Thermal stability and deactivation energy of free and immobilized invertase

• Autor(a) principal: Bassetti,F.J.
• Data de Publicação: 2000
• Outros Autores: Bergamasco,R., Moraes,F.F., Zanin,G.M.
• Tipo de documento: Artigo
• Idioma: eng
• Título da fonte: Brazilian Journal of Chemical Engineering
• Texto Completo: http://old.scielo.br/scielo.php?script=sci_arttext&pid=S0104-66322000000400050
• topic: invertase; thermal stability; immobilized invertase; sucrose; energy of deactivation

The thermal stability and the energy of deactivation of free invertase and the immobilized enzyme (IE) was measured at temperatures in the range of 35 to 65°C for the hydrolysis of a 5% w/v sucrose solution. The free enzyme at pH 5.0 is stable up to 50°C for a period of 4 h. Invertase immobilized in controlled pore silica by the silane-glutaraldehyde covalent method is stable up to 55ºC, in pH 4.5 for the same period. For higher temperatures the enzyme deactivation follows the exponential decay model and half-lives are 0.53, 1.80, and 13.9 h for free invertase, at 65, 60, and 55ºC, respectively. For the IE half-lives are 0.48, 1.83, and 20.9 h, at 65, 60, and 55ºC, respectively. The IE is more stable than the free invertase; the energy of deactivation being 83.1 kcal/mol for the IE and 72.0 kcal/mol for the free enzyme.