Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
14748 | Biotechnology Advances | 2006 | 6 Pages |
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 °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.
Keywords
Related Topics
Physical Sciences and Engineering
Chemical Engineering
Bioengineering
Authors
Dariush Norouzian, Azim Akbarzadeh, Jeno M. Scharer, Murray Moo Young,