scholarly journals Processo enzimático para produção de acetato de isoamila livre de solvente orgânico

2019 ◽  
Vol 10 (1) ◽  
pp. 129
Author(s):  
Nádia Ligianara Dewes Nyari ◽  
Josiane B. da Silva ◽  
Tainára Orlando ◽  
Suelen P. Piazza ◽  
Rogério L. Cansian ◽  
...  
Keyword(s):  
Candida Antarctica ◽  
Novozym 435 ◽  
Candida Antarctica B

Nos últimos anos, a crescente demanda por produtos naturais na indústria de alimentos incentivou esforços notáveis no desenvolvimento de processos biotecnológicos para a produção de compostos aromatizantes. O presente estudo relata a maximização da produção de acetato de isoamila por esterificação de álcool isoamílico e ácido acético em um sistema isento de solventes usando duas lipases diferentes como catalisador. A lipase Novozyme NZL-102-LYO-HQ (Candida antarctica B imobilizada em poliuretano – PU) foi comparada com a comercializada Novozym 435 e foi avaliada em termos de desempenho, rendimento e estabilidade operacional. Os efeitos nas taxas de reação mostraram valores maximizados diferentes, empregando esses dois catalisadores, no entanto as condições reacionais no que se refere a razão molar do substrato (ácido acético: álcool isoamílico), massa de catalisador e tempo de reação foram distintos. Embora Novozym 435 exibisse maior conversão inicial com relação a NZL-102-LYO-HQ, ambas formas lineares e apresentaram uma conversão superior a 90%. Para o catalisador Novozym 435 (razão molar 1:3 de ácido acético:álcool isoamílico e massa de catalisador 17% em peso) em 240 minutos e a Novozyme NZL-102-LYO-HQ (Candida antarctica B imobilizada em poliuretano – PU) (razão molar 1:5 de ácido acético:álcool isoamílico e massa de catalisador 7% em peso) em 360 minutos de reação com 10 ciclos de reutilização. Sendo assim esses resultados são de grande valia para a produção industrial, sobretudo na síntese de ésteres de cadeia média, como acetato de isoamila em diferentes preparações enzimáticas, tornando uma fonte promissora comparado com estudo apresentados na literatura aberta.

Novozym 435 displays very different selectivity compared to lipase from Candida antarctica B adsorbed on other hydrophobic supports

2009 ◽  
Vol 57 (1-4) ◽  
pp. 171-176 ◽  
Author(s):  
Zaida Cabrera ◽  
Gloria Fernandez-Lorente ◽  
Roberto Fernandez-Lafuente ◽  
Jose M. Palomo ◽  
Jose M. Guisan
Keyword(s):  
Candida Antarctica ◽  
Novozym 435 ◽  
Hydrophobic Supports ◽  
Candida Antarctica B

In situ immobilization of Candida antarctica B lipase in polyurethane foam support

2016 ◽  
Vol 124 ◽  
pp. 52-61 ◽  
Author(s):  
Nadia Ligianara D. Nyari ◽  
Ilizandra A. Fernandes ◽  
Cindy E. Bustamante-Vargas ◽  
Clarisse Steffens ◽  
Débora de Oliveira ◽  
...  
Keyword(s):  
Polyurethane Foam ◽  
Candida Antarctica ◽  
In Situ Immobilization ◽  
Candida Antarctica B ◽  
Candida Antarctica B Lipase

Effect of mutations in Candida antarctica B lipase

1998 ◽  
Vol 93 (1-2) ◽  
pp. 95-101 ◽  
Author(s):  
S Patkar ◽  
J Vind ◽  
E Kelstrup ◽  
M.W Christensen ◽  
A Svendsen ◽  
...  
Keyword(s):  
Candida Antarctica ◽  
Candida Antarctica B ◽  
Candida Antarctica B Lipase

Batch esterification of fatty acids charges under ultrasound irradiation using candida antarctica B immobilized in polyurethane foam

2014 ◽  
Vol 3 (3) ◽  
pp. 90-94 ◽  
Author(s):  
Claudia M.T. Santin ◽  
Robison P. Scherer ◽  
Nádia L.D. Nyari ◽  
Clarissa Dalla Rosa ◽  
Rogério M. Dallago ◽  
...  
Keyword(s):  
Fatty Acids ◽  
Polyurethane Foam ◽  
Ultrasound Irradiation ◽  
Candida Antarctica ◽  
Candida Antarctica B

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.

scholarly journals Immobilization of Candida antarctica B (CALB) in Silica Aerogel: Morphological Characteristics and Stability

2020 ◽  
Vol 10 (6) ◽  
pp. 6744-6756 ◽  
Keyword(s):  
Sol Gel ◽  
Morphological Characteristics ◽  
Amorphous Structure ◽  
Industrial Applications ◽  
Candida Antarctica ◽  
Type Iv ◽  
Wide Range ◽  
The Stability ◽  
Immobilized Calb ◽  
Candida Antarctica B

Enzymes have been extensively used due to their catalytic properties, and immobilization is a promising technique to enhance their catalytic activity and stability. Lipases are enzymes naturally efficient, can be employed for the production of many different molecules, and have a wide range of industrial applications thanks to their broad selectivity. The objective of the present study was to characterize the Candida antarctica B CALB immobilized obtained using the aerogel technique regarding the morphological characteristics of the aerogel silica and its stability. For this purpose, analyzes of XRD, adsorption-desorption isotherms, TGA, SEM, and stability (storage, operational, and thermal) were performed. The supports obtained have an amorphous structure and isotherm type IV. Regarding TGA, two distinct regions were obtained and studied. Aerogels showed an increase in thermal, storage, and operational stability in relation to the free enzyme and demonstrated between 8 and 12 cycles of reuse. The contribution of this work was to present the stability advantages of the immobilized CALB enzyme through the sol-gel technique.

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