Characterization and properties of catalase immobilized onto controlled pore glass and its application in batch and plug-flow type reactors

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

doi:10.1016/j.molcatb.2008.12.004

Cited by 48 publications

(25 citation statements)

References 51 publications

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“…Another commonly used strategy to covalently immobilize enzyme is using a bifunctional reagent glutaraldehyde. A Schiff base is formed between the carbonyl group of glutaraldehyde and the amino functional groups of the enzyme [29]. In this study, Immobead 150 support was modified with ethylenediamine and then activated with glutaraldehyde for the covalent immobilization of C. methylica FDH (Fig.…”

Section: Resultsmentioning

confidence: 99%

Highly stable and reusable immobilized formate dehydrogenases: Promising biocatalysts for in situ regeneration of NADH

Bi̇nay

Alagöz

Yıldırım

et al. 2016

Beilstein J. Org. Chem.

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SummaryThis study aimed to prepare robust immobilized formate dehydrogenase (FDH) preparations which can be used as effective biocatalysts along with functional oxidoreductases, in which in situ regeneration of NADH is required. For this purpose, Candida methylica FDH was covalently immobilized onto Immobead 150 support (FDHI150), Immobead 150 support modified with ethylenediamine and then activated with glutaraldehyde (FDHIGLU), and Immobead 150 support functionalized with aldehyde groups (FDHIALD). The highest immobilization yield and activity yield were obtained as 90% and 132%, respectively when Immobead 150 functionalized with aldehyde groups was used as support. The half-life times (t 1/2) of free FDH, FDHI150, FDHIGLU and FDHIALD were calculated as 10.6, 28.9, 22.4 and 38.5 h, respectively at 35 °C. FDHI150, FDHIGLU and FDHIALD retained 69, 38 and 51% of their initial activities, respectively after 10 reuses. The results show that the FDHI150, FDHIGLU and FDHIALD offer feasible potentials for in situ regeneration of NADH.

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Section: Resultsmentioning

confidence: 99%

Highly stable and reusable immobilized formate dehydrogenases: Promising biocatalysts for in situ regeneration of NADH

Bi̇nay

Alagöz

Yıldırım

et al. 2016

Beilstein J. Org. Chem.

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“…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

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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.

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“…16 It is usually prepared by using aluminum alkoxides 10,17 as the precursor in the most studies. Obviously, the cost is high due to the involvement of the expensive alkoxide precursor.…”

Section: Introductionmentioning

confidence: 99%

Sol–Gel Derived Boehmite as an Efficient and Robust Carrier for Enzyme Encapsulation

Zhu

Jiang

Zhang

et al. 2011

Ind. Eng. Chem. Res.

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Boehmite particles were prepared by a facile solÀgel method using sodium aluminate as the precursor under ambient conditions, and they were characterized by scanning electron microscopy (SEM), transmission electron microscopy (TEM), powder X-ray diffraction (XRD), nitrogen adsorption, etc. It is found that the boehmite particles consist of flat nanostrips, which are about 230 nm in length and 30 nm in width. The nanostrips are composed of nanoneedles of about 7 nm in diameter and 24 nm in length. The BrunauerÀEmmettÀTeller (BET) specific surface area, pore size, and pore volume of boehmite particles are 165 m 2 g À1 , 3.8 nm, and 0.11 cm 3 g À1 , respectively. Moreover, these boehmite particles are used as an efficient and robust carrier to encapsulate a model enzyme: bovine liver catalase. The catalase encapsulated in boehmite particles exhibits higher pH, thermal, and storage stabilities compared to its free counterpart. These results indicate that boehmite may become a competitive carrier for biological and technological applications.

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Characterization and properties of catalase immobilized onto controlled pore glass and its application in batch and plug-flow type reactors

Cited by 48 publications

References 51 publications

Highly stable and reusable immobilized formate dehydrogenases: Promising biocatalysts for in situ regeneration of NADH

Highly stable and reusable immobilized formate dehydrogenases: Promising biocatalysts for in situ regeneration of NADH

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

Sol–Gel Derived Boehmite as an Efficient and Robust Carrier for Enzyme Encapsulation

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