| Autor: |
de Oliveira RL; School of Food Engineering, Federal University of Agreste of Pernambuco/UFAPE, Av. Bom Pastor, Boa Vista, s/n, Garanhuns 55296-901, Brazil., Dos Santos AFA; Education Unit of Penedo, Federal University of Alagoas/UFAL, Avenida Beira Rio, s/n, Penedo 57200-000, Brazil., Cardoso BA; Education Unit of Penedo, Federal University of Alagoas/UFAL, Avenida Beira Rio, s/n, Penedo 57200-000, Brazil., da Silva Santos TS; Education Unit of Penedo, Federal University of Alagoas/UFAL, Avenida Beira Rio, s/n, Penedo 57200-000, Brazil., de Campos-Takaki GM; Nucleus of Research in Environmental Sciences and Biotechnology, Catholic University of Pernambuco/UNICAP, Rua do Príncipe, 526, Recife 50050-590, Brazil., Porto TS; Department of Morphology and Animal Physiology, Federal Rural University of Pernambuco/UFRPE, Av. Dom Manoel de Medeiros, s/n, Recife 52171-900, Brazil., Porto CS; Education Unit of Penedo, Federal University of Alagoas/UFAL, Avenida Beira Rio, s/n, Penedo 57200-000, Brazil. |
| Abstrakt: |
β-fructofuranosidases (FFases) are enzymes involved in sucrose hydrolysis and can be used in the production of invert sugar and fructo-oligosaccharides (FOS). This last is an important prebiotic extensively used in the food industry. In the present study, the FFase production by Aspergillus tamarii Kita UCP 1279 was assessed by solid-state fermentation using a mixture of wheat and soy brans as substrate. The FFase presents optimum pH and temperature at 5.0-7.0 and 60 °C, respectively. According to the kinetic/thermodynamic study, the FFase was relatively stable at 50 °C, a temperature frequently used in industrial FOS synthesis, using sucrose as substrate, evidenced by the parameters half-life (115.52 min) and D -value (383.76 min) and confirmed by thermodynamic parameters evaluated. The influence of static magnetic field with a 1450 G magnetic flux density presented a positive impact on FFase kinetic parameters evidenced by an increase of affinity of enzyme by substrate after exposition, observed by a decrease of 149.70 to 81.73 mM on K m . The results obtained indicate that FFases present suitable characteristics for further use in food industry applications. Moreover, the positive influence of a magnetic field is an indicator for further developments of bioprocesses with the presence of a magnetic field. |
