|Title:||Hydrolyzation of mogrosides: Immobilized £]-glucosidase for mogrosides deglycosylation from Lo Han Kuo||Authors:||Wang H.-T.
|Keywords:||glucosidase;immobilized enzyme;Lo Han Kuo;mogroside IIIE;mogroside V||Issue Date:||2019||Journal Volume:||7||Journal Issue:||2||Start page/Pages:||834-843||Source:||Food Science and Nutrition||Abstract:||
An immobilized enzyme system for bioconversion of Lo Han Kuo (LHK) mogrosides was established. £]-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¢XC. 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 £n 50 in which 50% of mogroside V deglycosylation/mogroside IIIE production was reached, and the £n 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. ? 2019 The Authors. Food Science & Nutrition published by Wiley Periodicals, Inc.
|Appears in Collections:||生物科技研究所|
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