Benzyl butyrate esterification mediated by immobilized lipases: Evaluation of batch and fed-batch reactors to overcome lipase-acid deactivation

Meneses, Alessandra Cristina de; Sá, Amanda Gomes Almeida; Lerin, Lindomar Alberto; Corazza, Marcos L.; Araújo, Pedro Henrique Hermes de; Sayer, Cláudia; Oliveira, Débora de

doi:10.1016/j.procbio.2018.12.029

Cited by 25 publications

(12 citation statements)

References 37 publications

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“…On the other hand, Figure 2 also shows that the enzymatic reaction stops after 6 h of reaction, which could be attributed to an enzyme deactivation caused by the acid [7] or to alcohol evaporation [5]. Related to the first hypothesis, several studies have described the irreversible inactivation of CalB caused by the high polarity of short-chain acids, such as heptanoic, butyric, propionic and other acids [7,[17][18][19]. It has been demonstrated that lipase is not able to catalyze esterification reactions with acids exhibiting a pKa value less than 4.8.…”

Section: Biocatalytic Synthesis Of 2-ethylhexyl 2-methylhexanoatementioning

confidence: 98%

“…Based on previous studies [7], and in order to increase the final conversion, the acid was added in two equal fractions, the first at the beginning of the reaction and the second when the acid had been consumed. The synthesis was carried Related to the first hypothesis, several studies have described the irreversible inactivation of CalB caused by the high polarity of short-chain acids, such as heptanoic, butyric, propionic and other acids [7,[17][18][19]. It has been demonstrated that lipase is not able to catalyze esterification reactions with acids exhibiting a pKa value less than 4.8.…”

Section: Biocatalytic Synthesis Of 2-ethylhexyl 2-methylhexanoatementioning

confidence: 99%

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Sustainable Biocatalytic Procedure for Obtaining New Branched Acid Esters

et al. 2021

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Biocatalytic synthesis of 2-ethylhexyl 2-methylhexanoate is described in this work for the first time. This branched-chain ester is suitable for use at low temperatures in numerous applications. The immobilized lipase Novozym® 435 has demonstrated its ability to catalyze the ester synthesis from 2-ethylhexanol and 2-methylhexanoic acid in a solvent-free medium. The high reaction times that are required result in a loss of alcohol by evaporation, which must be compensated for with an excess of this substrate if high conversions are to be achieved. Therefore, two strategies are established: 70 °C with a 10% excess of alcohol, which requires a longer operating time and provides conversions of 97%, and 80 °C with a 20% excess of alcohol, which allows for the achievement of a 99% conversion in a shorter time. The optimal reaction conditions have been chosen based on reusability of the enzyme, process productivity, green metrics and preliminary economic study. When the synthesis is carried out under the best conditions (70 °C, 10% molar excess of alcohol and six uses of the immobilized enzyme) a productivity of 203.84 kg product × kg biocatalyst−1 is attained. The biocatalytic procedure matches many of the objectives of “green chemistry” and is suitable to be scaled up and used in industrial manufacturing.

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Section: Biocatalytic Synthesis Of 2-ethylhexyl 2-methylhexanoatementioning

confidence: 98%

Section: Biocatalytic Synthesis Of 2-ethylhexyl 2-methylhexanoatementioning

confidence: 99%

Sustainable Biocatalytic Procedure for Obtaining New Branched Acid Esters

et al. 2021

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“…On the other side, an excess of lipase can generate its agglomeration and thus hinder the access of substrates to the enzyme [7,[26][27], negatively interfering with the rate of the substrate. Therefore, the amount of lipase should be controlled to ensure high conversions and low cost [4,28]. In order to further reduce the amount of lipase used, the reaction kinetics for the effect of the amount of enzyme was evaluated using the condition optimized in the previous step, that is, run 13 (Table 1; molar ratio of 1:2 (acid to alcohol), 70 °C, 600 rpm) and reaction time of up to 48 H. The results are shown in Fig.…”

Section: Influence Of Enzyme Concentrationmentioning

confidence: 99%

Optimization, kinetic, and scaling‐up of solvent‐free lipase‐catalyzed synthesis of ethylene glycol oleate emollient ester

Cordeiro

Henriques

Deucher

et al. 2020

Biotechnology and Applied Biochemistry

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The use of enzymatic catalysts is an alternative to chemical catalysts as they can help to obtain products with less environmental impact, considered sustainable within the concept of green chemistry. The optimization, kinetic, lipase reuse, and scale-up of enzymatic production of ethylene glycol oleate in the batch mode were carried out using the NS 88011 lipase in a solvent-free system. For the optimization step, a 2 3 Central Composite Design was used and the optimized condition for the ethylene glycol oleate production, with conversions above 99%, was at 70 °C, 600 rpm, substrates molar ratio of 1:2, 1 wt% of NS 88011 in 32 H of reaction. Kinetic tests were also carried out with different amounts of enzyme, and it showed that by decreasing the amount of the enzyme, the conversion also decreases. The lipase reuse showed good conversions until the second cycle of use, after which it had a progressive reduction reaching 83% in the fourth cycle of use. The scale-up (ninefold increase) showed promising results, with conversion above 99%, achieving conversions similar to small-scale reactions. Therefore, this work proposed an environmentally safe route to produce an emollient ester using a low-cost biocatalyst in a solvent-free system.

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“…6 Cristina de Meneses et al reported the enzyme-catalyzed synthesis of benzyl butyrate (>80%) from benzyl alcohol and butyric acid in a solvent-free system (SFS) with good yields, using the commercially available Novozym 435 [lipase B from C. antarctica (CaL-B) immobilized on a macroporous resin]. 26 In order to solve many enzyme limitations, such as the risk of contamination with proteins from the denaturated enzyme, low stability, activity and/or selectivity, and inactivation by chemicals, the enzyme can be immobilized by affinity-tag binding, adsorption, inclusion, covalent binding, cross-linking, or a mix of the five immobilization techniques on/in various supports. 27−30 Out of the impressive diversity of immobilization techniques developed in the past years, 31 the encapsulation of enzymes in sol−gel enjoys special attention.…”

Section: ■ Introductionmentioning

confidence: 99%

Green Process for the Enzymatic Synthesis of Aroma Compounds Mediated by Lipases Entrapped in Tailored Sol–Gel Matrices

Dudu

Lăcătuş

Bencze

et al. 2021

ACS Sustainable Chem. Eng.

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We report a simple enzymatic procedure for the synthesis of short-chained flavor esters by direct esterification of natural acids with short-chain primary alcohols mediated by lipase B from Candida antarctica entrapped in a tailored sol–gel matrix in the presence of three additives, using vacuum for water removal. Maximal immobilization yields (100%) were obtained for all three biocatalysts, while the enzyme loading and the synthetic activity depend on the used additive (6.7, 7.6, and 7.7 μg enzyme/mg biocatalyst for β-cyclodextrin, polyvinyl alcohol, and glycerol, respectively, and 76–110% recovered activity as compared with free lipase). The process was optimized using the reaction of hexan-1-ol with butyric acid as the model with significant conversion improvements (from <40% to >94%) reducing the alcohol/enzyme ratio (from 100:1 to 25:1 weight ratio) for all novel biocatalysts. Other short-chain flavor esters were prepared with excellent yields (>90%) under the previously established optimal conditions. Atom economy (90.53), E-factor (17.22), atom efficiency (88.36), mass intensity (18.58), and reaction mass efficiency (60.07) as relevant sustainability metrics were calculated for the preparative scale model reaction with glycerol as the additive. Based on our results, this green and sustainable new approach can be used for the synthesis of many flavor esters.

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Benzyl butyrate esterification mediated by immobilized lipases: Evaluation of batch and fed-batch reactors to overcome lipase-acid deactivation

Cited by 25 publications

References 37 publications

Sustainable Biocatalytic Procedure for Obtaining New Branched Acid Esters

Sustainable Biocatalytic Procedure for Obtaining New Branched Acid Esters

Optimization, kinetic, and scaling‐up of solvent‐free lipase‐catalyzed synthesis of ethylene glycol oleate emollient ester

Green Process for the Enzymatic Synthesis of Aroma Compounds Mediated by Lipases Entrapped in Tailored Sol–Gel Matrices

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