Preparation of a biocatalyst via physical adsorption of lipase from Thermomyces lanuginosus on hydrophobic support to catalyze biolubricant synthesis by esterification reaction in a solvent-free system

Lage, Flávia Arantes Pires; Bassi, Jaquelinne J.; Corradini, Maria Carolina Cucatti; Todero, Larissa Midiane; Luiz, Jaine Honorata Hortolan; Mendes, Adriano A.

doi:10.1016/j.enzmictec.2015.12.007

Cited by 142 publications

(56 citation statements)

References 51 publications

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“…This observation can be explained on the basis of Le Chateliêr's principle: when the concentration of a reagent in the reaction medium is increased, the equilibrium of the system will shift, resulting in higher molar conversion. Such results are in agreement with data reported in literature, in particular with the results reported by Lage et al [15] concerning the enzymatic synthesis of isoamyl oleate by Thermomyces lanuginosus lipase immobilized on poly(propyl methacrylate). The authors reported that the increase in acid concentration in the reaction medium (0.5-2 mol L -1 ) led to higher molar conversion.…”

Section: Modelingsupporting

confidence: 93%

Synthesis of Isopropyl Palmitate by Lipase Immobilized on a Magnetized Polymer Matrix

et al. 2020

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Penicillium camemberti lipase immobilized on a magnetized poly(styrene‐co‐divinylbenzene) was used as a biocatalyst for isopropyl palmitate synthesis. The reaction conditions were determined by 22 factorial central composite design. A mathematical model based on a simplified kinetic approach was developed to describe the system and validated with the experimental data. An assay carried out in a stirred‐tank reactor confirmed the proposed model. The ester was purified and the properties such as density and water content were similar to those found in commercially available isopropyl palmitate.

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Section: Modelingsupporting

confidence: 93%

Synthesis of Isopropyl Palmitate by Lipase Immobilized on a Magnetized Polymer Matrix

et al. 2020

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“…M540-PS is a preparation made by adsorption, thus enzyme leaking can occur during the washing steps, which can lead to reduced enzyme activity. These results show stronger interaction of the enzyme with the support activated with PDE, but maybe incorrect elimination of the remaining compounds during the washing steps, which led to almost 40 % activity decrease after 5 cycles [61].…”

Section: Reusability Of Lipase Ps Biocatalystsmentioning

confidence: 91%

Bisepoxide-activated Hollow Silica Microspheres for Covalent Immobilization of Lipase from Burkholderia cepacia

Nagy

Szabó

Bugovics

et al. 2019

Period. Polytech. Chem. Eng.

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An efficient and easy-to-perform method was developed for covalent immobilization of lipase from Burkholderia cepacia (Lipase PS) on hollow silica microspheres (M540) by bisepoxide activation. For immobilization, various bisepoxides of different length, rigidity and hydrophobicity in their linkers were applied to activate the amino groups on the M540 support. Effect of the individual bisepoxides on the catalytic performance of the immobilized Lipase PS was studied by using lipase-catalyzed kinetic resolution (KR) of racemic 1-phenylethanol (rac-1) with vinyl acetate in batch mode. Catalytic activity, enantiomer selectivity, recyclability and thermal stability of the new immobilized Lipase PS biocatalysts were investigated. The optimal enzyme / support ratio with the support activated by the most efficient bisepoxide, i.e. poly(ethylene glycol) diglycidyl ether (PDE), was 1:5. The most efficient Lipase PS on PDE activated M540 showed an almost five fold higher biocatalytic activity value (rbatch = 42.8 U/g) with enhanced selectivity (ee(R)-2 = 99.1 %) to the free form of Lipase PS (rbatch = 9.0 U/g; ee(R)-2 = 98.9 %). The Lipase PS on PDE-M540 was compared to a commercially available immobilized Lipase PS biocatalyst (Lipobond Lipase PS) and also applied in a packed-bed enzyme reactor operated in continuous-flow mode, where the optimal temperature of M540-PDE-PS reached the 70 °C, while the optimum for Lipobond Lipase PS was 50 °C.

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“…Although immobilization has proven to be advantageous in some cases, it is important to recognize that the support and immobilization process add additional cost to the biocatalyst and this should always be taken into consideration when assessing the feasibility of a process. Furthermore, although most immobilization supports allow for high protein loadings due to their large specific surface areas, internal diffusion limitations frequently make such high loadings ineffective [67,68]. As a result, immobilization often limits the amount of enzyme that can be loaded into a reactor, compared to soluble enzymes.…”

Section: Immobilizationmentioning

confidence: 99%

Reactor Selection for Effective Continuous Biocatalytic Production of Pharmaceuticals

Lindeque

Woodley

2019

Catalysts

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Enzyme catalyzed reactions are rapidly becoming an invaluable tool for the synthesis of many active pharmaceutical ingredients. These reactions are commonly performed in batch, but continuous biocatalysis is gaining interest in industry because it would allow seamless integration of chemical and enzymatic reaction steps. However, because this is an emerging field, little attention has been paid towards the suitability of different reactor types for continuous biocatalytic reactions. Two types of continuous flow reactor are possible: continuous stirred tank and continuous plug-flow. These reactor types differ in a number of ways, but in this contribution, we focus on residence time distribution and how enzyme kinetics are affected by the unique mass balance of each reactor. For the first time, we present a tool to facilitate reactor selection for continuous biocatalytic production of pharmaceuticals. From this analysis, it was found that plug-flow reactors should generally be the system of choice. However, there are particular cases where they may need to be coupled with a continuous stirred tank reactor or replaced entirely by a series of continuous stirred tank reactors, which can approximate plug-flow behavior. This systematic approach should accelerate the implementation of biocatalysis for continuous pharmaceutical production.Catalysts 2019, 9, 262 2 of 17 counterparts) and thereby the use of flow technology is hard to justify. In reality, the arguments for flow technology are perhaps a little different for enzymes and, in this brief review, we will discuss the issue of reactor selection, in order to capitalize upon the benefits of both flow technology and biocatalysis. Downstream unit operations are not included in this discussion. Figure 1 shows schematic diagrams of the three ideal reactor types, namely the batch stirred tank reactor (BSTR), the continuous stirred tank reactor (CSTR) and the continuous plug-flow reactor (CPFR). The characteristics of these reactors have been described in extensive detail elsewhere [18] and will therefore be only briefly summarized here. Reactor TypesCatalysts 2019, 9, x FOR PEER REVIEW 2 of 17 (compared to their chemical counterparts) and thereby the use of flow technology is hard to justify. In reality, the arguments for flow technology are perhaps a little different for enzymes and, in this brief review, we will discuss the issue of reactor selection, in order to capitalize upon the benefits of both flow technology and biocatalysis. Downstream unit operations are not included in this discussion. Reactor Types

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Preparation of a biocatalyst via physical adsorption of lipase from Thermomyces lanuginosus on hydrophobic support to catalyze biolubricant synthesis by esterification reaction in a solvent-free system

Cited by 142 publications

References 51 publications

Synthesis of Isopropyl Palmitate by Lipase Immobilized on a Magnetized Polymer Matrix

Synthesis of Isopropyl Palmitate by Lipase Immobilized on a Magnetized Polymer Matrix

Bisepoxide-activated Hollow Silica Microspheres for Covalent Immobilization of Lipase from Burkholderia cepacia

Reactor Selection for Effective Continuous Biocatalytic Production of Pharmaceuticals

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