Stability and catalytic properties of chloroperoxidase immobilized on SBA-16 mesoporous materials

Aburto, Jorge; Ayala, Marcela; Bustos‐Jaimes, Ismael; Montiel, Carmina; Terrés, E.; Domínguez, José Manuel; Torres, Eduardo

doi:10.1016/j.micromeso.2005.04.008

Cited by 100 publications

(75 citation statements)

References 32 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…The free enzyme achieved 0.13% conversion of ketorolac, while the immobilized enzyme degraded 4% of the ketorolac. It is known that immobilization with chitosan and other materials, such as silica derivatives, can improve the activity or stability of peroxidases by providing a protective microenvironment against fluctuations in pH [53,54]. The improvement in the stabilization or activity of enzymes by immobilization is often the result of a combination of physicochemical factors, such as enzyme rigidification, enzyme distortion, pH gradients, substrate or product gradients, partitioning (towards or away from the enzyme environment, for the substrate or the products), or the blocking of some enzyme areas (e.g., reduced inhibition), which may greatly improve enzyme performance [55].…”

Section: Application Of the Enzymatic Treatment In Simulated Treated mentioning

confidence: 99%

Chloroperoxidase-Mediated Halogenation of Selected Pharmaceutical Micropollutants

et al. 2018

Self Cite

View full text Add to dashboard Cite

Abstract:The oxidation of eight pharmaceutical micropollutants by chloroperoxidase derived from Caldaromyces fumago using hydrogen peroxide as an electron acceptor is reported. All the tested compounds, namely trazadone, sulfamethoxazole, naproxen, tetracycline, estradiol, ketoconazole, ketorolac, and diclofenac, were found to be substrates for oxidation by chloroperoxidase. The respective oxidation products were identified by electrospray ionization-mass spectrometry. All the products contain at least one chloride atom in their structure after the enzymatic oxidation. Degradability experiments indicated that most of the reaction products are more biodegradable than the corresponding unmodified compounds. The enzyme was found to be catalytically active in effluent from a water treatment facility, transforming the micropollutants with high reaction rates and conversions. The enzyme was immobilized in chitosan macrospheres, which allowed the catalyst to be recycled for up to three treatment cycles in simulated samples of treated residual water. The conversion was high in the first two cycles; however, in the third, a 50% reduction in the capacity of the enzyme to oxidize ketorolac was observed. Additionally, immobilization improved the performance of the enzyme over a wider pH range, achieving the conversion of ketorolac at pH 5, while the free enzyme was not active at this pH. Overall, the results of this study suggest that chloroperoxidase represents a powerful potential catalyst in terms of its catalytic activity for the transformation of pharmaceutical micropollutants.

show abstract

Section: Application Of the Enzymatic Treatment In Simulated Treated mentioning

confidence: 99%

Chloroperoxidase-Mediated Halogenation of Selected Pharmaceutical Micropollutants

et al. 2018

Self Cite

View full text Add to dashboard Cite

show abstract

“…Heteroatom oxidation (N -and S -oxidation) has also been achieved; therefore, oxidation of heterocyclic sulfur compounds present in fuels and the modification of petroporphyrins and asphaltene molecules are two promising large-scale applications for e.g. petroleum industry, in order to improve the quality of petroleum and petroleum fuels, as well as for reducing their environmental polluting effects [288]. Studies on this enzyme were also extended to understand DET [215], immobilized on mesoporous materials [288], ionic liquid-modified carbon electrodes [215] and with conductive polymers [289].…”

Section: Novel Enzymes and Their Applicationsmentioning

confidence: 99%

“…petroleum industry, in order to improve the quality of petroleum and petroleum fuels, as well as for reducing their environmental polluting effects [288]. Studies on this enzyme were also extended to understand DET [215], immobilized on mesoporous materials [288], ionic liquid-modified carbon electrodes [215] and with conductive polymers [289]. Moreover, this enzyme can also be applied at anodes for electrochemical heteroatom oxidation (N -and S -oxidation) with simultaneous cathodic reduction of O 2 and H 2 O 2 [215,289].…”

Section: Novel Enzymes and Their Applicationsmentioning

confidence: 99%

Enzymatic Electrosynthesis: An Overview on the Progress in Enzyme- Electrodes for the Production of Electricity, Fuels and Chemicals

Satyawali¹

2013

J Microbial Biochem Technol

View full text Add to dashboard Cite

Recent interest in the field of biocommodities production through bioelectrochemical systems has generated interest in the enzyme catalyzed redox reactions. Enzyme catalyzed electrodes are well established as sensors and power generators. However, a paradigm shift in recent science towards the production of useful chemicals has changed the face of biofuel cells, keeping the fuels or chemicals production in the upfront. This review article comprehensively presents the progress in the field of enzyme-electrodes for the production of electricity, fuels and chemicals with an aim to represent a practical outline for understanding the use of single or multiple redox enzymes as electrocatalysts for their electron transfer onto electrodes. It also provides the state-of-the-art information regarding the different existing processes to fabricate enzyme electrodes. Successfully-achieved electroenzymatic anodic and cathodic reactions are further discussed, together with their potential applications. Particular focus was made on the novel single/multiple enzyme systems towards product synthesis and other applications. Finally, techno-economic and environmental elements for industrial processing with enzyme catalyzed bioelectrochemical system (e-BES) are anticipated, in order to provide useful strategies for further development of this technology.

show abstract

“…Immobilized enzymes can display activities superior to that of the free enzyme [1][2][3][4] while remaining stable and exhibiting significant catalytic activity in harsh media such as non-aqueous solvents 5,6 . However, more often than not immobilized enzymes display activities significantly less than free enzyme 7 . Mesoporous silicates (MPS) have been extensively studied as supports for enzymes 8 .…”

mentioning

confidence: 99%

Tailored adsorption of His₆-tagged protein onto nickel(ii)–cyclam grafted mesoporous silica

et al. 2010

View full text Add to dashboard Cite

show abstract

Stability and catalytic properties of chloroperoxidase immobilized on SBA-16 mesoporous materials

Cited by 100 publications

References 32 publications

Chloroperoxidase-Mediated Halogenation of Selected Pharmaceutical Micropollutants

Chloroperoxidase-Mediated Halogenation of Selected Pharmaceutical Micropollutants

Enzymatic Electrosynthesis: An Overview on the Progress in Enzyme- Electrodes for the Production of Electricity, Fuels and Chemicals

Tailored adsorption of His₆-tagged protein onto nickel(ii)–cyclam grafted mesoporous silica

Contact Info

Product

Resources

About

Stability and catalytic properties of chloroperoxidase immobilized on SBA-16 mesoporous materials

Cited by 100 publications

References 32 publications

Chloroperoxidase-Mediated Halogenation of Selected Pharmaceutical Micropollutants

Chloroperoxidase-Mediated Halogenation of Selected Pharmaceutical Micropollutants

Enzymatic Electrosynthesis: An Overview on the Progress in Enzyme- Electrodes for the Production of Electricity, Fuels and Chemicals

Tailored adsorption of His6-tagged protein onto nickel(ii)–cyclam grafted mesoporous silica

Contact Info

Product

Resources

About

Tailored adsorption of His₆-tagged protein onto nickel(ii)–cyclam grafted mesoporous silica