Immobilization and characterization of inulinase from Ulocladium atrum on nonwoven fabrics

J Biosci. 2014 Dec;39(5):785-94. doi: 10.1007/s12038-014-9477-1.

Abstract

Ulocladium atrum inulinase was immobilized on different composite membranes composed of chitosan/nonwoven fabrics. Km values of free and immobilized U. atrum inulinase on different composite membranes were calculated. The enzyme had optimum pH at 5.6 for free and immobilized U. atrum inulinase on polyester nonwoven fabric coated with 3 percent chitosan solution (PPNWF3), but optimum pH was 5 for immobilized U. atrum inulinase on polyester and polypropylene nonwoven fabrics coated with 1 percent chitosan solution. The enzyme had optimum temperature at 40 degree C for immobilized enzyme on each of polyester and polypropylene composite membranes coated with 1 percent chitosan, while it was 50 degree C for free and immobilized enzyme on polypropylene nonwoven fabric coated with 3 percent chitosan solution. Free U. atrum inulinase was stable at 40 degree C but thermal stability of the immobilized enzyme was detected up to 60 degree C. Reusability of immobilized enzyme was from 38 to 42 cycles of reuse; after this, the immobilized enzyme lost its activity completely. In conclusion, immobilized U. atrum inulinase was considerably more stable than the free enzyme, and could be stored for extended periods.

MeSH terms

  • Ascomycota / enzymology*
  • Chitosan / chemistry*
  • Enzyme Stability
  • Enzymes, Immobilized / chemistry*
  • Glycoside Hydrolases / chemistry*
  • Glycoside Hydrolases / isolation & purification
  • Hydrogen-Ion Concentration
  • Kinetics
  • Surface Properties
  • Temperature

Substances

  • Enzymes, Immobilized
  • Chitosan
  • Glycoside Hydrolases
  • inulinase