Evaluation of reaction parameters and kinetic modelling for Novozym 435 catalysed synthesis of isoamyl butyrate

Bansode, Sneha R.; Hardikar, Mukta A; Rathod, Virendra K.

doi:10.1002/jctb.5125

Cited by 28 publications

(19 citation statements)

References 28 publications

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“…In order to promote mass transfer while safeguarding the biocatalyst from mechanical breakdown, all the assays were performed at 350 rpm. 20,21 Four commercial immobilized lipases were used:…”

Section: Experimental Datamentioning

confidence: 99%

A simplified kinetic model to describe the solvent‐free enzymatic synthesis of wax esters

Serrano‐Arnaldos

Murcia

Ortega‐Requena

et al. 2021

J of Chemical Tech & Biotech

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BACKGROUND: The use of biotechnological processes at industrial scale is a promising tool to replace conventional synthesis as an efficient and eco-friendly technology. For that purpose, the kinetic modelling of an in-lab optimized enzymatic process prior to scaling-up is of great utility. RESULTS: In this work, a kinetic model for the solvent-free synthesis of cetyl laurate, myristate, palmitate and stearate using different commercial immobilized lipases has been developed. In order to describe the esterification process of the cetyl esters separately and as a mixture similar to natural spermaceti, a pseudo-first-order kinetic has been proposed and tested. A relation between the inverse values of the kinetic constant and the amount of biocatalyst has been observed. The effect of temperature on the reaction rate can be accurately described by the Arrhenius equation except for immobilized Thermomyces lanuginosus, which appears to be less resistant to temperatures above 70°C.CONCLUSION: Low deviations between experimental and predicted values (R 2 ≥ 0.99) indicate that this pseudo-first-order kinetic model can be considered valid for the data range studied. In addition, the reaction rate of spermaceti can be successfully predicted through a weighted average of the kinetic constants obtained during the synthesis of each cetyl ester. This simple but accurate kinetic model for describing the solvent-free enzymatic biosynthesis of wax esters from spermaceti may contribute to extending the application of lipases as industrial catalysts.

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Section: Experimental Datamentioning

confidence: 99%

A simplified kinetic model to describe the solvent‐free enzymatic synthesis of wax esters

Serrano‐Arnaldos

Murcia

Ortega‐Requena

et al. 2021

J of Chemical Tech & Biotech

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“…[67][68][69] The model constants were estimated using a least-squares curve-fitting method in MATLAB. [67][68][69] The model constants were estimated using a least-squares curve-fitting method in MATLAB.…”

Section: Intrinsic Kinetics Of N-amyl Acetate Synthesismentioning

confidence: 99%

“…Based on the available literature, the ping-pong bi-bi model and order bi-bi model with n-amyl alcohol inhibition were studied in this work. [67][68][69] The model constants were estimated using a least-squares curve-fitting method in MATLAB. The regression coefficient values were 0.87 (ping pong bi-bi model) and 0.95 (order bi-bi model).…”

Section: Intrinsic Kinetics Of N-amyl Acetate Synthesismentioning

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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“…But with an increase in enzyme concentration there is inefficient mixing that limits the mass transfer, effectual contact and diffusion of substrates and enzyme that cause conversion rate to decrease. 19 Agglomeration of immobilised lipase and inefficient exposure of surplus enzyme active sites is also responsible for lower conversions at higher lipase loading. 14…”

Section: Effect Of Catalysts Loadingmentioning

confidence: 99%

“…The G calculated at different temperatures was almost similar and in the range of 110−113 kJ mol −1 . 19…”

Section: Determination Of Thermodynamic Parametersmentioning

confidence: 99%

Solvent free lipase catalyzed synthesis of butyl caprylate

2017

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The ester, butyl caprylate has wide applications in commercial market and it also possesses characteristic fruity flavor. The work exhibits the effect of various reaction parameters and the optimization study for the synthesis of butyl caprylate in presence of bio-catalyst. To achieve maximum conversion the optimum parameters thus established include; temperature 60 • C, mole ratio of caprylic acid and butanol as 1:2, lipase loading 2% (w/v), 250 rpm speed of agitation and 4g of molecular sieves. The immobilized enzyme was also recycled and reused for 7 cycles with only 30% loss from its initial activity. The thermodynamic parameters at different temperatures were also determined. The esterification was conducted successfully with 92% as maximum conversion in 5 h in a stirred batch reactor under solvent free system and in presence of molecular sieves that was used to adsorb water formed in reaction.

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Evaluation of reaction parameters and kinetic modelling for Novozym 435 catalysed synthesis of isoamyl butyrate

Cited by 28 publications

References 28 publications

A simplified kinetic model to describe the solvent‐free enzymatic synthesis of wax esters

A simplified kinetic model to describe the solvent‐free enzymatic synthesis of wax esters

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

Solvent free lipase catalyzed synthesis of butyl caprylate

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