Hydrolysis of soybean isoflavones by Debaryomyces hansenii UFV-1 immobilised cells and free β-glucosidase
| Autor: | Lorena Gusmão Alvarenga Lage, Valéria Monteze Guimarães, Evan Michael Visser, Gabriela Piccolo Maitan-Alfenas, Maíra Nicolau de Almeida, Sebastião Tavares de Rezende |
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| Rok vydání: | 2013 |
| Předmět: |
Calcium alginate
Debaryomyces Cellobiose Analytical Chemistry Fungal Proteins chemistry.chemical_compound Hydrolysis Soy molasses Debaryomyces hansenii Enzyme Stability Debaryomyces hansenii UFV-1 Immobilisation Food science Thermostability chemistry.chemical_classification biology beta-Glucosidase General Medicine Cells Immobilized biology.organism_classification Isoflavones Yeast β-Glucosidase Kinetics Enzyme chemistry Biochemistry Soybeans Food Science |
| Zdroj: | LOCUS Repositório Institucional da UFV Universidade Federal de Viçosa (UFV) instacron:UFV |
| ISSN: | 1873-7072 |
| Popis: | An intracellular β-glucosidase from Debaryomyces hansenii UFV-1 was produced in an YP medium with cellobiose as the carbon source. This enzyme was purified, characterised and presented a Mr of 65.15 kDa. Yeast cells containing the intracellular β-glucosidase were immobilised in calcium alginate. The free β-glucosidase and immobilised cells containing the enzyme presented optima values of pH and temperature of 6.0 and 45 °C and 5.5 and 50 °C, respectively. The free enzyme maintained 62% and 47% of its original activity after 90 days at 4 °C and after 15 days at room temperature, respectively. The immobilisation process resulted in higher enzyme thermostability at 45 and 50 °C. Soy molasses treatment with the free enzyme and the immobilised cells containing β-glucosidase, for 2 h at 40 °C, promoted efficient hydrolysis of isoflavone glicosides to their aglycon forms. The results suggest that this enzyme could be used in the food industry, in the free or immobilised forms, for a safe and efficient process to hydrolyse isoflavone glycosides in soy molasses. |
| Databáze: | OpenAIRE |
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