Aspergillus 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. 

E. M. S. Harris, A. E. Aleshin, L. M. Firsov, and R. B. Honzatko, Refined structure of the complex of 1-deoxynojirimycin with glucoamylase from Aspergillus awamori var. X100 to 2.4-A resolution, Biochemistry, 32 (1993) 1618—1626. 

Pavezzi, F. C., Gomes, E., da Silva, R. (2008). Production and characterization of glucoamylase from fungus Aspergillus awamori expressed in yeast Saccharomyces cerevisiae using different carbon sources. Braz. 

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... 

Pure glucoamylase from Rhizopus nivetis from Aspergillus niger glucose 90 n.d. 80-100 65-75 80-100 40-50... 

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. 

Studies of the hydrolyses of cyclohexa-, cyclohepta-, and cyclo-octa-amyloses by Taka-amylase A (one of the a-amylases from Aspergillus oryzae) indicated that each cycloamylose binds to the same active site of the enzyme. Since there is little difference in the respective AG, Af/, and AS values for enzymic hydrolysis of these cycloamyloses, their binding modes appear to be similar. The extent of multiple attack on the cycloamyloses was not affected by temperature. A 4-phenylazobenzoyl derivative of Taka-amylase A has been used to investigate the active site of the enzyme. A. oryzae a-amylase has a synergistic effect on the action of the glucoamylase from A. awamori var. kawachi ... 

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. 

Possible synergistic effects in the combined actions of an a-amylase (from Aspergillus oryzae) and a glucoamylase (from A, awamori) have been investigated. ... 

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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