Immobilization of catalase onto Eupergit C and its characterization

Alptekin, Özlem; Tükel, S. Seyhan; Yıldırım, Deniz; Alagöz, Dilek

doi:10.1016/j.molcatb.2009.09.010

Cited by 83 publications

(52 citation statements)

References 48 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The efficiency of the immobilised laccase (2.75 ± 0.05 l/lmol min), based on the ratio between the turnover number and the Michaelis constant (k cat /K M ), was approximately twice as low as that of the free enzyme (6.01 ± 0.40 l/lmol min). Lower efficiencies for immobilised laccase and catalase from Lentinus edodes on Eupergit C were also reported by D'Annibale et al (2000) and Alptekin et al (2010), respectively. Several authors have suggested that this effect could be related to diffusion substrate limitations, substrate partitioning, lower accessibility of the substrate to the active site, protein conformational changes, internal mass transport constraint and/or substrate/product adsorption onto the carrier surface (Davis and Burns 1992;Hernaiz and Crout 2000;Rekuc et al 2010;Yamak et al 2009).…”

Section: Determination Of Apparent Kinetic Parameterssupporting

confidence: 72%

“…For example, free laccase was completely inactivated after 1 h of incubation at pH 2, and retained only 15% of initial activity at pH 4. However, the residual activity of immobilised laccase after 1 h amounted to 70 and 80% at pH 2 and 4, respectively, and 10 and 30% of the initial activity after 24 h. Alptekin et al (2010) reported that the multiplecovalent bonding of laccase to the resin resulting in more rigid enzyme less prone to pH-induced a The amount of immobilised protein was calculated from the difference between the protein in the control and protein remaining in the supernatant of immobilised assay b Assay conditions: 5 mM ABTS, 0.1 M sodium acetate buffer, pH 5, 20 mg/ml biocatalyst, in a final volume of 3 ml. Measured with immobilised biocatalyst over 10 min period c Activity recovered was calculated as the ratio of measured activity to theoretic bound activity (difference between the laccase activity in the controls and the remaining in the supernatant of immobilised assay) conformational changes, that could cause higher pHstability.…”

Section: Optimum Ph and Ph Stabilitymentioning

confidence: 90%

“…In previous research, covalently immobilised laccase from Myceliophthora thermophila on Sepabeads EC-EP3 carriers retained 96% of its initial activity after storage at 4°C for 4 months (Kunamneni et al 2008). Alptekin et al (2010) reported residual activities of immobilised catalase on Eupergit C of 68 and 79% after storage for 28 days at 5°C and room temperature, respectively.…”

Section: Storage Stabilitymentioning

confidence: 99%

See 2 more Smart Citations

Immobilisation of laccase on Eupergit supports and its application for the removal of endocrine disrupting chemicals in a packed-bed reactor

et al. 2011

View full text Add to dashboard Cite

Laccase from Myceliophthora thermophila was covalently immobilised on Eupergit C and Eupergit C 250L yielding specific activities of up to 17 and 80 U/g, respectively. Due to its superior activity, Eupergit C 250L was chosen for further research. The somewhat lower catalytic efficiency (based on the ratio between the turnover number and the Michaelis constant, k cat /K M ) of the immobilised enzyme in comparison with that of the free enzyme was balanced by its increased stability and broader operational window related to temperature and pH. The feasibility of the immobilised laccase was tested by using a packed bed reactor (PBR) operating in consecutive cycles for the removal of Acid Green 27 dye as model substrate. High degrees of elimination were achieved (88, 79, 69 and 57% in 4 consecutive cycles), while the levels of adsorption on the support varied from 18 to 6%, proving that dye removal took place mainly due to the action of the enzyme. Finally, a continuous PBR with the solid biocatalyst was applied for the treatment of a solution containing the following endocrine disrupting chemicals: estrone (E1), 17b-estradiol (E2) and 17a-ethinylestradiol (EE2). At steady-state operation, E1 was degraded by 65% and E2 and EE2 were removed up to 80% and only limited adsorption of these compounds on the support, between 12 and 22%, was detected. In addition, a 79% decrease in estrogenic activity was detected in the effluent of the enzymatic reactor while only 14% was attained by inactivated laccase.

show abstract

Section: Determination Of Apparent Kinetic Parameterssupporting

confidence: 72%

Section: Optimum Ph and Ph Stabilitymentioning

confidence: 90%

Section: Storage Stabilitymentioning

confidence: 99%

See 1 more Smart Citation

Immobilisation of laccase on Eupergit supports and its application for the removal of endocrine disrupting chemicals in a packed-bed reactor

et al. 2011

View full text Add to dashboard Cite

show abstract

“…Previously, the optimum immobilization time and temperature for catalase were reported as 24 h and 5 1C [33][34]. Based on these results, in this study, the SOD and CAT enzyme immobilizations were carried out at 4 1C and physiological pH of 7.4 within 24 h by varying the initial enzyme and PEI concentrations.…”

Section: Optimization Conditions For Sod/cat Immobilizationmentioning

confidence: 95%

Immobilization of superoxide dismutase/catalase onto polysulfone membranes to suppress hemodialysis-induced oxidative stress: A comparison of two immobilization methods

Mahlicli

Şen

Mutlu

et al. 2015

Journal of Membrane Science

View full text Add to dashboard Cite

a b s t r a c tThe objective of this study is to improve the blood compatibility of polysulfone (PSF) based hemodialysis membranes through generating antioxidative surfaces with superoxide dismutase (SOD)/catalase (CAT) enzyme couple immobilization. Enzymes were attached both covalently and ionically on the plasma treated and polyethyleneimine (PEI) deposited membranes, respectively. The loss of enzymes from PEI modified surface at the end of 4 h was found to be relatively higher during storage in phosphate buffered saline (PBS) at pH 7.4 when compared to the enzymes on the plasma treated surface. The kinetic studies indicated that SOD catalyzed the reaction in the diffusion-limited regime at all substrate concentrations and its inactivation by hydrogen peroxide was prevented in the presence of CAT. SOD/CAT coated PSF membranes were capable of reducing the levels of reactive oxygen species in blood and can significantly prolong activated partial thromboplastin time. In addition, both the adsorption of human plasma proteins and platelet activation on all modified membranes decreased significantly compared to the unmodified PSF membranes. Proposed modification methods did not affect high permeability, high mechanical strength or the non-toxic properties of the PSF membranes.

show abstract

“…In the second step, a covalent reaction occurs between the adsorbed enzyme and neighboring epoxide groups. 9 The support epoxy groups can react with the amino, sulfhydryl, and hydroxyl groups of the enzyme, forming extremely stable O-C and N-C bonds. 10 Immobilized enzymes can be recovered after a batch, guaranteeing their reutilization in further batches and significantly reducing their costs.…”

Section: Eupergitmentioning

confidence: 99%

A NEW APPROACH TO EVALUATE IMMOBILIZATION OF β-GALACTOSIDASE ON EUPERGIT^®C: STRUCTURAL, KINETIC, AND THERMAL CHARACTERIZATION

Braga¹,

Silva²,

Oliveira³

et al. 2014

Química Nova

View full text Add to dashboard Cite

This study aimed to evaluate β-galactosidase immobilization. For this purpose, the ionic strength of the buffer, reaction time, amount of the immobilization support, and pH were evaluated by a central composite design. Assay 8, which consisted of 1.5 mol L −1 phosphate buffer (pH 7.5) and a reaction time of 2 h, produced the maximum yield. Eupergit ® C (400 mg) was subsequently used as an immobilization support. Immobilization kinetics wereinvestigated, and a significant increase in the yield was obtained after immobilization compared with that obtained from assay 8 (22.0 U mL −1 vs. 15.6 U mL −1). The enzyme efficiency of actuation was evaluated using o-nitrophenyl-β-d-galactopyranoside and lactose, with lactose providing better results. The reuse of β-galactosidase was evaluated, and more than 50% of the initial enzyme activity was maintained after five cycles of use. Enzyme characterization revealed that immobilization improved some aspects of the thermostability of β-galactosidase.

show abstract

Immobilization of catalase onto Eupergit C and its characterization

Cited by 83 publications

References 48 publications

Immobilisation of laccase on Eupergit supports and its application for the removal of endocrine disrupting chemicals in a packed-bed reactor

Immobilisation of laccase on Eupergit supports and its application for the removal of endocrine disrupting chemicals in a packed-bed reactor

Immobilization of superoxide dismutase/catalase onto polysulfone membranes to suppress hemodialysis-induced oxidative stress: A comparison of two immobilization methods

A NEW APPROACH TO EVALUATE IMMOBILIZATION OF β-GALACTOSIDASE ON EUPERGIT^®C: STRUCTURAL, KINETIC, AND THERMAL CHARACTERIZATION

Contact Info

Product

Resources

About

Immobilization of catalase onto Eupergit C and its characterization

Cited by 83 publications

References 48 publications

Immobilisation of laccase on Eupergit supports and its application for the removal of endocrine disrupting chemicals in a packed-bed reactor

Immobilisation of laccase on Eupergit supports and its application for the removal of endocrine disrupting chemicals in a packed-bed reactor

Immobilization of superoxide dismutase/catalase onto polysulfone membranes to suppress hemodialysis-induced oxidative stress: A comparison of two immobilization methods

A NEW APPROACH TO EVALUATE IMMOBILIZATION OF β-GALACTOSIDASE ON EUPERGIT®C: STRUCTURAL, KINETIC, AND THERMAL CHARACTERIZATION

Contact Info

Product

Resources

About

A NEW APPROACH TO EVALUATE IMMOBILIZATION OF β-GALACTOSIDASE ON EUPERGIT^®C: STRUCTURAL, KINETIC, AND THERMAL CHARACTERIZATION