Displaying Candida antarctica lipase B on the cell surface of Aspergillus niger as a potential food-grade whole-cell catalyst

2014 ◽  
Vol 41 (4) ◽  
pp. 711-720 ◽  
Author(s):  
Zhi-You Pan ◽  
Zhi-Ming Yang ◽  
Li Pan ◽  
Sui-Ping Zheng ◽  
Shuang-Yan Han ◽  
...  
Keyword(s):  
Aspergillus Niger ◽  
Cell Surface ◽  
Candida Antarctica ◽  
Candida Antarctica Lipase B ◽  
Candida Antarctica Lipase ◽  
Lipase B ◽  
Whole Cell ◽  
Food Grade ◽  
Potential Food

Production of Omega-3 Triacylglycerol Concentrates using a New Food Grade Immobilized Candida antarctica Lipase B

2010 ◽  
Vol 63 (6) ◽  
pp. 922 ◽  
Author(s):  
Jaroslav A. Kralovec ◽  
Weijie Wang ◽  
Colin J. Barrow
Keyword(s):  
Fatty Acids ◽  
Candida Antarctica ◽  
Packed Bed Reactor ◽  
Candida Antarctica Lipase B ◽  
Candida Antarctica Lipase ◽  
Omega 3 ◽  
Lipase B ◽  
Food Grade ◽  
Commercial System ◽  
Immobilized Candida Antarctica Lipase

Triacylglycerol concentrates of eicosapentaenoic and docosahexaenoic omega-3 fatty acids were synthesized either via transesterification or esterification of glycerol with the corresponding ethyl ester or free fatty acid concentrates, respectively. A newly developed food grade immobilized Candida antarctica lipase B system using an Amberlite FPX-66 hydrophobic matrix, was compared with a commercially available non-food grade commercial system, for their ability to catalyze these reactions. For either system, the transesterification required higher temperature (90°C) than esterification (70°C) to achieve maximum triacylglycerol yields. The newly developed immobilized system efficiently catalyzes the esterification of free fatty acids with glycerol and differs from the existing commercial system in that it is food grade and has a more uniform and larger particle distribution. The new system significantly improves flow in a packed bed reactor, enabling multiple reuse of the catalyst for up to 80 repeats.

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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