Kinetic properties and storage stability of catalase immobilized on to florisil

Indian J Biochem Biophys. 2007 Feb;44(1):38-43.

Abstract

The covalent immobilization of bovine liver catalase (CAT) on to florisil via glutaraldehyde was investigated. Optimum immobilization pH and temperature were determined as pH 6.0, 10 degrees C respectively, while the amount of initial CAT per g of carrier and immobilization time was determined as 5 mg g(-1) and 120 min, respectively. The Vmax values for free and immobilized CAT were found to be 1.7 x 10(5) and 2.0 x 10(4) micromol H2O2 min(-1) mg protein(-1), respectively, whereas KM values were 33.3 mM and 1722.0 mM respectively. Operational stability was determined by using a stirred batch-type column reactor. Immobilized CAT retained about 40% of its initial activity after 50 uses. It showed higher storage stability than free CAT at 4 degrees C and 25 degrees C. Its storage stability increased with increasing relative humidity (RH) from 0 to 20% of the medium. The highest storage stability was obtained in 20% RH, however, further increase in RH from 40 to 100% significantly decreased the storage stability.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Buffers
  • Catalase / chemistry
  • Catalase / metabolism*
  • Cattle
  • Drug Storage
  • Enzyme Stability
  • Enzymes, Immobilized / chemistry
  • Enzymes, Immobilized / metabolism*
  • Hydrogen-Ion Concentration
  • In Vitro Techniques
  • Kinetics
  • Liver / enzymology
  • Magnesium Silicates

Substances

  • Buffers
  • Enzymes, Immobilized
  • Magnesium Silicates
  • Florisil
  • Catalase