Carboligation reactivity of benzaldehyde lyase (BAL, EC 4.1.2.38) covalently attached to magnetic nanoparticles

Tural, Bilsen; Şimşek, İlke; Tural, Servet; Çelebi, Bülent; Demir, Ayhan S.

doi:10.1016/j.tetasy.2013.01.022

Cited by 15 publications

(11 citation statements)

References 48 publications

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“…Also transketolase, another ThDP‐dependent enzyme, inactivates during reaction progress in the presence of the substrate . Fortunately, the biocatalyst stability can be improved by enzyme engineering and reaction engineering . As an example, continuous membrane reactors maintain substrate concentration at low level and thereby, circumvent substrate dependent inactivation …”

Section: Introductionmentioning

confidence: 99%

“…7 Fortunately, the biocatalyst stability can be improved by enzyme engineering [8][9][10] and reaction engineering. [11][12][13][14][15] As an example, continuous membrane reactors maintain substrate concentration at low level and thereby, circumvent substrate dependent inactivation. 7,[16][17][18] There are many mathematical models available that describe different types of inactivation, for example first order or reversible inactivation, 19 thermal inactivation, 20 also combined with temperature-dependent activation, 21 pHdependent inactivation, 22 and inactivation during high-pressure processes, for example, fractional conversion models, multiphasic models, or the Weibull model.…”

Section: Introductionmentioning

confidence: 99%

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Simultaneous identification of reaction and inactivation kinetics of an enzyme‐catalyzed carboligation

Ohs

Leipnitz

Schöpping

et al. 2018

Biotechnology Progress

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Thiamine diphosphate (ThDP)-dependent enzymes catalyze a broad range of reactions with excellent enantioselectivity. Among these reactions, carboligations of aldehydes are of particular interest since the products, chiral hydroxy ketones, are valuable building blocks in the pharmaceutical industry. However, the substrates, for example, benzaldehyde, inactivate the biocatalysts, for example the ThDP-dependent benzaldehyde lyase from Pseudomonas fluorescens (PfBAL). Because only few mechanistic kinetic models for carboligation and simultaneous inactivation are available today, we quantitatively determined the reaction kinetics and inactivation of the self-carboligation of benzaldehyde yielding the product (R)-benzoin catalyzed by PfBAL directly from progress curves using model-based experimental analysis. Discrimination of several inactivation models identified the substrate-dependent inactivation by benzaldehyde to be significant. Sensitivity analysis and optimal experimental design improved parameter precision significantly, to between 4 and 26% relative standard deviation while maintaining the necessary number of 13 experiments moderate. The developed mechanistic kinetic model will enable to perform a model-based process optimization to circumvent the substrate-dependent enzyme inactivation. © 2018 American Institute of Chemical Engineers Biotechnol. Prog., 2018 © 2018 American Institute of Chemical Engineers Biotechnol. Prog., 34:1081-1092, 2018.

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Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Simultaneous identification of reaction and inactivation kinetics of an enzyme‐catalyzed carboligation

Ohs

Leipnitz

Schöpping

et al. 2018

Biotechnology Progress

View full text Add to dashboard Cite

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“…A). The decrease in the saturation magnetization of nanoparticles after coating can be explained by the diamagnetic contribution of silica and BAF shell . As can be seen from the inset in Fig.…”

Section: Resultsmentioning

confidence: 75%

“…Synthesis of silica‐coated Fe 3 O 4 (magnetite) nanoparticles (SCMPs) was previously reported by our group . We utilized a two‐step post graft method in order to synthesize the boronic acid functionalized magnetic nanoparticles .…”

Section: Methodsmentioning

confidence: 99%

Kinetic approach for the purification of nucleotides with magnetic separation

Tural

Ece

et al. 2014

J. Sep. Science

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The isolation of β-nicotinamide adenine dinucleotide is of great importance since it is widely used in different scientific and technologic fields such as biofuel cells, sensor technology, and hydrogen production. In order to isolate β-nicotinamide adenine dinucleotide, first 3-aminophenyboronic acid functionalized magnetic nanoparticles were prepared to serve as a magnetic solid support and subsequently they were used for reversible adsorption/desorption of β-nicotinamide adenine dinucleotide in a batch fashion. The loading capacity of the 3-aminophenyboronic acid functionalized nanoparticles for β-nicotinamide adenine dinucleotide adsorption was 13.0 μmol/g. Adsorption kinetic and isotherm studies showed that the adsorption process followed a pseudo-second-order kinetic model and the experimental data can be represented using Langmuir isotherm model. The 3-aminophenyboronic acid functionalized magnetic nanoparticles were proposed as an alternative support for the β-nicotinamide adenine dinucleotide purification. The results elucidated the significance of magnetic separation as a fast, relatively simple, and low-cost technique. Furthermore, the magnetic supports can be reused at least five times for purification processes.

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“…Similar observations were also reported previously by Bezbradica and his colleagues [14] who showed that epoxy-activated Purolite could be well used as carrier to immobilize lipase, and a high protein loading capacity and high lipase activity were obtained. Besides, Tural's group [13,29,30] also demonstrated that decarboxylase from Pseudomonas putida and benzaldehyde lyase immobilized on epoxy-activated magnetic support exhibited a high enzyme activity recovery.…”

Section: Effect Of Epoxy Density On Lipase Immobilizationmentioning

confidence: 98%

Lipase immobilization on epoxy-activated poly(vinyl acetate-acrylamide) microspheres

Zhang

Peng

Wang

et al. 2015

Colloids and Surfaces B: Biointerfaces

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Carboligation reactivity of benzaldehyde lyase (BAL, EC 4.1.2.38) covalently attached to magnetic nanoparticles

Cited by 15 publications

References 48 publications

Simultaneous identification of reaction and inactivation kinetics of an enzyme‐catalyzed carboligation

Simultaneous identification of reaction and inactivation kinetics of an enzyme‐catalyzed carboligation

Kinetic approach for the purification of nucleotides with magnetic separation

Lipase immobilization on epoxy-activated poly(vinyl acetate-acrylamide) microspheres

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