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Immobilization of pectinmethylesterase from acerola (Malpighia glabra L.) in porous silica.
de Assis, Sandra Aparecida; Trevisan, Henrique Celso; Mascarenhas, Olga Maria; Oliveira, Faria.
Biotechnol Lett ; 25(11): 869-72, 2003 Jun.
Article in English | MEDLINE | ID: mdl-12889796

ABSTRACT

The total and partially purified enzyme pectinmethylesterase from acerola fruit was covalently immobilized on porous silica particles. These efficiency values were 114% for the total PME and 351% for the partially purified PME. In both forms the immobilization resulted in compounds with high thermal stability.


Subject(s)
Carboxylic Ester Hydrolases/chemistry , Carboxylic Ester Hydrolases/metabolism , Coated Materials, Biocompatible/chemical synthesis , Malpighiaceae/enzymology , Silicon Dioxide/chemistry , Carboxylic Ester Hydrolases/isolation & purification , Coated Materials, Biocompatible/chemistry , Enzyme Activation , Enzyme Stability , Enzymes, Immobilized/chemistry , Hot Temperature , Hydrogen-Ion Concentration , Malpighiaceae/chemistry , Membranes, Artificial , Porosity , Temperature
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