Candida antarctica lipase B catalyzed polymerization of lactones: Effects of immobilization matrices on polymerization kinetics & molecular weight

2005 ◽  
Vol 1 (2) ◽  
pp. 126-134 ◽  
Author(s):  
Takahiko Nakaoki ◽  
Ying Mei ◽  
Lisa M. Miller ◽  
Ajay Kumar ◽  
Bhanu Kalra ◽  
...  
Keyword(s):  
Molecular Weight ◽  
Candida Antarctica ◽  
Polymerization Kinetics ◽  
Candida Antarctica Lipase B ◽  
Candida Antarctica Lipase ◽  
Lipase B ◽  
Catalyzed Polymerization

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.

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.

Efficient, galactose-free production of Candida antarctica lipase B by GAL10 promoter in Δgal80 mutant of Saccharomyces cerevisiae

2009 ◽  
Vol 44 (10) ◽  
pp. 1190-1192 ◽  
Author(s):  
Jake Whang ◽  
Jungoh Ahn ◽  
Chang-Soo Chun ◽  
Yeo-Jin Son ◽  
Hongweon Lee ◽  
...  
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Candida Antarctica ◽  
Candida Antarctica Lipase B ◽  
Candida Antarctica Lipase ◽  
Lipase B

Candida antarctica lipase B-catalyzed regioselective deacylation of dihydroxybenzenes acylated at both phenolic hydroxy groups

2016 ◽  
Vol 94 (1) ◽  
pp. 44-49 ◽  
Author(s):  
Toshifumi Miyazawa ◽  
Manabu Hamada ◽  
Ryohei Morimoto
Keyword(s):  
Candida Antarctica ◽  
Candida Antarctica Lipase B ◽  
Candida Antarctica Lipase ◽  
Primary Alcohols ◽  
Lipase B ◽  
Highly Active ◽  
Direct Acylation ◽  
Acyl Acceptors ◽  
Hydroxy Groups ◽  
Phenolic Hydroxy

Candida antarctica lipase B proved to be highly active in the deacylation of substituted hydroquinones and resorcinols acylated at both phenolic hydroxy groups. The deacylation reactions were much faster than the corresponding direct acylations of these dihydroxybenzenes catalyzed by the same lipase. More importantly, they took place generally in a markedly regioselective manner: the acyloxy group remote from the substituent was preferentially cleaved. The main or exclusive products obtained were the regioisomers of those produced through the direct acylation of the dihydroxybenzenes. In the case of alkyl-substituted hydroquinone derivatives, the regioselectivity increased with an increase in the bulk of the substituent. In the case of 4-substituted diacylated resorcinols, the 3-O-monoacyl derivatives were obtained generally as the sole products. Quite interestingly, some secondary alcohols proved to act as better acyl acceptors than the corresponding primary alcohols in these enzymatic deacylations.

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