Cyclohexyl Methacrylate with Tetra (Ethylene Glycol) Dimethacrylate in Tertahydrofuran Radical Copolymerization

2009 ◽  
Vol 609 ◽  
pp. 63-67 ◽  
Author(s):  
Asmahane Fasla ◽  
Seghier Ould Kada ◽  
Zoubida Seghier ◽  
Alain Périchaud
Keyword(s):  
Ethylene Glycol ◽  
Specific Activity ◽  
13C Nmr Spectroscopy ◽  
Radical Copolymerization ◽  
Ethylene Glycol Dimethacrylate ◽  
Random Copolymers ◽  
Glycol Dimethacrylate ◽  
Free Radical Copolymerization ◽  
Tetrahydrofuran Solution ◽  
Cyclohexyl Methacrylate

Free-radical copolymerization of cyclohexyl methacrylate (CHMA) and tetra (ethylene glycol) dimethacrylate (TtEGDMA) were carried out at 60 °C in tetrahydrofuran solution in presence of 2,2-azobisisobutyronitrile. The random copolymers were prepared with nominal crosslinking ratios, X of 1, 5 and 10% mol TtEGDMA / mol CHMA. The copolymers were characterized by 13C NMR spectroscopy. The copolymers was characterized by 13C RMN analysis and determined the copolymers composition. The monomer reactivity ratios r1 (TtEGDMA) and r2 (CHMA) were determined with the linearized copolymerization equations of the Fineman–Ross methods (r1 = 1.77 and r2 = 0.48) and Kelen–Tüdös (r1 = 1.81 and r2 = 0.46). Parameters of Alfrey-Price Q1 = - 1.10 (specific activity) and e1= - 0.64 (polarity) for TtEGDMA.

scholarly journals Immobilization of glucoamylase on macroporous spheres

2004 ◽  
pp. 207-214 ◽  
Author(s):  
Nenad Milosavic ◽  
Radivoje Prodanovic ◽  
Slobodan Jovanovic ◽  
Zoran Vujcic
Keyword(s):  
Ethylene Glycol ◽  
Coupling Agent ◽  
Glycidyl Methacrylate ◽  
Specific Activity ◽  
Ethylene Glycol Dimethacrylate ◽  
Glycol Dimethacrylate ◽  
Temperature Optimum ◽  
Km Value ◽  
Spacer Arm ◽  
Starch Hydrolysate

Glucoamylase was covalently immobilized through the spacer-arm of the poly(glycidyl methacrylate-co-ethylene glycol dimethacrylate) spheres by using a glutaraldehyde as a coupling agent. The influence of the enzyme load applied to the support on immobilization, yield and specific activity, has been determined. Obtained specific activity was 700 U/g with immobilization yield of 35 %. The Km value for immobilized glucoamylase was 1.28 % (w/v), pH and temperature optimum were 4.5 and 70?C, respectively. The conversion of 20 % (w/w) starch hydrolysate achieved with the immobilized glucoamylase was 97 % after 5 hours.

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