Improvement in the Thermostability of a Recombinant β-Glucosidase Immobilized in Zeolite under Different Conditions

β-Glucosidase is part of the cellulases and is responsible for degrading cellobiose into glucose, a compound that can be used to produce biofuels. However, the use of the free enzyme makes the process more expensive. Enzyme immobilization improves catalytic characteristics and supports, such as zeol...

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Published in:Molecules (Basel, Switzerland) Switzerland), 2022-06, Vol.27 (13), p.4105
Main Authors: Ramírez-Ramírez, Luis Gerardo, Zazueta-Álvarez, David Enrique, Fileto-Pérez, Héctor Alonso, Reyes-Jáquez, Damián, Núñez-Núñez, Cynthia Manuela, Galindo-De la Rosa, Juan de Dios, López-Miranda, Javier, Vázquez-Ortega, Perla Guadalupe
Format: Article
Language:English
Subjects:
Adsorption
beta-Glucosidase - metabolism
Biocatalysts
Biofuels
Cellobiose
Cellulase
Cellulose
Chromatography
E coli
Enzymatic activity
enzyme immobilization
Enzyme Stability
Enzymes
Enzymes, Immobilized - chemistry
Glucose
Glucosidase
Hydrogen-Ion Concentration
Hydrolysis
Immobilization
Ion exchange
Porous materials
Proteins
Temperature
Thermal stability
zeolite
Zeolites
β-Glucosidase
β-glucosidases
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Summary:β-Glucosidase is part of the cellulases and is responsible for degrading cellobiose into glucose, a compound that can be used to produce biofuels. However, the use of the free enzyme makes the process more expensive. Enzyme immobilization improves catalytic characteristics and supports, such as zeolites, which have physical-chemical characteristics and ion exchange capacity that have a promising application in the biotechnological industry. This research aimed to immobilize by adsorption a recombinant β-glucosidase from , obtained in BL21 (DE3), in a commercial zeolite. A Box Behnken statistical design was applied to find the optimal immobilization parameters, the stability against pH and temperature was determined, and the immobilized enzyme was characterized by SEM. The highest enzymatic activity was determined with 100 mg of zeolite at 35 °C and 175 min. Compared to the free enzyme, the immobilized recombinant β-glucosidase presented greater activity from pH 2 to 4 and greater thermostability. The kinetic parameters were calculated, and a lower K value was obtained for the immobilized enzyme compared to the free enzyme. The obtained immobilization parameters by a simple adsorption method and the significant operational stability indicate promising applications in different fields.
ISSN:1420-3049
1420-3049
DOI:10.3390/molecules27134105