Abstract
Amyloglucosidase from Novo (Copenhagen, Denmark) was immobilized in controlled pore silica particles with the silane-glutaraldehyde covalent method. Thermal stability of the free and immobilized enzyme (IE) was determined with 30% (w/v) α-amylase liquefied cassava starch, pH 4.5, temperatures from 35 to 75°C. Free amyloglucosidase maintained its activity practically constant for 240 min and temperatures up to 50°C. The IE has shown higher stability retaining its activity for the same period up to 60°C. Half-life for free enzyme was 20.6, 6.44, 2.07, 0.69, and 0.24 h for 55, 60, 65, 70, and 75°C, respectively, whereas the IE at the same temperatures had half-lives of 116.4, 30.88, 8.52, 2.44, and 0.73 h. The energy of thermal deactivation was thus 50.6 and 57.6 kcal/mol, respectively for the free and IE, confirming stabilization by immobilization.
Author to whom all correspondence and reprint requests should be addressed. E-mail: gisellazanin@cybertelecom.com.br
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Zanin, G.M., De Moraes, F.F. (1998). Thermal Stability and Energy of Deactivation of Free and Immobilized Amyloglucosidase in the Saccharification or Liquefied Cassava Starch. In: Finkelstein, M., Davison, B.H. (eds) Biotechnology for Fuels and Chemicals. Applied Biochemistry and Biotechnology. Humana Press, Totowa, NJ. https://doi.org/10.1007/978-1-4612-1814-2_36
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DOI: https://doi.org/10.1007/978-1-4612-1814-2_36
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