Aspergillus niger glucoamylase from

SoKd substrate fermentation using agricultural wastes was considered to be used for the production of both enzymes in order to reduce the production costs. Production of glucoamylase from Aspergillus niger J8 was reported (1,3). This report concerned on the production of pectinases from Rhizopus sp. 26R in solid substrates composting of agricultural wastes, optimization of the conditions for pectinases production in solid substrates and the estimation of the production cost. 

The efficiency in raw cassava starch hydrolyzation of pectinases from Rhizopus sp. 26R compared with a commercial pectinase when mixed with Glucoamylase from Aspergillus niger J8. 

Christensen, T., B. Svensson, and B.W. Sigurskjold. 1999. Thermodynamics of reversible and irreversible unfolding and domain interactions of glucoamylase from Aspergillus niger studied by differential scanning and isothermal titration calorimetry. Biochemistry 38 6300-6310. 

Sigurskjold, B.W., C.R. Berland, and B. Svensson. 1994. Thermodynamics of inhibitor binding to the catalytic site of glucoamylase from Aspergillus niger determined by displacement titration calorimetry. Biochemistry 33 10191-10199. 

For determination of starch concentration, starch was first hydrolyzed with glueoamylase to glucose. Glucoamylase from Aspergillus niger (6,100 U/mL, Sigma) was used for measurement of starch concentration after diluted 100 times with distilled water. Culture broth of 0.1 mL and 0.8 mL Dl water were preincubated at 30 °C for 5 min before adding... 

Glucoamylase from Aspergillus niger has been used in a study of the hydrolysis of starch in a membrane reactor in which an Amicon ultrafiltration cell was employed.It was shown that the enzyme did reduce the formation of a gel layer and gave higher and more stable performances of the membrane reactor than the ones obtained in previous studies. 

Maltose has been used frequently as a substrate in the assay of glucoamylase because of the simplicity of analysis, a practice which has caused no difficulty since the enzyme is reported to follow Michaelis-Menten kinetics. However, tests of glucoamylase from Aspergillus niger over an extended concentration range exhibited a decided deviation from Michaelis-Menten kinetics. Explanations as to why this may be the rule rather than the exception were offered. 

Two fractional model for evaluating the activity of glucoamylase from Aspergillus niger under combined pressure and temperature conditions. 

J.H. Pazur, Glucoamylase from Aspergillus niger. Methods Enzymol, 1972, 28, 931-934. 

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