Hydrolyzation of mogrosides: Immobilized β‐glucosidase for mogrosides deglycosylation from Lo Han Kuo

Food Science and Nutrition - Tập 7 Số 2 - Trang 834-843 - 2019
Hsueh‐Ting Wang1, Jintong Yang1, Kuan‐I Chen1, Tan‐Ying Wang1, Ting‐Jang Lu1, Kuan‐Chen Cheng2,1,3
1Graduate Institute of Food Science and Technology, National Taiwan University, Taipei, Taiwan, ROC
2Department of Medical Research, China Medical University Hospital, China Medical University, Taichung, Taiwan, ROC
3Institute of Biotechnology, National Taiwan University, Taipei, Taiwan, ROC

Tóm tắt

Abstract

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 (Km) of the system was determined to be 0.33 mM. The kinetic parameters, rate constant (K) at which Mogrosides conversion was determined, the τ50 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.

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Thông tin xuất bản

Food Science and Nutrition

Tập 7 Số 2

834-843

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