Continuous cellobiose hydrolysis using self-immobilized β-glucosidase from Aspergillus phoenicis QM 329 in a fluidized-bed reactor

K. Réczey, Henrik StalbrÅnd, Ingrid Persson, BÄrbel Hahn-HÄgerdal, Folke Tjerneld

Research output: Contribution to journalArticle

7 Citations (Scopus)

Abstract

Aspergillus phoenicis QM 329 was grown in the shape of beads in shake flasks and in an air-lift fermentor. The production of β-glucosidase started when the carbon source, glucose, was consumed. The β-glucosidase activity was retained in the beads at a pH below 6.0. The influence of bead diameter on enzyme activity and the pH and temperature optima for cellobiose hydrolysis has been studied. The enzyme-containing beads were used in a fluidized-bed reactor for continuous cellobiose hydrolysis, and a productivity of 2.0 g/L-h at a substrate conversion of 76% was obtained. The self-immobilized β- glucosidase is a stable and reusable enzyme with a half-life of 700 h when operating at 50°C and pH 4.8.

Original languageEnglish
Pages (from-to)637-649
Number of pages13
JournalApplied Biochemistry and Biotechnology - Part A Enzyme Engineering and Biotechnology
Volume24-25
Issue number1
DOIs
Publication statusPublished - Mar 1990

Fingerprint

Glucosidases
Cellobiose
Aspergillus
Fluidized beds
Hydrolysis
Enzymes
Enzyme activity
Bioreactors
Glucose
Half-Life
Carbon
Productivity
Air
Temperature
Substrates

Keywords

  • β glucosidase
  • Aspergillus phoenicis
  • cellobiose hydrolysis
  • fluidized-bed reactor
  • immobilization

ASJC Scopus subject areas

  • Bioengineering
  • Biotechnology
  • Biochemistry
  • Biochemistry, Genetics and Molecular Biology(all)
  • Applied Microbiology and Biotechnology
  • Environmental Engineering
  • Molecular Biology

Cite this

Continuous cellobiose hydrolysis using self-immobilized β-glucosidase from Aspergillus phoenicis QM 329 in a fluidized-bed reactor. / Réczey, K.; StalbrÅnd, Henrik; Persson, Ingrid; Hahn-HÄgerdal, BÄrbel; Tjerneld, Folke.

In: Applied Biochemistry and Biotechnology - Part A Enzyme Engineering and Biotechnology, Vol. 24-25, No. 1, 03.1990, p. 637-649.

Research output: Contribution to journalArticle

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