title: Fungal glucoamylases.
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.
authors.affiliation: Department of Chemical Engineering, University of Waterloo, Ontario, Canada. danorouzian@yahoo.com
authors.forename: Dariush
authors.initials: D
authors.lastname: Norouzian
authors.forename: Azim
authors.initials: A
authors.lastname: Akbarzadeh
authors.forename: Jeno M
authors.initials: JM
authors.lastname: Scharer
authors.forename: Murray
authors.initials: M
authors.lastname: Moo Young
mesh_terms: D002384:Catalysis; D005658:Fungi / Q000201:enzymology*; D005087:Glucan 1,4-alpha-Glucosidase / Q000096:biosynthesis* / Q000737:chemistry*; D007700:Kinetics
chemical_list: D005087:Glucan 1,4-alpha-Glucosidase