Immobilization of pectinmethylesterase from acerola (Malpighia glabra L.) in porous silica.
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.
de Assis
Sandra Aparecida
SA
Instituto de Química, Departamento de Bioquímica e Tecnologia Química, UNESP, Rua Prof. Francisco Degni, s/n. o, C.P. 355, CEP 14801-970, Araraquara, SP, Brasil.
Trevisan
Henrique Celso
HC
Mascarenhas
Olga Maria
OM
Oliveira
Faria
F
D002265:Carboxylic Ester Hydrolases / Q000737:chemistry* / Q000302:isolation & purification / Q000378:metabolism*; D020099:Coated Materials, Biocompatible / Q000138:chemical synthesis* / Q000737:chemistry; D004789:Enzyme Activation; D004795:Enzyme Stability; D004800:Enzymes, Immobilized / Q000737:chemistry; D006358:Hot Temperature; D006863:Hydrogen-Ion Concentration; D029581:Malpighiaceae / Q000737:chemistry / Q000201:enzymology*; D008567:Membranes, Artificial; D016062:Porosity; D012822:Silicon Dioxide / Q000737:chemistry*; D013696:Temperature
D020099:Coated Materials, Biocompatible; D004800:Enzymes, Immobilized; D008567:Membranes, Artificial; D012822:Silicon Dioxide; D002265:Carboxylic Ester Hydrolases; C022323:pectinesterase