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Review
. 2006 Jan-Feb;24(1):80-5.
doi: 10.1016/j.biotechadv.2005.06.003. Epub 2005 Aug 8.

Fungal glucoamylases

Dariush Norouzian  1 , Azim Akbarzadeh, Jeno M Scharer, Murray Moo Young
Affiliations
Review

Fungal glucoamylases

Dariush Norouzian et al. Biotechnol Adv. 2006 Jan-Feb.

Abstract

Fungi are employed to produce industrially important glucoamylases. Most glucoamylases are glycosylated. Glycosylation enhances the enzyme stability. Glucoamylases contain both starch binding and catalytic binding domains, the former being responsible for activity on raw (insoluble) starch. Proteases may act on this domain causing the enzyme to lose its activity on insoluble starch. Optimal activity is observed at pH 4.5 to 6.5 and 50 to 70 degrees C. Glucoamylases contain up to 7 sub-sites with highly varying affinity. They can be produced by different methods including submerged, solid state and semi-solid state fermentation processes.

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