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Fungal glucoamylases

Paper ID Volume ID Publish Year Pages File Format Full-Text
14748 1245 2006 6 PDF Available
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 °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
Glucoamylase function; Fungal fermentation; Fungal enzymes; Biochemical properties; Kinetic characteristics; Industrial production
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Fungal glucoamylases
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Publisher
Database: Elsevier - ScienceDirect
Journal: Biotechnology Advances - Volume 24, Issue 1, January–February 2006, Pages 80–85
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering
Get Full-Text Now
Don't Miss Today's Special Offer
Price was $35.95
You save - $31
Price after discount Only $4.95
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Full-text PDF Download
Online Support
Any Questions? feel free to contact us