Synthesis of butyl butyrate in batch and continuous enzymatic reactors using Thermomyces lanuginosus lipase immobilized in Immobead 150

Matte, Carla Roberta; Bordinhão, Carolina; Poppe, Jakeline Kathiele; Rodrigues, Rafael C.; Hertz, Plinho Francisco; Ayub, Marco Antônio Záchia

doi:10.1016/j.molcatb.2016.02.016

Cited by 57 publications

(43 citation statements)

References 43 publications

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“…The substrate, kept in a circulating water bath, was pumped at a fixed flow rate of 0.15 mL min −1 . The amounts of Tween‐80 and the organic solvents were chosen based on previous reports …”

Section: Methodsmentioning

confidence: 99%

Enzymatic synthesis of ethyl esters from waste oil using mixtures of lipases in a plug‐flow packed‐bed continuous reactor

Poppe

Matte

Freitas

et al. 2018

Biotechnology Progress

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This work describes the continuous synthesis of ethyl esters via enzymatic catalysis on a packed-bed continuous reactor, using mixtures of immobilized lipases (combi-lipases) of Candida antarctica (CALB), Thermomyces lanuginosus (TLL), and Rhizomucor miehei (RML). The influence of the addition of glass beads to the reactor bed, evaluation of the use of different solvents, and flow rate on reaction conditions was studied. All experiments were conducted using the best combination of lipases according to the fatty acid composition of the waste oil (combi-lipase composition: 40% of TLL, 35% of CALB, and 25% of RML) and soybean oil (combi-lipase composition: 22.5% of TLL, 50% of CALB, and 27.5% of RML). The best general reaction conditions were found to be using tert-butanol as solvent, and the flow rate of 0.08 mL min . The combi-lipase reactors operating at steady state for over 30 days (720 h), kept conversion yields of ∼50%, with average productivity of 1.94 g h , regardless of the type of oil in use. © 2018 American Institute of Chemical Engineers Biotechnol. Prog., 34:952-959, 2018.

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Section: Methodsmentioning

confidence: 99%

Enzymatic synthesis of ethyl esters from waste oil using mixtures of lipases in a plug‐flow packed‐bed continuous reactor

Poppe

Matte

Freitas

et al. 2018

Biotechnology Progress

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“…We have selected Immobead‐350 (IB‐350) as support to immobilize CALB. This support presents good properties to permit a certain multipoint covalent attachment between the enzyme and the epoxides groups on the surface of a solid support . The IB‐350 beads, a crosslinked copolymer of methacrylate, presents ∼2,300 μmol of epoxy groups per gram of support, is remarkably thermal stable and has a high hydrophobicity.…”

Section: Introductionmentioning

confidence: 99%

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

Pinheiro

Rios

Fonseca

et al. 2018

Biotechnology Progress

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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“…These investigations can clarify the effect of individual variables on the desired output such as conversion and selectivity, but may not really account for the interactive effects between the variables. [46][47][48][49][50][51][52][53] In the current work, immobilization of various lipases was carried out on a biodegradable polymer blend in the form of a film rather than spherical beads. 37,38 The RSM tool helps in independent parameter optimization and quantifying the effect of parameter interaction on response variables and has been used widely for enzymatic processes.…”

Section: Introductionmentioning

confidence: 99%

Immobilized lipase catalyzed synthesis of n‐amyl acetate: parameter optimization, heterogeneous kinetics, continuous flow operation and reactor modeling

Mathpati

Kalghatgi

Mathpati

et al. 2018

J of Chemical Tech & Biotech

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BACKGROUND The work describes the synthesis of n‐amyl acetate from n‐amyl alcohol, a byproduct of the sugar industry. The synthesis was carried out using Burkholderia cepacia lipase immobilized on a hydrophobic polymer support containing hydroxypropyl methyl cellulose and polyvinyl alcohol. The reaction conditions were optimized and intrinsic kinetics were evaluated. An immobilized lipase‐coated film reactor was designed and evaluated for continuous flow synthesis. An attempt has been made to model the coated film reactor based on axial dispersion method. RESULTS The reaction conditions were optimized using a central composite design‐based response surface method. The optimum conditions for a maximum conversion of 99.5% were an acyl donor : alcohol ratio of 2:1, temperature 50 °C and catalyst loading 40 mg in n‐hexane. The intrinsic kinetics of reaction were fitted using an order bi–bi model with alcohol inhibition. The continuous flow synthesis was carried out in a coated film reactor with residence times ranging from 12 min to 60 min with per pass conversions of 5.6% and 22%, respectively. The catalyst was successfully recycled for five cycles. CONCLUSION The activation energy of the reaction was found to be 15.48 kJ mol−1. The productivity from batch and continuous flow reactor were found to be 8.16 and 6.54 mmol g−1 h−1. © 2018 Society of Chemical Industry

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Synthesis of butyl butyrate in batch and continuous enzymatic reactors using Thermomyces lanuginosus lipase immobilized in Immobead 150

Cited by 57 publications

References 43 publications

Enzymatic synthesis of ethyl esters from waste oil using mixtures of lipases in a plug‐flow packed‐bed continuous reactor

Enzymatic synthesis of ethyl esters from waste oil using mixtures of lipases in a plug‐flow packed‐bed continuous reactor

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

Immobilized lipase catalyzed synthesis of n‐amyl acetate: parameter optimization, heterogeneous kinetics, continuous flow operation and reactor modeling

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