Immobilization of fungal peroxidase on alkylaminated organic and inorganic porous supports

L̷obarzewski, J.; Kolarz, Bożena N.; Wójcik, Anna; Wojaczyńska, Maria; Trochimczuk, Andrzej W.; Błaszczynska, T.

doi:10.1002/abio.370080108

Cited by 11 publications

(1 citation statement)

References 15 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Controlled-porous glass (CPG, mesh: 200-250, POCH Gliwice, Poland) and silica-gel (S-Gel, mesh: 200-500, POCH, Gliwice, Poland) were activated using ?-aminopropyltriethoxysilane (APTES) after the method of Lappi [20]. The supports III and IV were prepared according to the method described by Lobarzewski et al [28]. Further activation of CPG was performed using sugars solutions treated with K104, according to the method described by Zaborsky [21 ].…”

Section: Affinity Chromatographymentioning

confidence: 99%

The optimization of the liquid affinity chromatography conditions of the extracellular invertase isolation from theCandida utilis cultures

et al. 2000

View full text Add to dashboard Cite

SummaryThe Candida utilis yeast strain was used as a source for the extracellular invertase (E.C.3.2.1.26). The conditions for the highest extracellular invertase activity production were established using three liquid media. The enzyme was purified using one-step affinity chromatography method in the optimized conditions. Three saccharides: sucrose, maltose and inulin were comparatively used as ligands in the affinity technique. The partially purified invertase was afterwards immobilized on the newly described solid matrix with keratin as an activator.

show abstract

Section: Affinity Chromatographymentioning

confidence: 99%

The optimization of the liquid affinity chromatography conditions of the extracellular invertase isolation from theCandida utilis cultures

et al. 2000

View full text Add to dashboard Cite

show abstract

Acrylic carriers for the immobilization of enzymes

Kolarz

L̷obarzewski

Trochimczuk

et al. 1989

Angew. Makromol. Chem.

View full text Add to dashboard Cite

The influence of the supermolecular structure of carriers obtained by aminolysis of nitrile or ester groups of acrylic copolymers crosslinked with divinylbenzene or ethylene dimethacrylate was investigated. The enzymes peroxidase, glucoamylase and urease immobilized on the carriers of a porous structure display a higher activity as compared to carriers with an expanded structure. The number of functional groups in the carrier influences the activity of the immobilized enzyme, but there is no linear relationship.

show abstract

Urease immobilized on aminated butyl acrylate‐ethylenedimethacrylate copolymer

Krajewska

Leszko

Zaborska

1990

Angew. Makromol. Chem.

View full text Add to dashboard Cite

Urease was covalently immobilized on a new acrylic enzyme carrier: aminated butyl acrylate-ethylenedimethacrylate copolymer. The enzyme retained 56% of its original activity. The properties of the free and immobilized urease were determined and compared. The Michaelis constant was found to be higher for the immobilized urease than for the free one, while maximum reaction rate was lower for the immobilized enzyme. The stability of urease against change in pH was considerably improved by the immobilization. The immobilized urease showed very good storage stability and reusability. Resistance of the enzyme against heat inactivation at 70 "C, however, was not found to be improved. ZUSAMMENFASSUNG:Urease wurde auf einem aminierten Butylacrylat-Ethylendimethacrylat-Copolymeren als neuem Enzymtrager kovalent gebunden. Hierbei behalt das Enzym 56% seiner ursprunglichen Aktivitat. Die Eigenschaften der freien und der gebundene Urease wurden bestimmt und miteinander verglichen: Die Michaeliskonstante der immobilisierten Urease ist grofler als die des freien Enzyms. Dagegen ist die maximale Reaktionsgeschwindigkeit des gebundenen Enzyms etwas niedriger als die des freien Enzyms. Die StabilitLt der Urease gegenuber pH-Wertanderungen wurde durch die Immobilisierung betrachtlich erhoht. Die immobilisierte Urease zeigt eine sehr gute Lagerungsstabilitat und Wiederverwendungsfahigkeit. Dagegen wurde durch die Immobilisierung keine Verbesserung der Enzymwiderstandsfahigkeit gegenuber Hitzeinaktivierung (bei 70 "C) erreicht.

show abstract

Immobilization of fungal peroxidase on alkylaminated organic and inorganic porous supports

Cited by 11 publications

References 15 publications

The optimization of the liquid affinity chromatography conditions of the extracellular invertase isolation from theCandida utilis cultures

The optimization of the liquid affinity chromatography conditions of the extracellular invertase isolation from theCandida utilis cultures

Acrylic carriers for the immobilization of enzymes

Urease immobilized on aminated butyl acrylate‐ethylenedimethacrylate copolymer

Contact Info

Product

Resources

About