Open AccessHydrolyzation of mogrosides: Immobilized β‐glucosidase for mogrosides deglycosylation from Lo Han Kuo
Author(s) -
Wang HsuehTing,
Yang Jintong,
Chen KuanI,
Wang TanYing,
Lu TingJang,
Cheng KuanChen
Publication year - 2019
Publication title -
food science and nutrition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.614
H-Index - 27
ISSN - 2048-7177
DOI - 10.1002/fsn3.932
Subject(s) - chemistry , bioconversion , chromatography , immobilized enzyme , hydrolysis , michaelis–menten kinetics , enzyme , organic chemistry , enzyme assay , fermentation
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.