Immobilization of beta-fructofuranosidase from Aspergillus japonicus on chitosan using tris(hydroxymethyl)phosphine or glutaraldehyde as a coupling agent

Biotechnol Lett. 2005 Mar;27(5):335-8. doi: 10.1007/s10529-005-0984-x.

Abstract

A partially purified beta-fructofuranosidase from Aspergillus japonicus was covalently immobilized on to chitosan beads using either glutaraldehyde or tris(hydroxymethyl)phosphine (THP) as a coupling agent. Compared with the glutaraldehyde-immobilized and the free enzyme, the THP-immobilized enzyme had the highest thermal stability with 78% activity retained after 12 days at 37 degrees C. The THP-immobilized enzyme also had higher reusability than that immobilized by glutaraldehyde, 75% activity was retained after 11 batches (or 11 days) at 37 degrees C for the THP immobilized enzyme system. Less yield (48%) of fructooligosaccharides (FOS) were produced by the THP-immobilized enzyme compared with the free enzyme system (58%) from 50 (w/v) sucrose at 50 degrees C.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Aspergillus / metabolism*
  • Biotechnology / methods*
  • Chitin / chemistry
  • Chitosan / chemistry*
  • Enzyme Stability
  • Enzymes, Immobilized / chemistry*
  • Glutaral / chemistry*
  • Hydrogen-Ion Concentration
  • Oligosaccharides / chemistry
  • Organophosphorus Compounds / chemistry*
  • Phosphines / chemistry
  • Phosphines / pharmacology*
  • Sucrose / chemistry
  • Temperature
  • Time Factors
  • beta-Fructofuranosidase / chemistry*

Substances

  • Enzymes, Immobilized
  • Oligosaccharides
  • Organophosphorus Compounds
  • Phosphines
  • Chitin
  • Sucrose
  • Chitosan
  • beta-Fructofuranosidase
  • phosphine
  • Glutaral
  • tris(hydroxymethyl)phosphine