Production, purification and thermal characterisation of invertase from a newly isolated Fusarium sp. under solid‐state fermentation

Abstract

SummaryProduction of invertase employing a newly isolated Fusarium sp. under solid‐state fermentation was optimised. Different process parameters were optimised. The maximum enzyme activity under optimum conditions was 47.23 ± 2.12 U gds−1 with nitrogen additives. The enzyme was purified by ammonium sulphate precipitation, diethylaminoethyl cellulose ion‐exchange chromatography and Sephadex gel filtration. This protocol gave 20.25‐fold purification and 5.53% recovery. The optimum pH and temperature for activity were 5.0 and 50 °C. The Km and Vmax values for the enzyme were 8.33 mm and 21.48 μmol min−1, respectively. A detailed kinetic study of thermal inactivation has been carried out. Enthalpy of activation (ΔH*) decreased when entropy (ΔS*) of activation increased at higher temperatures. Moreover, free energy of denaturation (ΔG*) increased at higher temperature making the enzyme thermally stable. A possible explanation for the thermal inactivation of invertase at higher temperatures is also discussed.