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Related Experiment Videos

Modeling and optimisation of D-fructose isomerisation using a fluorosensor.

V Abarna1, T K Radhakrishnan, S Sundaram

  • 1Department of Chemical Engineering, Regional Engineering College, Tiruchirappalli, India.

Biomedical Sciences Instrumentation
|June 2, 2000
PubMed
Summary
This summary is machine-generated.

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This study optimized D-fructose isomerization using Sweetzyme T, identifying an optimal substrate concentration of 0.04 M for maximum enzyme activity. Reaction kinetics followed a first-order model with high accuracy.

Area of Science:

  • Biocatalysis
  • Enzyme kinetics
  • Carbohydrate chemistry

Background:

  • Enzymatic isomerization of D-fructose is crucial for producing high-fructose syrups.
  • Optimizing enzyme concentration and reaction conditions is key to efficient bioprocessing.

Purpose of the Study:

  • To determine the optimal feed concentration of D-fructose for isomerization using Sweetzyme T.
  • To investigate the reaction kinetics and model the isomerization process.

Main Methods:

  • D-fructose isomerization was performed in a 1.5 L fermentor with Sweetzyme T at 40°C.
  • Five feed concentrations (0.01–1.0 M) were tested, with stirring at 100 rpm.
  • Reaction progress was monitored using a Dr. Ingold Fluorosensor, recording fluorescence voltage over time.

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Main Results:

  • Maximum fluorescence voltage, indicating optimal reaction rate, was observed at 0.04 M D-fructose.
  • Enzyme activity increased with substrate concentration up to 0.04 M, then decreased.
  • Fluorescence voltage-time data accurately fitted a first-order kinetic model (<0.8% error).

Conclusions:

  • The optimal D-fructose concentration for Sweetzyme T-catalyzed isomerization is 0.04 M.
  • The isomerization reaction follows predictable first-order kinetics, facilitating process scale-up.
  • Fluorosensor monitoring provides an effective method for real-time assessment of enzyme activity.