Hydrolyzation of mogrosides: Immobilized β-glucosidase for mogrosides deglycosylation from Lo Han Kuo
Journal
Food Science and Nutrition
Journal Volume
7
Journal Issue
2
Date Issued
2019-02-01
Author(s)
Abstract
© 2019 The Authors. Food Science & Nutrition published by Wiley Periodicals, Inc. 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 (K m ) of the system was determined to be 0.33 mM. The kinetic parameters, rate constant (K) at which Mogrosides conversion was determined, the τ 50 in which 50% of mogroside V deglycosylation/mogroside IIIE production was reached, and the τ complete of complete mogroside V deglycosylation/mogroside IIIE production, were 0.044/0.017 min −1 , 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.
Subjects
glucosidase | immobilized enzyme | Lo Han Kuo | mogroside IIIE | mogroside V
Type
journal article