Kinetics and Thermodynamics of Thermal Inactivation of β-Galactosidase from Aspergillus oryzae
Braz. arch. biol. technol
; 61: e18160489, 2018. tab, graf
Article
in English
| LILACS
| ID: biblio-951495
Responsible library:
BR1.1
ABSTRACT
ABSTRACT For optimization of biochemical processes in food and pharmaceutical industries, the evaluation of enzyme inactivation kinetic models is necessary to allow their adequate use. Kinetic studies of thermal inactivation of β-galactosidase from Aspergillus oryzae were conducted in order to critically evaluate mathematical equations presented in the literature. Statistical analysis showed that Weibull model presented the best adequacy to residual enzymatic activity data through the processing time and its kinetic parameters as a function of the temperature, in the range of 58-66 ºC. The investigation suggests the existence of a non-sensitive heat fraction on the enzyme structure, which is relatively stable up to temperatures close to 59 ºC. Thermodynamic parameters were evaluated and showed that such β-galactosidase presents activation energy of 277 kJ mol-1 and that the enzyme inactivation is due to molecular structural changes. Results shown that the enzyme is quite stable for biotechnological applications.
Full text:
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Collection:
International databases
Database:
LILACS
Language:
English
Journal:
Braz. arch. biol. technol
Journal subject:
Biology
Year:
2018
Document type:
Article
Affiliation country:
Brazil
Institution/Affiliation country:
Universidade Estadual do Rio Grande do Sul/BR
/
Universidade Federal de Ciências da Saúde de Porto Alegre/BR
/
Universidade Federal de Santa Catarina/BR
/
Universidade Federal do Rio Grande do Sul/BR