INIQUI 05448
INSTITUTO DE INVESTIGACIONES PARA LA INDUSTRIA QUIMICA
Unidad Ejecutora - UE
artículos
Título:
Alpha-Amylase Aspergillus oryzae Immobilized on Modified Expanded Perlite
Autor/es:
J.J. RODRIGUEZ ZOTELO; F. SORIA; H. GERONAZZO; H. DESTEFANIS
Revista:
INTERNATIONAL JOURNAL OF CHEMICAL REACTOR ENGINEERING
Editorial:
BERKELEY ELECTRONIC PRESS
Referencias:
Lugar: Ontario; Año: 2014 vol. 12 p. 587 - 596
ISSN:
1542-6580
Resumen:
The alpha-amylase from Aspergillus oryzae was immobilized covalently onto expanded perlite (EP) and modified EP by treatment with TiO2 (EP-TiO2), dye HE3B (EP-HE3B) polyethylene terephthalate (PET)-hydrazide (EP-PET) and magnetite (EP-magnetite). The modified EP was characterized using Fourier transform infrared spectroscopy (FTIR) and scanning electron microscopy (SEM). The supports were functionalized with aminopropyltriethoxysilane (APTES) and glutaraldehyde (GA). The optimum pH for free and immobilized α-amylase was 5.5. Temperature of maximum activity for free enzyme and immobilized enzyme on EP-HE3B was 50°C. The immobilized enzyme in EP-APTES this value was 55°C. The immobilized α-amylase in EP-APTES and EP-HE3BAPTES exhibited better thermostability than free enzyme. The immobilized derivatives showed moderate operational stability by retaining 50% of initial activity after seven successive reuses.
