Activity and stability of chemically modified Candida antarctica lipase B adsorbed on solid supports

1999 ◽  
Vol 52 (6) ◽  
pp. 791-796 ◽  
Author(s):  
B. C. Koops ◽  
E. Papadimou ◽  
H. M. Verheij ◽  
A. J. Slotboom ◽  
M. R. Egmond
Keyword(s):  
Candida Antarctica ◽  
Candida Antarctica Lipase B ◽  
Candida Antarctica Lipase ◽  
Lipase B ◽  
Solid Supports ◽  
Chemically Modified

Over-Stabilization of Chemically Modified and Cross-Linked Candida antarctica Lipase B Using Various Epoxides and Diepoxides

2009 ◽  
Vol 62 (8) ◽  
pp. 799 ◽  
Author(s):  
Nemanja Miletić ◽  
Katja Loos
Keyword(s):  
Thermal Stability ◽  
Kinetic Resolution ◽  
Structural Rearrangement ◽  
Candida Antarctica ◽  
Candida Antarctica Lipase B ◽  
Cross Linking ◽  
Candida Antarctica Lipase ◽  
Lipase B ◽  
Chemically Modified ◽  
Spacer Arm

Candida antarctica lipase B, Cal-B, was (i) chemically modified with various epoxides, or (ii) cross-linked with various diepoxides in order to improve enzyme activity and thermal stability. Changed enzyme structure was confirmed by kinetic resolution of p-nitrophenol acetate with methanol and determination of the kinetic parameters. Thermal stability measurements were carried out for each Cal-B derivative, proving that Cal-B modified with 1,2-epoxypropane and 1,2-epoxypentane, and cross-linked with 1,2,7,8-diepoxyoctane and 1,2,9,10-diepoxydecane showed higher stability than soluble enzyme. The influence of the length of the epoxide arm in the modification process, as well as the length of the spacer arm in the cross-linking process, on the final enzyme preparation properties was investigated. The amount of epoxides and diepoxides used for structural rearrangement played an important role in the derivatives’ characteristics. The influence of the precipitant used and the presence of additives, such as surfactant or crown-ether, during modification and cross-linking processes was also revealed.

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
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