AI Article Synopsis

  • An immobilized enzyme system was created for converting Lo Han Kuo mogrosides, showing high efficiency with β-Glucosidase on glass spheres compared to other methods.
  • The best conditions for this process were found to be pH 4 and 30°C, with the enzyme maintaining over 80% effectiveness for 50 days and being reusable for at least 10 cycles.
  • Key kinetic parameters were identified, indicating the rates and times needed for the conversion of specific mogrosides, with the formation of intermediates affecting the differences in the conversion rates.

Article 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 ( ) 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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Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC6392867PMC
http://dx.doi.org/10.1002/fsn3.932DOI Listing

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