Erythromycin degradation by esterase (EreB) in enzymatic membrane reactors

Cazes, Matthias de; Belleville, Marie‐Pierre; Petit, Eddy; Salomo, M.; Bayer, Sally; Czaja, Rico; Gunzburg, Jean de; Sánchez-Marcano, José

doi:10.1016/j.bej.2016.06.029

Cited by 33 publications

(13 citation statements)

References 40 publications

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“…In addition to the hydrolysis and synthesis of fat, esterases can also catalyze the hydrolysis of some antibiotics with ester bonds . Three different EMRs were designed to degrade erythromycin using esterase EreB . In the first model, esterase was present in the free form in an EMR system.…”

Section: The Applications Of Reimsmentioning

confidence: 99%

Immobilization of Enzymes in/on Membranes and their Applications

et al. 2019

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Enzyme membrane reactors (EMRs) are becoming increasingly interesting for application in bioconversion processes in food processing, pharmaceutics, biorefinery and wastewater treatment. Integrating the highly efficient enzymatic reaction with selectable membrane separation technology, the EMRs are able to reduce product inhibition, improve the stability of the enzyme, increase the number of reaction cycles and sustainably separate products from biotransformation solutions. Generally, in EMRs, enzymes can be either free in the solution, immobilized on an additional carrier or immobilized directly in/on a porous structure of the membrane, of which the system with the enzyme immobilized directly in/on the membrane (EIM) is a relatively simple and most widely applied method. The EIM system not only facilitates recycling of the enzymes but also in many cases additionally enhances enzyme properties such as the stability and viability. A membrane with a porous structure is usually considered as a potential carrier for enzyme immobilization. A series of immobilization methods has been developed to fix the enzymes on the membranes. The purpose of this review is to systemically summarize the immobilization methods of enzymes in/on membranes and the applications of the EIM system for biocatalysis.

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Section: The Applications Of Reimsmentioning

confidence: 99%

Immobilization of Enzymes in/on Membranes and their Applications

et al. 2019

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“…Indeed, it is also possible a competition for the oxidative process between the pharmaceuticals and oxidation products formed. De Cazes [55,56] has already noticed his effect for the degradation of tetracycline and erythromycin with immobilized enzymes. The authors observed a decrease of the degradation yield with time up to stabilization of antibiotics concentration after 24h of reaction.…”

Section: Effect Of Syringaldehyde Additionmentioning

confidence: 99%

Effect of redox mediators in pharmaceuticals degradation by laccase: A comparative study

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Belleville

Alanis

et al. 2019

Process Biochemistry

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“…Membranes containing immobilized enzymes have been intensively used in wastewater treatment processes, such as the selective removal of pesticides from vegetative water [24,25]; the removal of dyes [12,26]; the degradation of bisphenol A [2,27]; the degradation of antibiotics [22,28]; and the catalytic production of valuable chemicals, such as oligodextran production [29], the production of peptides from milk protein [30], the production of oligosaccharides [31,32], and the conversion of carbon dioxide into methanol [21]. De Cazes et al [22] immobilized laccase on ceramic membranes by coating the ceramic support with a gelatin layer, followed by the GA activation and the subsequent enzyme attachment.…”

Section: Introductionmentioning

confidence: 99%

“…Under the optimal conditions, e.g., pH at 4 and temperature at 45 • C, the immobilized esterase displayed after 100 h a degradation rate of 15.8 mg h −1 . It was stated that the immobilized enzyme showed better stability in comparison to the free enzyme [28]. Zhang et al [26] immobilized laccase on porous zeolite-like geopolymer membranes for the removal of crystal violet (CV) from wastewater.…”

Section: Introductionmentioning

confidence: 99%

Bioconjugation Strategy for Ceramic Membranes Decorated with Candida Antarctica Lipase B—Impact of Immobilization Process on Material Features

et al. 2022

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A strategy for the bioconjugation of the enzyme Candida antarctica lipase B onto titania ceramic membranes with varied pore sizes (15, 50, 150, and 300 kDa) was successfully performed. The relationship between the membrane morphology, i.e.,the pore size of the ceramic support, and bioconjugation performance was considered. Owing to the dimension of the enzyme (~33 kDa), the morphology of the ceramics allowed (50, 150, and 300 kDa) or did not allow (15 kDa) the entrance of the enzyme molecules into the porous structure. Such a strategy made it possible to better understand the changes in the material (morphology) and physicochemical features (wettability, adhesiveness, and surface charge) of the samples, which were systematically examined. The silane functionalization and enzyme immobilization were accomplished via the covalent route. The samples were characterized after each stage of the modification, which was very informative from the material point of view. As a consequence of the modification, significant changes in the contact angle, roughness, adhesion, and zeta potential were observed. For instance, for the 50 kDa membrane, the contact angle increased from 29.1 ± 1.5° for the pristine sample to 72.3 ± 1.5° after silane attachment; subsequently, it was reduced to 57.2 ± 1.5° after the enzyme immobilization. Finally, the contact angle of the bioconjugated membrane used in the enzymatic process rose to 92.9 ± 1.5°. By roughness (Sq) controlling, the following amendments were noticed: for the pristine 50 kDa membrane, Sq = 1.87 ± 0.21 µm; after silanization, Sq = 2.33 ± 0.30 µm; after enzyme immobilization, Sq = 2.74 ± 0.26 µm; and eventually, after the enzymatic process, Sq = 2.37 ± 0.27 µm. The adhesion work of the 50 kDa samples was equal to 136.41 ± 2.20 mN m−1 (pristine membrane), 94.93 ± 2.00 mN m−1 (with silane), 112.24 ± 1.90 mN m−1 (with silane and enzyme), and finally, 69.12 ± 1.40 mN m−1 (after the enzymatic process). The materials and physicochemical features changed substantially, particularly after the application of the membrane in the enzymatic process. Moreover, the impact of ceramic material morphology on the zeta potential value is here presented for the first time. With an increase in the ceramic support cut-off, the amount of immobilized lipase rose, but the specific productivity was higher for membranes possessing smaller pores, owing to the higher grafting density. For the enzymatic process, two modes of accomplishment were selected, i.e., stirred-tank and cross-flow. The latter method was characterized by a much higher effectiveness, with a resulting productivity equal to 99.7 and 60.3 µmol h−1 for the 300 and 15 kD membranes, respectively.

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Erythromycin degradation by esterase (EreB) in enzymatic membrane reactors

Cited by 33 publications

References 40 publications

Immobilization of Enzymes in/on Membranes and their Applications

Immobilization of Enzymes in/on Membranes and their Applications

Effect of redox mediators in pharmaceuticals degradation by laccase: A comparative study

Bioconjugation Strategy for Ceramic Membranes Decorated with Candida Antarctica Lipase B—Impact of Immobilization Process on Material Features

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