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Immobilization of glucosyltransferase from Erwinia sp. using two different techniques
Fabiano Jares Contesini1, Carolina Ibarguren, Carlos Raimundo Ferreira Grosso
1Laboratory of Food Biochemistry, Department of Food Science, College of Food Engineering, State University of Campinas, Campinas, SP, Brazil. fabiano.contesini@gmail.com
Enzyme immobilization techniques were explored for converting sucrose to isomaltulose. Immobilizing glucosyltransferase on Celite 545 achieved over 60% conversion, while pectin microcapsules showed initial promise but limited stability.
Area of Science:
- Biocatalysis
- Enzyme Technology
- Carbohydrate Chemistry
Background:
- Glucosyltransferase (GTF) is crucial for sucrose conversion.
- Efficient enzyme immobilization is key for industrial applications.
- Isomaltulose is a valuable sucrose isomer with unique properties.
Purpose of the Study:
- To investigate two distinct glucosyltransferase immobilization methods.
- To optimize conditions for GTF immobilization onto Celite 545.
- To evaluate the efficacy of pectin microcapsules for GTF entrapment.
Main Methods:
- Response surface methodology was used to determine optimal immobilization conditions on Celite 545.
- Glucosyltransferase was entrapped in low-methoxyl pectin and fat microcapsules.
- Enzyme activity and sucrose conversion rates were monitored over multiple batches.
Main Results:
- Optimal immobilization on Celite 545 (pH 4.0, 170 U/g) yielded >60% sucrose to isomaltulose conversion.
- Non-lyophilized pectin microcapsules with fat exhibited higher initial GTF activity than lyophilized versions.
- Pectin microcapsules showed a significant decrease in conversion efficiency after the 10th batch due to enzyme inactivation.
Conclusions:
- Celite 545 immobilization offers a highly efficient method for isomaltulose production.
- Pectin microencapsulation presents challenges in long-term enzyme stability for continuous processes.
- Further research is needed to enhance the stability of enzymes within microcapsule systems.
