Enhancement of operation and storage stability of glucoamylase from Aspergillus awamori by a protease inhibitor preparation

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Abstract

Glucoamylase was produced extracellularly by fermentation of strain Aspergillus awamori, which had been genetically modified to have high-level glucoamylase activity. Initial experiments showed that the enzyme deactivated quickly, with a half-life of less than 6 days even stored at 5°C. A possible reason for the rapid deactivation was the presence of proteases, attacking and degrading the glucoamylase. Therefore a liquid protease inhibitor cocktail (Sigma, USA) was selected and applied to enhance the stability of the enzyme. The activity of the enzyme (stored at 5°C) measured by the Schoorl-method with starch as substrate showed that the cocktail was effective with the enzyme maintaining 95% of its initial storage activity for almost one year. The enzyme preparation has been used for starch hydrolysis in a flat-sheet membrane bioreactor at 60°C to manufacture glucose solution and its operation stability extended by using the cocktail.

Original languageEnglish
Pages (from-to)281-284
Number of pages4
JournalBiocatalysis and Biotransformation
Volume23
Issue number3-4
DOIs
Publication statusPublished - May 1 2005

Keywords

  • Aspergillus awamori
  • Glucoamylase
  • Membrane bioreactor
  • Starch hydrolysis

ASJC Scopus subject areas

  • Biotechnology
  • Catalysis
  • Biochemistry

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