Go Back Research Article December, 1996

Purification and characterization of glucoamylase produced by Aspergillus niger in solid state fermentation

Author Ashok Pandey

Abstract

Glucoamylases produced by Aspergillus niger grown on wheat bran in solid cultures were purified. Four different forms, GA I, GA I', GA II and GA III, were found having apparent molecular weights of 112 000, 104 000, 74 000 and 61 000 Da respectively. The enzymes are glycoproteins with a carbohydrate content of 16%, and optimal activity at 60d̀C and pH 4.4. Activity was strongly inhibited by Hg2+ while Mn2+ and Fe2+ were stimulatory. The Km values for the degradation of starch and maltose were 3.5 and 7.8 mg ml-1, respectively.

Keywords

Glucoamylase Aspergillus Niger Wheat Bran Solid-State Fermentation Enzyme Purification Molecular Weight Glycoprotein Carbohydrate Content Optimal Temperature pH Stability Metal Ion Effect Enzyme Inhibition Enzyme Stimulation Hg2+ Inhibition Mn2+ Stimulation Fe2+ Stimulation Km Value Starch Degradation Maltose Degradation Industrial Enzyme Biochemical Characterization Fermentation Biotechnology Enzyme Activity Fungal Enzyme Protein Purification Biocatalysis Starch Hydrolysis Carbohydrate Metabolism Solid Cultures Enzyme Kinetics
Details
Volume 23
Issue 6
Pages 403-406
DOI 10.1111/j.1472-765X.1996.tb01346.x
ISSN 1472-765X
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