Characterization of free and immobilized invertase regarding activity and energy of activation

Invertase from NOVO Nordisk has been immobilized in controlled pore silica particles (diameter: 0.351 mm and mean pore size: 37.5 nm) by covalent binding with the silane-glutaraldehyde method. The activity of the free and immobilized enzyme (IE) was determined with 5% (w/v) sucrose, at 35 to 65ºC an...

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Bibliographic Details
Published inBrazilian journal of chemical engineering Vol. 17; no. 4-7; pp. 873 - 880
Main Authors Bergamasco, R., Bassetti, F.J., Moraes, F.F. de, Zanin, G.M.
Format Journal Article
LanguageEnglish
Published Brazilian Society of Chemical Engineering 01.12.2000
Subjects
ENGINEERING, CHEMICAL
immobilized invertase
controlled pore silica
sucrose
invertase
energy of activation
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Summary:Invertase from NOVO Nordisk has been immobilized in controlled pore silica particles (diameter: 0.351 mm and mean pore size: 37.5 nm) by covalent binding with the silane-glutaraldehyde method. The activity of the free and immobilized enzyme (IE) was determined with 5% (w/v) sucrose, at 35 to 65ºC and pH from 3 to 7. Maximum activities were found in the pH range from 5 to 6 for free invertase, and pH 4.5 for the IE. Activity yield for the IE was 24%. The Energy of Activation (Ea) was found to be a function of pH, giving for free invertase, Ea = 7.0 and 6.86 kcal/mol at pH 5.0 and 5.5, respectively, whereas for the immobilized enzyme, Ea = 6.55 and 5.93 kcal/mol at pH 4.5 and 5.0, respectively.
ISSN:0104-6632
1678-4383
0104-6632
DOI:10.1590/S0104-66322000000400051