β-galactosidase from Kluyveromyces lactis in genipin-activated chitosan: An investigation on immobilization, stability, and application in diluted UHT milk
| Autor: | Isadora Gazoni, Daniela Bresolin, Alexandra Melissa Gonçalves de Carvalho, Pâmela Cristina Lima, Darlene Cavalheiro, Elisandra Rigo, Débora de Oliveira |
|---|---|
| Rok vydání: | 2020 |
| Předmět: |
Thermogravimetric analysis
Immobilized enzyme Lactose 01 natural sciences Analytical Chemistry Chitosan chemistry.chemical_compound Hydrolysis Kluyveromyces 0404 agricultural biotechnology Enzyme Stability Animals Thermal stability Iridoids Kluyveromyces lactis biology Chemistry 010401 analytical chemistry 04 agricultural and veterinary sciences General Medicine biology.organism_classification Enzymes Immobilized beta-Galactosidase 040401 food science Enzyme assay 0104 chemical sciences Milk Genipin biology.protein Food Science Nuclear chemistry |
| Zdroj: | Food chemistry. 349 |
| ISSN: | 1873-7072 |
| Popis: | The objective of this research was to evaluate the immobilization of the enzyme β-galactosidase in a genipin-activated chitosan support. The influence of the number of spheres and substrate concentration on immobilization yield (IY) and enzyme activity (EA) was analyzed using experimental design. Thermal, operational and storage stabilities were assessed, and the enzymatic derivatives were characterized by thermogravimetric analysis (TGA) and scanning electron microscopy (SEM). The TGA showed that the enzymatic derivatives kept their thermal behavior, and the SEM images revealed smooth surfaces in all the spheres. The optimized conditions for the immobilization process were 4.57 mg·mL−1 of spheres and a substrate concentration of 10 mM (IY = 84.13%; EA = 24.97 U·g−1). Thermal stability was enhanced at 10 and 37 °C, enabling four successive cycles of lactose hydrolysis in diluted UHT milk. Therefore, the immobilized enzyme in genipin-activated chitosan has potential for lactose hydrolysis and applications in the food industry. |
| Databáze: | OpenAIRE |
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