Immobilization of Rhizomucor miehei lipase on a polymeric film for synthesis of important fatty acid esters: kinetics and application studies

Badgujar, Vivek C.; Badgujar, Kirtikumar C.; Yeole, Pravin M.; Bhanage, Bhalchandra M.

doi:10.1007/s00449-017-1804-0

Cited by 29 publications

(9 citation statements)

References 55 publications

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“…This may be due to the reason that excesses of lipase cover the active sites which decreases the yield as well as conversion. 103,104 Substrate structure…”

Section: Reaction Parameters Studymentioning

confidence: 99%

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A comparative study on the performance of acid catalysts in the synthesis of levulinate ester using biomass‐derived levulinic acid: a review

Gautam

Barman

Ali

2022

Biofuels Bioprod Bioref

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Non‐renewable resources have adverse effects on the environment, which result in global warming. Research has been shifted toward sustainable resources and lignocellulosic biomass is the best example of this. Lignocellulosic biomass is inexpensive, abundantly available and a rich source of carbon, which makes society less dependant on the use of fossil fuels. It is necessary for society to stop using petroleum‐based technologies and start developing more biomass‐based technologies. Lignocellulosic biomass can be converted into levulinic acid through various methods. Various value‐added chemicals are synthesized from levulinic acid, such as levulinate esters, acrylic acid, β‐acetyl acrylic acid, 1,4‐pentanediol, 2‐methyl tetrahydrofuran, γ‐valerolactone, etc. Among these, levulinate esters have received much attention owing to their broad applications as fuel additives, plasticizers and solvents in the pharmaceutical industries. Levulinate esters can be synthesized from the esterification reaction of levulinic acid and alcohol in the presence of either liquid or solid acid catalysts. Heterogeneous catalysts are favoured above homogeneous catalysts because of their properties, like being easy to separate, having good catalytic activity, being non‐corrosive to the reactor and having good recyclability. The performance of various heterogeneous catalysts such as zirconia, heteropolyacids, zeolite, carbonaceous material, resins and biocatalysts is reported in detail in the review. © 2022 Society of Chemical Industry and John Wiley & Sons, Ltd

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“…This may be due to the reason that excesses of lipase cover the active sites which decreases the yield as well as conversion. 103,104 Substrate structure…”

Section: Reaction Parameters Studymentioning

confidence: 99%

“…It can be concluded that after a certain point of loading of lipase on the substrate, an increase in the conversion is not observed. This may be due to the reason that excesses of lipase cover the active sites which decreases the yield as well as conversion 103,104 …”

Section: Catalytic Synthesis Of Levulinate Estersmentioning

confidence: 99%

A comparative study on the performance of acid catalysts in the synthesis of levulinate ester using biomass‐derived levulinic acid: a review

Gautam

Barman

Ali

2022

Biofuels Bioprod Bioref

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“…Natural-polymer-based matrices are widely used for enzyme immobilization [ 1 ] due to their practical significance in the design of biocatalytic hydrogels/membranes/vessels for industrial synthesis [ 2 , 3 ]. In addition, compared to free enzymes, immobilized ones are more resistant to environmental changes.…”

Section: Introductionmentioning

confidence: 99%

(Hydroxypropyl)methyl Cellulose-Chitosan Film as a Matrix for Lipase Immobilization—Part ΙΙ: Structural Studies

Vassiliadi

Tsirigotis-Maniecka

Symons

et al. 2022

Gels

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The present work reports on the structural study of a film made of a hybrid blend of biopolymers used as an enzyme carrier. A cellulose derivative (HPMC) and chitosan (CS) were combined in order to formulate a film on which Mucor miehei lipase was immobilized. The film was successfully used as a biocatalyst; however, little is known about the structure of the system. Therefore, small-angle X-ray scattering, Fourier transform infrared spectroscopy (FTIR), optical microscopy, and scanning electron microscopy (SEM), as well as microindentation measurements, were used to shed light on the structure of the promising biocatalyst. Among the results, intermolecular hydrogen bonds were observed between the amide groups of the two polymers and the lipase. The presence of the enzyme does not seem to affect the mechanical properties of the matrix. The used film after 35 cycles of reaction seemed to be fatigued and had lost part of its humidity, explaining the reduction of the enzyme activity.

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“…Response surface methodology (RSM) is an efficient statistical technique for modelling and optimization of multiple variables to predict optimum conditions with a minimum number of experiments. [54][55][56][57][58] Film-type immobilization has a potential for commercial application which so far has not been focused, 50 although film-coated reactors have been investigated for synthetic catalysis application. [39][40][41][42][43][44] Commercial technologies based on immobilized enzymes are based on batch operations in stirred tank reactors.…”

Section: Introductionmentioning

confidence: 99%

“…This film-type immobilization has been successfully demonstrated for synthesis of a flavour ester as well as kinetic resolution of racemic alcohols. [54][55][56][57][58] Film-type immobilization has a potential for commercial application which so far has not been focused, 50 although film-coated reactors have been investigated for synthetic catalysis application. 59,60 In this work, we attempted to coat the reactor wall with immobilized lipase for the production of flavour esters.…”

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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Immobilization of Rhizomucor miehei lipase on a polymeric film for synthesis of important fatty acid esters: kinetics and application studies

Cited by 29 publications

References 55 publications

A comparative study on the performance of acid catalysts in the synthesis of levulinate ester using biomass‐derived levulinic acid: a review

A comparative study on the performance of acid catalysts in the synthesis of levulinate ester using biomass‐derived levulinic acid: a review

(Hydroxypropyl)methyl Cellulose-Chitosan Film as a Matrix for Lipase Immobilization—Part ΙΙ: Structural Studies

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

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