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RevistaPROCESS BIOCHEMISTRY
Año2018
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Internacional

A NEW HETEROFUNCTIONAL AMINO-VINYL SULFONE SUPPORT TO IMMOBILIZE ENZYMES: APPLICATION TO THE STABILIZATION OF β-GALACTOSIDASE FROM Aspergillus oryzae

Autores:Roberto Fernandez-Lafuente
Grupos de investigación:Optimización de biocatalizadores y bioprocesos enzimáticos
Hadjer Zaak a,b,c, Mohamed Sassi c, Roberto Fernandez-Lafuente a,*.
 
a Departamento de Biocatálisis.  Instituto de Catálisis-CSIC, Campus UAM-CSIC Madrid, Spain.
b Food Biotechnology Division, Biotechnology Research Center (CRBt), Algeria
c Agrobiotechnology and nutrition in semi-arid zones Laboratory, Ibn Khalboun University, Algeria.
 The paper shows the preparation of a new heterofunctional agarose support: amino-vinylsulfone. This has been employed to immobilize the interesting enzyme β-galactosidase from Aspergillus oryzae. The enzyme cannot be immobilized on just vinylsulfone activated support a pH values ranging from 5.0 to 9.0. Neither the enzyme was immobilized using 200 mM of NaCl on amino-vinylsulfone support. However, the enzyme was readily immobilized at moderate ion strength at pH values from 5.0 to 9.0 via ion exchange on amino-vinylsulfone support, and later some covalent enzyme-support bonds could be formed, more rapidly at alkaline pH value. After optimization of immobilization pH, incubation pH and time, and blocking reagent, several immobilized biocatalysts on amino-vinylsulfone support having 50-80% of the initial activity and a stabilization factor of around 8-15 were prepared, depending on the exact immobilization conditions
Palabras clave:Enzyme stabilization, Enzyme immobilization, heterofunctional supports, divinylsulfone, ion exchange, enzyme orientation
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