Design of a lipase-nano particle biocatalysts and its use in the kinetic resolution of medicament precursors

Bezerra, Rayanne Mendes; Neto, Davino M. Andrade; Galvão, Wesley S.; Rios, Nathália Saraiva; Carvalho, Ana Caroline Lustosa de Melo; Corrêa, M.A.; Bohn, F.; Fernández-Lafuente, Roberto; Fechine, Pierre Basílio Almeida; Mattos, Marcos Carlos de; Santos, José Cleiton Sousa dos; Gonçalves, Luciana Rocha Barros

doi:10.1016/j.bej.2017.05.024

Cited by 83 publications

(29 citation statements)

References 50 publications

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“…At the end of each cycle, the biocatalyst was separated from the reaction medium by vacuum filtration using filter paper. Then, the biocatalyst was washed three times with hexane, dried again in vacuo and then taken to the desiccator where it was held for 30 min [102].…”

Section: Operational Stability Of the Biocatalystmentioning

confidence: 99%

Optimization of the Production of Enzymatic Biodiesel from Residual Babassu Oil (Orbignya sp.) via RSM

et al. 2020

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Residual oil from babassu (Orbignya sp.), a low-cost raw material, was used in the enzymatic esterification for biodiesel production, using lipase B from Candida antarctica (Novozym® 435) and ethanol. For the first time in the literature, residual babassu oil and Novozym® 435 are being investigated to obtain biodiesel. In this communication, response surface methodology (RSM) and a central composite design (CCD) were used to optimize the esterification and study the effects of four factors (molar ratio (1:1–1:16, free fatty acids (FFAs) /alcohol), temperature (30–50 °C), biocatalyst content (0.05–0.15 g) and reaction time (2–6 h)) in the conversion into fatty acid ethyl esters. Under optimized conditions (1:18 molar ratio (FFAs/alcohol), 0.14 g of Novozym® 435, 48 °C and 4 h), the conversion into ethyl esters was 96.8%. It was found that after 10 consecutive cycles of esterification under optimal conditions, Novozym® 435 showed a maximum loss of activity of 5.8%, suggesting a very small change in the support/enzyme ratio proved by Fourier Transform Infrared (FTIR) spectroscopy and insignificant changes in the surface of Novozym® 435 proved by scanning electron microscopy (SEM) after the 10 consecutive cycles of esterification.

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Section: Operational Stability Of the Biocatalystmentioning

confidence: 99%

Optimization of the Production of Enzymatic Biodiesel from Residual Babassu Oil (Orbignya sp.) via RSM

et al. 2020

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“…For this reason, the most common method of retaining enzymes within a reactor is by binding them to larger carrier particles that are easier to separate from the reactor effluent than the soluble enzyme. Recently, the use of paramagnetic nanoparticles as supports has received much attention due to their high specific surface areas and simple retention within the reactor by a magnetic field [54]. Numerous methods and support materials have been described for the immobilization of a wide variety of enzymes [55].…”

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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“…Among enzymes, the use of lipases as biocatalysts has been gaining prominence in the recent years, since they operate in different types of solvents (ionic liquids, supercritical fluids, organic solvents, and the least contaminant aqueous media), with many different substrates and being able to catalyze a broad range of reactions [ 9 , 10 , 11 ]. The use of lipases as catalysts results in selective synthesis, with low to no production of undesirable byproducts and being environmentally safe [ 12 ].…”

Section: Introductionmentioning

confidence: 99%

Synthesis of Benzyl Acetate Catalyzed by Lipase Immobilized in Nontoxic Chitosan-Polyphosphate Beads

et al. 2017

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Enzymes serve as biocatalysts for innumerable important reactions, however, their application has limitations, which can in many cases be overcome by using appropriate immobilization strategies. Here, a new support for immobilizing enzymes is proposed. This hybrid organic-inorganic support is composed of chitosan—a natural, nontoxic, biodegradable, and edible biopolymer—and sodium polyphosphate as the inorganic component. Lipase B from Candida antarctica (CALB) was immobilized on microspheres by encapsulation using these polymers. The characterization of the composites (by infrared spectroscopy, thermogravimetric analysis, and confocal Raman microscopy) confirmed the hybrid nature of the support, whose external part consisted of polyphosphate and core was composed of chitosan. The immobilized enzyme had the following advantages: possibility of enzyme reuse, easy biocatalyst recovery, increased resistance to variations in temperature (activity declined from 60 °C and the enzyme was inactivated at 80 °C), and increased catalytic activity in the transesterification reactions. The encapsulated enzymes were utilized as biocatalysts for transesterification reactions to produce the compound responsible for the aroma of jasmine.

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Design of a lipase-nano particle biocatalysts and its use in the kinetic resolution of medicament precursors

Cited by 83 publications

References 50 publications

Optimization of the Production of Enzymatic Biodiesel from Residual Babassu Oil (Orbignya sp.) via RSM

Optimization of the Production of Enzymatic Biodiesel from Residual Babassu Oil (Orbignya sp.) via RSM

Reactor Selection for Effective Continuous Biocatalytic Production of Pharmaceuticals

Synthesis of Benzyl Acetate Catalyzed by Lipase Immobilized in Nontoxic Chitosan-Polyphosphate Beads

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