Systemic Concocting of Cross‐Linked Enzyme Aggregates of Candida antarctica Lipase B (Novozyme 435) for the Biomanufacturing of Rhamnolipids

2019 ◽  
Vol 22 (3) ◽  
pp. 477-490 ◽  
Author(s):  
Abiram Karanam Rathankumar ◽  
Sundar SaiLavanyaa ◽  
Kongkona Saikia ◽  
Anusha Gururajan ◽  
Subramanian Sivanesan ◽  
...  
Keyword(s):  
Candida Antarctica ◽  
Candida Antarctica Lipase B ◽  
Candida Antarctica Lipase ◽  
Lipase B ◽  
Novozyme 435

scholarly journals Immobilization of Candida antarctica Lipase B on Silicone Nanofilaments

2021 ◽  
Vol 2021 ◽  
pp. 1-8
Author(s):  
Noah U. Naef ◽  
Stefan Seeger
Keyword(s):  
Surface Area ◽  
Candida Antarctica ◽  
Candida Antarctica Lipase B ◽  
High Signal ◽  
Candida Antarctica Lipase ◽  
Lipase B ◽  
Detection Systems ◽  
Novozyme 435 ◽  
The Impact ◽  
Enzyme Layer

Candida antarctica lipase B was immobilized on a series of silicone nanofilament-coated matrices of different porosities. In addition to creating a more open surface, SNF’s hydrophobicity allows for a simple immobilization pathway via adsorption. In order to study the impact of the nanostructure, the performance was compared with control samples lacking SNFs. For all materials, the surface was characterized with BET measurements, and the immobilized enzyme was measured as well as the catalytic activity. Enzyme loads ranged between 3.85% w / w and 2.53% w / w and decreased with the decreasing surface area of the carrier material from 200 m2/g to 0.04 m2/g, while the activity per enzyme increases from 824 U to 2040 U. The data suggest that the coating seals off inner surfaces, forcing the enzyme to be immobilized at more accessible positions allowing for higher activity per enzyme. Optimization of the immobilization conditions allowed us to create a thinner enzyme layer which further improved the activity per enzyme to 3129 U. While this activity is comparable to the commercial Novozyme 435 with 3073 U, the SNF-based system performs the catalysis in a thin surface layer of around 13 μm. A favorite area of application is, for example, the creation of enzyme-based detection systems, where the high activity per surface area of up to 89622 U · mg/m2 would lead to high signal strength.

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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