytokine TNF-α. However, two active hydrogen groups are present in the phenylglycinol molecule. It is difficult to control the process without hydroxyl group protection to dominantly produce amide in the traditional chemical synthesis. A selective catalytic the amidation route of phenylglycinol by lipases was investigated in this research. The results indicated that the commercial immobilized lipase Novozym 435 has the best regio-selectivity on the amide group. Based on the experimental results and in silico simulation, it was found that the mechanism of specific N-acyl selectivity of lipase was not only from intramolecular migration and proton shuttle mechanism, but also from the special structure of active site of enzyme. The optimal reaction yield of aromatic amide compound in a solvent-free system with lipase loading of 15 wt% (to the weight of total substrate) reached 89.41 ± 2.8% with very few of byproducts detected (0.21 ± 0.1% ester and 0.64 ± 0.2% diacetylated compound). Compare to other reported works, this work have the advantages such as low enzyme loading, solvent free, and high N-acylation selectivity. Meanwhile, this Novozym 435 lipase based synthesis method has an excellent regio-selectivity on most kinds of amino alcohol compounds. Compared to the chemical method, the enzymatic synthesis exhibited high regio-selectivity, and conversion rates. The method could be a promising alternative strategy for the synthesis of aromatic alkanolamides.

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Section: Effect Of Solvents and Temperature On The Amidation Reactionmentioning

confidence: 99%

Optimization of the Lipase-Catalyzed Selective Amidation of Phenylglycinol

Sun

Nie

Wang

et al. 2020

Front. Bioeng. Biotechnol.

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“…Amide synthesis in literature have been performed under varying reaction conditions, viz., without catalyst 15,19 , in presence of bio 22,29,45 or chemical catalysts 16,20,[30][31][32]41,[46][47][48] . Table 3 present …”

Section: Comparison Of Ni/cao Activity With Few Literature Reported Cmentioning

confidence: 99%

“…Literature reported bio as well as chemical heterogeneous catalysts such as Novozym 435 (using 40:1 of amine: feedstock molar ratio) 29 chemical method and its characterization by SEM, TEM, powder XRD, and Hammett indicator 3 studies. The prepared Ni/CaO was employed as heterogeneous catalyst for the aminolysis of triglycerides with diethanolamine to prepare corresponding amide derivatives.…”

Section: Introductionmentioning

confidence: 99%

Aminolysis of triglycerides using nanocrystalline nickel doped CaO as an efficient solid catalyst

2016

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Present manuscript reports the preparation of Ni doped CaO in nanocrystalline form, using wet chemical method, and investigation of their catalytic activity towards aminolysis of variety of triglycerides with diethanolamine. The powder XRD study suggested the formation of a solid solution of NiO in CaO as long as nickel content in catalyst remain ≤ 5 wt%. Transmission electron microscopy study supported the formation of Ni/CaO particles in the form of nanorods at 650 °C calcination temperature. Catalyst activity was found to be a function of basic strength which in turn depends upon the catalyst calcination temperature. Catalyst prepared by 0.5 wt% Ni doping in CaO at 650 °C was found to complete the aminolysis (> 99% amide yield) of waste cottonseed oil within 0.5 and 3.0 h at 110°C and room temperature (35 °C), respectively. The catalyst was easily recovered from the reaction mixture by simple filtration and reused during seven consecutive reaction cycles without significant loss in activity. The (pseudo) first order rate constant and activation energy for the reaction was observed 0.15 min -1 and 52.7 kJ mol -1 , respectively.

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“…31 Lipases (EC 3.1) can catalyze many popular reactions such as hydrolysis of fatty oil, 32 esterification, 33 aminolysis and enantioselectivity. 34 Therefore, they are widely used in the food and chemical industry, such as, synthesis of structured lipids, 35 synthesis of sugar esters, 36 and biotransformation of polyphenols. 37 Although free lipases are quite robust compared with most enzymes, they may still require stabilization for certain applications.…”

Section: Introductionmentioning

confidence: 99%

Preparation of spherical cross-linked lipase aggregates with improved activity, stability and reusability characteristic in water-in-ionic liquid microemulsion

Cui

Lin

Feng

et al. 2017

J. Chem. Technol. Biotechnol

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BACKGROUND Cross‐linking enzyme aggregates (CLEAs) seem to be a promising immobilization method due to mild processing conditions and short preparation time. However, the CLEAs prepared in aqueous solution exhibit amorphous large clusters that cause significant mass‐transfer limitations, leading to low catalytic efficiency. In this work, novel spherical CLEAs of lipase from bovine pancreas (spherical CLEAs) were prepared within droplets dispersed in a water‐in‐hydrophobic ionic liquid microemulsion rather than a conventional aqueous solution. The properties of the spherical CLEAs were determined. RESULTS The resultant CLEAs exhibited spherical structure with good monodispersity instead of the amorphous clusters of conventional CLEAs, and showed higher activity recovery (84.6%) than that of conventional CLEAs (52.8%). The high activity recovery of spherical CLEAs could be attributed to both interfacial activation of the microemulsion system and the well‐defined structure of the spherical CLEAs, which not only activated lipases in an active form, but also decreased mass‐transfer limitations. Moreover, the thermostability, storage stability, tolerance against hydrophilic solvents, and mechanical stability of the spherical CLEAs were enhanced significantly. The spherical CLEAs evidenced excellent reusability in comparison with conventional CLEAs. CONCLUSIONS The novel strategy in this study might open an attractive way towards effectively improving the catalytic properties of traditional CLEAs. © 2016 Society of Chemical Industry

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Stereoselective synthesis of caffeic acid amides via enzyme-catalyzed asymmetric aminolysis reaction

Cited by 23 publications

References 36 publications

Optimization of the Lipase-Catalyzed Selective Amidation of Phenylglycinol

Optimization of the Lipase-Catalyzed Selective Amidation of Phenylglycinol

Aminolysis of triglycerides using nanocrystalline nickel doped CaO as an efficient solid catalyst

Preparation of spherical cross-linked lipase aggregates with improved activity, stability and reusability characteristic in water-in-ionic liquid microemulsion

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