scholarly journals Efficient Physisorption of Candida Antarctica Lipase B on Polypropylene Beads and Application for Polyester Synthesis

Catalysts ◽  
2018 ◽  
Vol 8 (9) ◽  
pp. 369 ◽  
Author(s):  
Simone Weinberger ◽  
Alessandro Pellis ◽  
James Comerford ◽  
Thomas Farmer ◽  
Georg Guebitz
Keyword(s):  
Molecular Weight ◽  
Reaction Time ◽  
Candida Antarctica ◽  
Candida Antarctica Lipase B ◽  
Novozym 435 ◽  
Polymerization Process ◽  
Candida Antarctica Lipase ◽  
Reaction Products ◽  
Lipase B ◽  
Conversion Rates

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.

Comparative Study between Candida antarctica Lipase B and Pseudomonas floroscens as Catalyst for Polycaprolactone Production

2012 ◽  
Vol 626 ◽  
pp. 547-550
Author(s):  
Senthil Kumar Senthil ◽  
M.H. Uzir ◽  
Z. Ahmad
Keyword(s):  
Molecular Weight ◽  
Reaction Time ◽  
Comparative Study ◽  
Ring Opening ◽  
Gradual Increase ◽  
Candida Antarctica ◽  
Novozym 435 ◽  
Lipase B ◽  
Polymerization System ◽  
Effects Of Temperature

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.

Direct acylation of flavonoid glycosides with phenolic acids catalysed by Candida antarctica lipase B (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
Keyword(s):  
Phenolic Acids ◽  
Candida Antarctica ◽  
Candida Antarctica Lipase B ◽  
Novozym 435 ◽  
Flavonoid Glycosides ◽  
Candida Antarctica Lipase ◽  
Lipase B ◽  
Direct Acylation

Combinatorial enzymic synthesis for functional testing of phenolic acid esters catalysed by Candida antarctica lipase B (Novozym 435®)

2007 ◽  
Vol 40 (5) ◽  
pp. 1078-1086 ◽  
Author(s):  
David E. Stevenson ◽  
Shanthi G. Parkar ◽  
Jingli Zhang ◽  
Roger A. Stanley ◽  
Dwayne J. Jensen ◽  
...  
Keyword(s):  
Phenolic Acid ◽  
Candida Antarctica ◽  
Candida Antarctica Lipase B ◽  
Novozym 435 ◽  
Functional Testing ◽  
Candida Antarctica Lipase ◽  
Lipase B ◽  
Enzymic Synthesis ◽  
Acid Esters

Pore-expanded SBA-15 for the immobilization of a recombinant Candida antarctica lipase B: Application in esterification and hydrolysis as model reactions

2018 ◽  
Vol 129 ◽  
pp. 12-24 ◽  
Author(s):  
Nathalia Saraiva Rios ◽  
Maisa Pessoa Pinheiro ◽  
Magno Luís Bezerra Lima ◽  
Denise Maria Guimarães Freire ◽  
Ivanildo José da Silva ◽  
...  
Keyword(s):  
Candida Antarctica ◽  
Candida Antarctica Lipase B ◽  
Candida Antarctica Lipase ◽  
Lipase B ◽  
Model Reactions

Structural effects on chemo- and enantioselectivity of Candida antarctica lipase B - Resolution of β-amino esters

2002 ◽  
Vol 80 (6) ◽  
pp. 565-570 ◽  
Author(s):  
Szilvia Gedey ◽  
Arto Liljeblad ◽  
László Lázár ◽  
Ferenc Fülöp ◽  
Liisa T Kanerva
Keyword(s):  
Key Words ◽  
Candida Antarctica ◽  
Diisopropyl Ether ◽  
The Other ◽  
Candida Antarctica Lipase B ◽  
Candida Antarctica Lipase ◽  
Structural Effects ◽  
Lipase B ◽  
Amino Esters ◽  
Catalyzed Reactions

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.

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