An immobilized enzyme system for bioconversion of Lo Han Kuo (LHK) mogrosides was established. β-Glucosidase which was covalently immobilized onto the glass spheres exhibited a significant bioconversion efficiency from pNPG to pnitrophenol over other carriers. Optimum operational pH and temperature were determined to be pH 4 and 30°C. Results of storage stability test demonstrated that the glass sphere enzyme immobilization system was capable of sustaining more than 80% residual activity until 50 days, and operation reusability was confirmed for at least 10 cycles. The Michaelis constant ( ) of the system was determined to be 0.33 mM. The kinetic parameters, rate constant () at which Mogrosides conversion was determined, the in which 50% of mogroside V deglycosylation/mogroside IIIE production was reached, and the complete of complete mogroside V deglycosylation/mogroside IIIE production, were 0.044/0.017 min, 15.6/41.1 min, and 60/120 min, respectively. Formation of the intermediates contributed to the kinetic differences between mogroside V deglycosylation and mogroside IIIE formation.
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| http://dx.doi.org/10.1002/fsn3.932 | DOI Listing |
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