scholarly journals Chemoenzymatic Epoxidation of Alkenes and Reusability Study of the Phenylacetic Acid

2014 ◽  
Vol 2014 ◽  
pp. 1-7 ◽  
Author(s):  
Emilia Abdulmalek ◽  
Mahashanon Arumugam ◽  
Hanis Nabillah Mizan ◽  
Mohd. Basyaruddin Abdul Rahman ◽  
Mahiran Basri ◽  
...  

Here, we focused on a simple enzymatic epoxidation of alkenes using lipase and phenylacetic acid. The immobilisedCandida antarcticalipase B, Novozym 435 was used to catalyse the formation of peroxy acid instantly from hydrogen peroxide (H2O2) and phenylacetic acid. The peroxy phenylacetic acid generated was then utilised directly forin situoxidation of alkenes. A variety of alkenes were oxidised with this system, resulting in 75–99% yield of the respective epoxides. On the other hand, the phenylacetic acid was recovered from the reaction media and reused for more epoxidation. Interestingly, the waste phenylacetic acid had the ability to be reused for epoxidation of the 1-nonene to 1-nonene oxide, giving an excellent yield of 90%.

RSC Advances ◽  
2017 ◽  
Vol 7 (21) ◽  
pp. 12518-12523 ◽  
Author(s):  
Pengfei Zhou ◽  
Xuping Wang ◽  
Bo Yang ◽  
Frank Hollmann ◽  
Yonghua Wang

Epoxides are important synthetic intermediates for the synthesis of a broad range of industrial products.


2002 ◽  
Vol 80 (6) ◽  
pp. 565-570 ◽  
Author(s):  
Szilvia Gedey ◽  
Arto Liljeblad ◽  
László Lázár ◽  
Ferenc Fülöp ◽  
Liisa T Kanerva

The Candida antarctica lipase B-catalyzed reactions of five β-amino esters with neat butyl butanoate and with 2,2,2-trifluoroethyl butanoate in diisopropyl ether were studied, as were the reactions of the same β-amino esters and their N-butanamides with neat butanol. The possibility for sequential resolution, where the amino and ester functions of the substrate both react with an achiral butanoate, became less likely with increasing size of the substrate from ethyl 3-aminobutanoate (1a) to pentanoate (1b) or larger. On the other hand, the alcoholyses of N-acylated β-amino esters successfully proceeded in butanol with E > 100. Gram-scale resolution of the N-butanoylated 1a was performed to demonstrate the usefulness of the method. Key words: lipase, interesterification, acylation, alcoholysis, resolution, β-amino esters.


2012 ◽  
Vol 626 ◽  
pp. 547-550
Author(s):  
Senthil Kumar Senthil ◽  
M.H. Uzir ◽  
Z. Ahmad

The Effects of temperature on ring-opening bulk polymerizations of ε-caprolactone was studied by using two different lipases Novozym 435 (immobilized form of lipase B from Candida antarctica), and Pseudomonas Floroscens as biocatalyst. The polymerization of ε-caprolactone was carried out at 50°C, 60°C, 70°C, 80°C, 90°C, and 100°C. For Novozym 435 the results showed that increasing the reaction time of the polymerization system resulted in an increased rate of monomer consumption and hence increased the molecular weight. For an increase in reaction time the conversion increases steadily and after a gradual increase there is a decrease which is found uniform for all the temperature showing a uniform trend. For a temperature of 70°C and 4 hours molecular weight was found to be 8.4 x 104 daltons which were the highest of all the readings that were obtained. In the copolymerizaton of ε-caprolactone (ε-CL) and δ-valerolactone using Pseudomonas fluorescens lipase at 60°C for 20 days a copolymer with molecular weight of 1.97 x 105 was obtained. Effects of the reaction time and temperature on the copolymerization have been examined.


Catalysts ◽  
2018 ◽  
Vol 8 (9) ◽  
pp. 369 ◽  
Author(s):  
Simone Weinberger ◽  
Alessandro Pellis ◽  
James Comerford ◽  
Thomas Farmer ◽  
Georg Guebitz

In the present work, Candida antarctica lipase B (CaLB) was adsorbed onto polypropylene beads using different reaction conditions, in order to investigate their influence on the immobilization process and the enzyme activity of the preparations in polymerization reactions. In general, lower salt concentrations were more favorable for the binding of enzyme to the carrier. Polymerisation of dimethyl adipate (DMA) and 1,4-butanediol (BDO) was investigated in thin-film systems at 70 °C and at both atmosphere pressure (1000 mbar) and 70 mbar. Conversion rates and molecular masses of the reaction products were compared with reactions catalyzed by CaLB in its commercially available form, known as Novozym 435 (CaLB immobilized on macroporous acrylic resin). The best results according to molecular weight and monomer conversion after 24 h reaction time were obtained with CaLB immobilized in 0.1 M Na2HPO4\NaH2PO4 buffer at pH 8, producing polyesters with 4 kDa at conversion rates of 96% under low pressure conditions. The stability of this preparation was studied in a simulated continuous polymerization process at 70 °C, 70 mbar for 4 h reaction time. The data of this continuous polymerizations show that the preparation produces lower molecular weights at lower conversion rates, but is comparable to the commercial enzyme concerning stability for 10 cycles. However, after 24 h reaction time, using our optimum preparation, higher molecular weight polyesters (4 kDa versus 3.1 kDa) were obtained when compared to Novozym 435.


2006 ◽  
Vol 39 (6) ◽  
pp. 1236-1241 ◽  
Author(s):  
David E. Stevenson ◽  
Reginald Wibisono ◽  
Dwayne J. Jensen ◽  
Roger A. Stanley ◽  
Janine M. Cooney

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