Immobilization of catalase onto Eupergit C and its characterization

2010 ◽  
Vol 64 (3-4) ◽  
pp. 177-183 ◽  
Author(s):  
Özlem Alptekin ◽  
S. Seyhan Tükel ◽  
Deniz Yıldırım ◽  
Dilek Alagöz
Keyword(s):  
Eupergit C

Immobilization of the recombinant xylanase B (XynB) from the hyperthermophilic Thermotoga maritima on metal-chelate Eupergit C 250L

2007 ◽  
Vol 41 (3) ◽  
pp. 278-285 ◽  
Author(s):  
Lite Li ◽  
Yunping Zhu ◽  
Zhigang Huang ◽  
Zhengqiang Jiang ◽  
Weiwei Chen
Keyword(s):  
Thermotoga Maritima ◽  
Metal Chelate ◽  
Eupergit C

Metal substitution in thermolysin: Catalytic properties of tungstate thermolysin in sulfoxidation with H2O2

2002 ◽  
Vol 80 (6) ◽  
pp. 622-625 ◽  
Author(s):  
Martin Bakker ◽  
Fred van Rantwijk ◽  
Roger A Sheldon
Keyword(s):  
Hydrogen Peroxide ◽  
Proteolytic Activity ◽  
Active Site ◽  
Catalytic Properties ◽  
Metal Substitution ◽  
Eupergit C ◽  
Partial Restoration ◽  
Covalently Bound

The catalytic Zn2+ ion was extracted from thermolysin, which had been covalently bound to Eupergit C. The apo-enzyme incorporated the oxometallate anions MoO42–, SeO42–, and WO42– with partial restoration of the proteolytic activity. Tungstate thermolysin was moderately active in the sulfoxidation of thioanisole by hydrogen peroxide, whereas its activity towards phenylmercaptoacetophenone, which was designed to bind well in the active site of thermolysin, was much higher.

scholarly journals Immobilization of His-tagged recombinant xylanase fromPenicillium occitanison Nickel-chelate Eupergit C for increasing digestibility of poultry feed

Bioengineered ◽  
2014 ◽  
Vol 5 (4) ◽  
pp. 274-279 ◽  
Author(s):  
Dorra Driss ◽  
Zied Driss ◽  
Fatma Chaari ◽  
Semia Ellouz Chaabouni
Keyword(s):  
Poultry Feed ◽  
Eupergit C ◽  
Nickel Chelate

scholarly journals Modification of β-galactosidase for use in organic mono-phase hexanol system

2009 ◽  
Vol 28 (1) ◽  
pp. 91 ◽  
Author(s):  
Daniela Nikolovska-Nedelkoska ◽  
Irina Mladenoska ◽  
Filimena Poposka ◽  
Eleonora Winkelhausen ◽  
Slobodanka Kuzmanova
Keyword(s):  
Enzyme Activity ◽  
Water Activity ◽  
Sodium Dodecyl ◽  
Reaction Medium ◽  
Fold Increase ◽  
Total Activity ◽  
Phase System ◽  
Eupergit C ◽  
Total Enzyme Activity ◽  
Micro Emulsion

Different methods for preparation of the Aspergillus oryzae β-galactosidase were evaluated and the total enzyme activity was determined in hexanol mono-phase system using p-nitrophenyl-β-D-galactoside as a substrate. Several supports such as Acurell EP-100, Amberlite IRC (50), Celite, Dowex, Eupergit C and silica gel were tested in order to select the most suitable matrix for immobilization of the β-galactosidase for performing transgalactosylation reactions in hexanol. Celite and Amberlite IRC (50) were selected as the most appropriate carriers. Albumin, PEG 6000, starch and glycine, added prior to the immobilization procedure, acted as stabilizers of the galactosidase. By adding albumin on Celite, a 3.3-fold increase of enzyme activity was achieved. Sodium dodecyl sulphate (SDS), dioctyl sulfosuccinate (AOT), Tween 65 and crown ether were used directly in the reaction medium in order to increase its homogeneity. Addition of SDS to the medium resulted in a 3.65-fold increased activity of the β- galactosidase deposited on Celite. A micro-emulsion system created by addition of AOT resulted in an increased catalytic activity. The β-galactosidase showed enhanced total activity with increased water activity in the system having the highest value for the water activity close to the saturation level (0.92).

Immobilization on Eupergit C of cyclodextrin glucosyltransferase (CGTase) and properties of the immobilized biocatalyst

2003 ◽  
Vol 21 (4-6) ◽  
pp. 299-308 ◽  
Author(s):  
M.Teresa Martı́n ◽  
Francisco J Plou ◽  
Miguel Alcalde ◽  
Antonio Ballesteros
Keyword(s):  
Eupergit C ◽  
Immobilized Biocatalyst
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