Accurel MP 1000 as a support for the immobilization of lipase from Burkholderia cepacia : Application to the kinetic resolution of myo -inositol derivatives

Manoel, Evelin Andrade; Ribeiro, Marcela F. P.; Santos, José Cleiton Sousa dos; Coelho, Maria Alice Zarur; Simas, Alessandro B. C.; Fernández‐Lafuente, Roberto; Freire, Denise Maria Guimarães

doi:10.1016/j.procbio.2015.06.023

Cited by 83 publications

(51 citation statements)

References 70 publications

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“…The enzymatic load capacity is an important economical parameter of the support, since it represents the amount of the protein that can be immobilized with one gram of the support. Thus, the enzymatic load of the support was investigated.…”

Section: Resultsmentioning

confidence: 99%

“…Lipases can be found in two different conformations: a closed one, in which the lid isolates the reaction site, and an open one, in which the lid has moved and the reaction site is exposed . The interaction with a hydrophobic interface may cause the lid to be stabilized in the open form, thus exposing the catalytic site and enabling catalysis . The lipase active site is formed by the catalytic triad Ser‐His‐Asp/Glu, while the lid is made up of one or two helixes or a loop region .…”

Section: Introductionmentioning

confidence: 99%

“…The lipase active site is formed by the catalytic triad Ser‐His‐Asp/Glu, while the lid is made up of one or two helixes or a loop region . This permits lipases to become immobilized on hydrophobic supports via interfacial activation …”

Section: Introductionmentioning

confidence: 99%

“…In modern industrial chemistry, preparing desired chiral substances is of great importance because they are intermediates for the synthesis of products with high added value such as drugs . Biocatalysis is a very attractive option for obtaining enantiomerically pure chiral drugs . Specifically, ( R )‐1‐chloro‐3‐( o ‐methoxyphenoxy)propan‐2‐ol is an intermediate in the synthesis of ( S )‐Moprolol, which is a β‐adrenergic blocking agent, used in the clinical treatment of ocular hypertension and heart problems .…”

Section: Introductionmentioning

confidence: 99%

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Kinetic resolution of drug intermediates catalyzed by lipase B from Candida antarctica immobilized on immobead‐350

Pinheiro

Rios

Fonseca

et al. 2018

Biotechnology Progress

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108

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Novozyme 435, which is a commercial immobilized lipase B from Candida antarctica (CALB), has been proven to be inadequate for the kinetic resolution of rac-indanyl acetate. As it has been previously described that different immobilization protocols may greatly alter lipase features, in this work, CALB was covalently immobilized on epoxy Immobead-350 (IB-350) and on glyoxyl-agarose to ascertain if better kinetic resolution would result. Afterwards, all CALB biocatalysts were utilized in the hydrolytic resolution of rac-indanyl acetate and rac-(chloromethyl)-2-(o-methoxyphenoxy) ethyl acetate. After optimization of the immobilization protocol on IB-350, its loading capacity was 150 mg protein/g dried support. Furthermore, the CALB-IB-350 thermal and solvent stabilities were higher than that of the soluble enzyme (e.g., by a 14-fold factor at pH 5-70°C and by a 11-fold factor in dioxane 30%-65°C) and that of the glyoxyl-agarose-CALB (e.g., by a 12-fold factor at pH 10-50°C and by a 21-fold factor in dioxane 30%-65°C). The CALB-IB-350 preparation (with 98% immobilization yield and activity versus p-nitrophenyl butyrate of 6.26 ± 0.2 U/g) was used in the hydrolysis of rac-indanyl acetate using a biocatalyst/substrate ratio of 2:1 and a pH value of 7.0 at 30°C for 24 h. The conversion obtained was 48% and the enantiomeric excess of the product (e.e. ) was 97%. These values were much higher than the ones obtained with Novozyme 435, 13% and 26% of conversion and e.e.p, respectively. © 2018 American Institute of Chemical Engineers Biotechnol. Prog., 34:878-889, 2018.

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Section: Resultsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

Kinetic resolution of drug intermediates catalyzed by lipase B from Candida antarctica immobilized on immobead‐350

Pinheiro

Rios

Fonseca

et al. 2018

Biotechnology Progress

Self Cite

108

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“…In this context, we highlight the enzymatic treatments that correspond to the most recent technology for the biological treatment of effluents (Buss & Henkes, 2014, Silva, Silva, Gois, Almeida, & Abud, 2015 by hydrolytic method reduce the concentration and degrade a large number of toxic and persistent substances (Liu et al, 2011, Baldo et al, 2013, Chen, Zhang, Xu, & Yan, 2013, Zadinelo et al, 2013. The use of immobilized lipase on a suitable support increases the process financial viability, mainly due to its reuse (reaction medium separation), it improves the thermal and mechanical properties (stability at different temperatures), operational stability, storage and the enzymatic activity (Cadena et al 2010, Hu et al, 2012, Palomino-Romero et al, 2012, Colla et al, 2014, Manoel et al, 2015, Nyari, Zeni, Steffens, Dallago, & Rigo, 2015, Shao, Jing, Tian, Zheng, & Shang, 2015, Nyari et al, 2016.…”

Section: Introductionmentioning

confidence: 99%

<b>Optimization of olive oil hydrolysis process using immobilized Lipase from <i>Burkholderia cepacia</i> sp. in Polyurethane

et al. 2017

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ABSTRACT. The aim of this study was to achieve the best conditions for the olive oil hydrolysis process at optimal pH and temperature using Burkholderia cepacia lipase immobilized in situ in rigid polyurethane support. The influences of the temperature (13.85 to 56.5ºC) and pH (4.18 to 9.82) were evaluated by a central composite rotational experimental design 2 2 . The operational stability and storage conditions were also studied. The olive oil hydrolysis process was optimized in pH 7.0, at 40°C and 15 min of reaction, with 66 and 93 U g -1 of hydrolysis activity in free and immobilized lipase, respectively, with > 700% yield. The immobilized remained stable for up to 40 days of storage at temperatures of 60 o C, and for 100 days from 4 to 25°C. The operational stability of the immobilized was 6 continuous cycles. In this way, immobilization showed to be a promising alternative for its application in olive oil hydrolysis, having storage stability and reuse capability. Otimização do processo de hidrólise do azeite de oliva utilizando lipase Burkholderia cepacia sp. imobilizada em poliuretano RESUMO. As lipases são enzimas que, naturalmente, atuam na hidrólise de óleos e gorduras, porém, em meios com quantidade baixa de água, são capazes de atuar em reações como a esterificação, alcoólise, acidólise, aminólise, entre outras. Sendo utilizadas na redução da concentração dos lipídios contidos nos efluentes, promovendo a hidrólise dos óleos e gorduras presentes. Sendo assim, o objetivo do presente estudo foi obter as melhores condições do processo de hidrólise do óleo de oliva em termos de pH e temperatura, utilizando lipase de Burkholderia cepacia imobilizada in situ em suporte rígido de poliuretano. O processo de hidrólise do óleo de oliva foi obtido utilizando as condições de pH de 7,0, temperatura de 40°C e 15 min de reação com atividade hidrolítica para a enzima livre e imobilizada de 66 e 93 U g -1 respectivamente, com rendimento de > 700%. O imobilizado apresentou estabilidade de 40 dias de estocagem nas temperaturas de 60ºC e 100 dias de armazenamento nas temperaturas entre -4 a 25ºC e a estabilidade operacional de 6 ciclos contínuos. O imobilizado se mostrou uma alternativa promissora para aplicação no processo de hidrólise frente à enzima livre, tendo estabilidade de estocagem e possibilidade de reutilização operacional.Palavras-chaves: biocatálise, lipase, imobilização in situ, poliuretano, hidrólise.

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An overview on the conversion of glycerol to value‐added industrial products via chemical and biochemical routes

Lima

Silva

Neto

et al. 2021

Biotech and App Biochem

106

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Glycerol is a common by-product of industrial biodiesel syntheses. Due to its properties, availability, and versatility, residual glycerol can be used as a raw material in the production of high value-added industrial inputs and outputs. In particular, products like hydrogen, propylene glycol, acrolein, epichlorohydrin, dioxalane and dioxane, glycerol carbonate, n-butanol, citric acid, ethanol, butanol, propionic acid, (mono-, di-, and triacylglycerols), cynamoil esters, glycerol acetate, benzoic acid, and other applications. In this context, the present study presents a critical evaluation of the innovative technologies based on the use of residual glycerol in different industries, including the pharmaceutical, textile, food, cosmetic, and energy sectors. Chemical and biochemical catalysts in the transformation of residual glycerol are explored, along with the factors to be considered regarding the choice of catalyst route used in the conversion process, aiming at improving the production of these industrial products.

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Accurel MP 1000 as a support for the immobilization of lipase from Burkholderia cepacia : Application to the kinetic resolution of myo -inositol derivatives

Cited by 83 publications

References 70 publications

Kinetic resolution of drug intermediates catalyzed by lipase B from Candida antarctica immobilized on immobead‐350

Kinetic resolution of drug intermediates catalyzed by lipase B from Candida antarctica immobilized on immobead‐350

<b>Optimization of olive oil hydrolysis process using immobilized Lipase from <i>Burkholderia cepacia</i> sp. in Polyurethane

An overview on the conversion of glycerol to value‐added industrial products via chemical and biochemical routes

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