Abstract
Crude extracellular invertase fromSclerotium rolfsii, when coupled to glutaraldehyde activated Indion 48-R, retained 70–80% activity of the soluble enzyme. Immobilization resulted in a decrease in the pH and temperature optima but it increased the temperature stability. Km and Vmax also increased as a result of immobilization. Both soluble and immobilized invertase showed inhibition at high substrate concentrations. The bound enzyme showed excellent stability to repeated use and retained approx 90% of its initial activity after 8 cycles of use.
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Kotwal, S.M., Shankar, V. Preparation and properties of sclerotium rolfsii invertase immobilized on indion 48-R. Appl Biochem Biotechnol 62, 151–158 (1997). https://doi.org/10.1007/BF02787991
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DOI: https://doi.org/10.1007/BF02787991