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.