Kinetics of sucrose conversion to fructo-oligosaccharides using enzyme (invertase) under free condition

• Published in: Bioprocess and biosystems engineering 2014-12, Vol.37 (12), p.2529-2537
• Main Authors: Khandekar, Deepa C., Palai, Tapas, Agarwal, Aman, Bhattacharya, Prashant K.
• Format: Article
• Language: English
• Subjects: beta-Fructofuranosidase - chemistry; Bioengineering; Biotechnology; Chemistry; Chemistry and Materials Science; Chromatography, High Pressure Liquid; Computer Simulation; Environmental Engineering/Biotechnology; Enzymes; Food Science; Fructose - chemistry; Glucose - chemistry; Hydrogen-Ion Concentration; Industrial and Production Engineering; Industrial Chemistry/Chemical Engineering; Kinetics; Oligosaccharides - chemistry; Original Paper; Saccharomyces cerevisiae; Saccharomyces cerevisiae - enzymology; Software; Sucrose; Sucrose - chemistry; Temperature; Trisaccharides - chemistry; Yeast
• ISSN: 1615-7591; 1615-7605
• DOI: 10.1007/s00449-014-1230-5

The study reports the synthesis of fructo-oligosaccharide (FOS) from sucrose using invertase derived from Saccharomyces cerevisiae . The reaction was conducted in a batch mode under free enzyme condition. Fructo-oligosaccharide formation was detected at a high sucrose concentration of over 200 g/L. The investigation was extended to study the effect of different parameters such as initial sucrose concentration (ISC), pH, and enzyme concentration. A maximum FOS yield of 10 % (dry basis) was observed using 525 g/L of ISC, with 6 U/mL of the enzyme, and pH 5.5 at 40 °C. 1-Kestose was the major product of among different forms of FOS. The FOS yield increased with an increase in sucrose concentration up to 525 g/L, beyond which it started to decrease. However, the maximum FOS yield was not affected by the increasing concentration of the enzyme beyond a certain level (2 U/mL). Furthermore, the activity of enzyme slightly increased with an increase in the pH up to 6, and thereafter it declined. Addition of glucose decreased the FOS yield because of enzyme inhibition. A five-step, ten-parameter model was developed, for which the simulation was performed in COPASI. The results predicted by the model were consistent with the experimental data.