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

Mathpati, Ashwini C.; Kalghatgi, Saurabh G; Mathpati, Channamallikarjun S.; Bhanage, Bhalchandra M.

doi:10.1002/jctb.5645

Cited by 8 publications

(3 citation statements)

References 70 publications

(139 reference statements)

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“…Despite the extensive literature on theoretical and experimental analyses of the HPD process, both the knowledge of the effect of operational conditions on bioreactor behaviour-especially temperature in case of batch processes and feed temperature in case of continuous processes-and development of mathematical methods applied to assess an optimal control variables values ensuring high bioreactor performance are required for efficient design of immobilized enzyme reactor [29,30].…”

Section: Methodsmentioning

confidence: 99%

Analytical Determination of the Optimal Feed Temperature for Hydrogen Peroxide Decomposition Process Occurring in Bioreactor with a Fixed-Bed of Commercial Catalase

Grubecki

2020

Catalysts

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The hydrogen peroxide-immobilized commercial catalase system was chosen to estimate the optimal feed temperature (OFT) for fixed-bed reactor (FXBR). This feed temperature was obtained based on analytical solution by maximizing the time-averaged substrate conversion under a constant feed flow rate and temperature constraints. In calculations a set of partial differential equations describing the conservation equation for fixed-bed reactor, assuming plug flow and kinetic equation for the rate of enzyme parallel deactivation was taken into account. The model is based on kinetic, and mass-transfer parameters estimated previously in a real decomposition process of hydrogen peroxide (HP). The simulation showed that the OFT is strongly dependent on hydrogen peroxide feed concentration, feed flow rate and diffusional resistances expressed by biocatalyst global effectiveness factor. It has been shown that the more significant diffusional resistances and the higher HP conversions are, the higher the optimal feed temperature is. The calculated values of the OFT were verified with the experimental results obtained in the model reactor at selected values of the feed flow rate. Presented analysis poses a significant simplification in a numerical computational procedure and can be very useful for engineers to select the temperature condition at which bioreactor productivity is expected to be maximal.

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Section: Methodsmentioning

confidence: 99%

Analytical Determination of the Optimal Feed Temperature for Hydrogen Peroxide Decomposition Process Occurring in Bioreactor with a Fixed-Bed of Commercial Catalase

Grubecki

2020

Catalysts

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“…Biocatalysis, applied in ester synthesis, is useful and its synthetic products can be identical to natural products. Recently, a transesterification reaction catalyzed by lipase (triacylglycerol ester hydrolase, EC 3.1.1.3) has been performed to produce esters [1]. Lipase-catalyzed reactions have been applied to the synthesis of chiral drugs [2], wax esters [3], structural lipids [4] and biodiesel [5].…”

Section: Introductionmentioning

confidence: 99%

Modification of Silica Xerogels with Polydopamine for Lipase B from Candida antarctica Immobilization

et al. 2021

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Silica xerogels have been proposed as a potential support to immobilize enzymes. Improving xerogels’ interactions with such enzymes and their mechanical strengths is critical to their practical applications. Herein, based on the mussel-inspired chemistry, we demonstrated a simple and highly effective strategy for stabilizing enzymes embedded inside silica xerogels by a polydopamine (PDA) coating through in-situ polymerization. The modified silica xerogels were characterized by scanning and transmission electron microscopy, Fourier tranform infrared spectroscopy, X-ray diffraction, X-ray photoelectron spectroscopy and pore structure analyses. When the PDA-modified silica xerogels were used to immobilize enzymes of Candida antarctica lipase B (CALB), they exhibited a high loading ability of 45.6 mg/gsupport, which was higher than that of immobilized CALB in silica xerogels (28.5 mg/gsupport). The immobilized CALB of the PDA-modified silica xerogels retained 71.4% of their initial activities after 90 days of storage, whereas the free CALB retained only 30.2%. Moreover, compared with the immobilization of enzymes in silica xerogels, the mechanical properties, thermal stability and reusability of enzymes immobilized in PDA-modified silica xerogels were also improved significantly. These advantages indicate that the new hybrid material can be used as a low-cost and effective immobilized-enzyme support.

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“…Biocatalysis offers several advantages, such as high specificity, selectivity, low energy consumption, and high yield [15][16][17]. Currently, an esterification or transesterification reaction catalyzed by lipase (triacylglycerol ester hydrolase, EC 3.1.1.3) in the organic solvent has been performed to produce esters [18,19]. Lipase-catalyzed reactions have been applied to the synthesis of emulsifiers [20], wax esters [21], structural lipids [22], and biodiesel [23].…”

Section: Introductionmentioning

confidence: 99%

Continuous Production of 2-Phenylethyl Acetate in a Solvent-Free System Using a Packed-Bed Reactor with Novozym® 435

Huang

Chen

et al. 2020

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2-Phenylethyl acetate (2-PEAc), a highly valued natural volatile ester, with a rose-like odor, is widely added in cosmetics, soaps, foods, and drinks to strengthen scent or flavour. Nowadays, 2-PEAc are commonly produced by chemical synthesis or extraction. Alternatively, biocatalysis is a potential method to replace chemical synthesis or extraction for the production of natural flavour. Continuous synthesis of 2-PEAc in a solvent-free system using a packed bed bioreactor through immobilized lipase-catalyzed transesterification of ethyl acetate (EA) with 2-phenethyl alcohol was studied. A Box–Behnken experimental design with three-level-three-factor, including 2-phenethyl alcohol (2-PE) concentration (100–500 mM), flow rate (1–5 mL min−1) and reaction temperature (45–65 °C), was selected to investigate their influence on the molar conversion of 2-PEAc. Then, response surface methodology and ridge max analysis were used to discuss in detail the optimal reaction conditions for the synthesis of 2-PEAc. The results indicated both 2-PE concentration and flow rate are significant factors in the molar conversion of 2-PEAc. Based on the ridge max analysis, the maximum molar conversion was 99.01 ± 0.09% under optimal conditions at a 2-PE concentration of 62.07 mM, a flow rate of 2.75 mL min−1, and a temperature of 54.03 °C, respectively. The continuous packed bed bioreactor showed good stability for 2-PEAc production, enabling operation for at least 72 h without a significant decrease of conversion.

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

Cited by 8 publications

References 70 publications

Analytical Determination of the Optimal Feed Temperature for Hydrogen Peroxide Decomposition Process Occurring in Bioreactor with a Fixed-Bed of Commercial Catalase

Analytical Determination of the Optimal Feed Temperature for Hydrogen Peroxide Decomposition Process Occurring in Bioreactor with a Fixed-Bed of Commercial Catalase

Modification of Silica Xerogels with Polydopamine for Lipase B from Candida antarctica Immobilization

Continuous Production of 2-Phenylethyl Acetate in a Solvent-Free System Using a Packed-Bed Reactor with Novozym® 435

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