PURIFICATION AND PROPERTIES OF PHOSPHOGLUCOSE ISOMERASE FROM ASPERGILLUS NIGER

1959 ◽  
Vol 37 (8) ◽  
pp. 927-932 ◽  
Author(s):  
Kartar Singh
Keyword(s):  
Calcium Phosphate ◽  
Aspergillus Niger ◽  
Metal Ions ◽  
Maximum Activity ◽  
Phosphoglucose Isomerase ◽  
Muscle Enzyme ◽  
Purification And Properties ◽  
Optimum Ph ◽  
Ammonium Sulphate Fractionation ◽  
Kinetics Of

Phosphoglucose isomerase from Aspergillus niger was purified about fiftyfold by ammonium sulphate fractionation and treatment with calcium phosphate gel. The properties and kinetics of the enzyme are described. The enzyme resembled the muscle phosphoglucose isomerase in not requiring metal ions for activation but differed in showing no inhibition with phosphate. The enzyme showed maximum activity between pH 7.8 to 8.0 as compared with the optimum pH 9.0 shown by the muscle enzyme.

PURIFICATION AND PROPERTIES OF PHOSPHOGLUCOSE ISOMERASE FROM ASPERGILLUS NIGER

1959 ◽  
Vol 37 (1) ◽  
pp. 927-932 ◽  
Author(s):  
Kartar Singh
Keyword(s):  
Calcium Phosphate ◽  
Aspergillus Niger ◽  
Metal Ions ◽  
Maximum Activity ◽  
Phosphoglucose Isomerase ◽  
Muscle Enzyme ◽  
Purification And Properties ◽  
Optimum Ph ◽  
Ammonium Sulphate Fractionation ◽  
Kinetics Of

Phosphoglucose isomerase from Aspergillus niger was purified about fiftyfold by ammonium sulphate fractionation and treatment with calcium phosphate gel. The properties and kinetics of the enzyme are described. The enzyme resembled the muscle phosphoglucose isomerase in not requiring metal ions for activation but differed in showing no inhibition with phosphate. The enzyme showed maximum activity between pH 7.8 to 8.0 as compared with the optimum pH 9.0 shown by the muscle enzyme.

scholarly journals Production of glucose and fructose syrups from cassava (Manihot esculenta Crantz) starch using enzymes produced by microorganisms isolated from Brazilian Cerrado soil

2010 ◽  
Vol 30 (1) ◽  
pp. 213-217 ◽  
Author(s):  
Roberto do Nascimento Silva ◽  
Fábio Pereira Quintino ◽  
Valdirene Neves Monteiro ◽  
Eduardo Ramirez Asquieri
Keyword(s):  
Aspergillus Niger ◽  
Manihot Esculenta ◽  
Glucose Isomerase ◽  
Cassava Starch ◽  
Maximum Activity ◽  
Brazilian Cerrado ◽  
Initial Activity ◽  
Manihot Esculenta Crantz ◽  
Streptomyces Sp ◽  
Optimum Ph

The high demands for sugars and the development of enzymatic technology have increased the production of sweeteners, especially for glucose and fructose syrups. This work describe a technology for glucose and fructose syrups from Brazilian cassava starch using enzymes produced by soil microrganisms isolated from the Brazilian Cerrado soil. Firstly, Aspergillus niger and Streptomyces sp. were isolated from the soil and used as glucoamylase (GA) and glucose isomerase (GI) producer sources. After characterization, GA and GI exhibited optimum pH 4.5 and 8.0, respectively. GA showed maximum activity at 60 ºC and GI at 85 ºC. GA and GI retained 65 and 80%, respectively, of initial activity after 180 minutes of incubation at 60 ºC. The kinetic parameters Km and Vmáx were 0.476 (mg.mL-1) and 8.58 (µmol/minute) for GA and 0.082 (M) and 48.20 (µmol/minute) for GI. The maximum glucose syrups production occurred after 24 hours of reaction with a 98% yield. The production of fructose syrups with 42% (w/v) was reached after 96 hours of reaction.

scholarly journals An inducible hydrolase from Aspergillus niger, acting on carbon–carbon bonds, for phlorrhizin and other C-acylated phenols

1970 ◽  
Vol 116 (5) ◽  
pp. 889-897 ◽  
Author(s):  
T. Minamikawa ◽  
N. P. Jayasankar ◽  
B. A. Bohm ◽  
I. E. P. Taylor ◽  
G. H. N. Towers
Keyword(s):  
Aspergillus Niger ◽  
Metal Ion ◽  
Deae Cellulose ◽  
Hydrolytic Activity ◽  
Maximum Activity ◽  
Protamine Sulphate ◽  
Carbon Carbon Bonds ◽  
Alkaline Conditions ◽  
Km Value ◽  
Ammonium Sulphate Fractionation

1. An inducible enzyme catalysing the hydrolysis of phloretin to form phloroglucinol and phloretic acid has been extracted from the acetone-dried powders of the mycelial felts of an Aspergillus niger strain grown in the presence of phlorrhizin. The enzyme was partially purified by treatment with protamine sulphate, ammonium sulphate fractionation, negative adsorption on tricalcium phosphate gel, and DEAE-cellulose column chromatography. 2. The hydrolytic activity on phloretin appeared to be maximal at about pH9.6. However, the characteristics of the enzyme were studied at pH7.2, because of the lability of the product, phloroglucinol, under alkaline conditions. 3. The apparent Km value at pH7.2 was about 0.3–0.4mm for phloretin and 0.15mm for 3′-methylphloracetophenone. 4. Maximum activity of the enzyme was obtained without the addition of any cofactor or metal ion. The involvement of thiol groups in the reaction was demonstrated by the potent inhibitory action of both heavy-metal ions and p-chloromercuribenzoate. 5. The enzyme showed a rather broad substrate specificity, and some other C-acylated phenols related to phloretin were hydrolysed. It was found that 3′-methylphloracetophenone, phloracetophenone and 2′,4,4′-trihydroxydihydrochalcone were attacked more efficiently than phloretin. We propose the systematic name C-acylphenol acylhydrolase for the enzyme. This enzyme belongs to EC group 3.7.1.

THE ENZYMATIC SYNTHESIS OF CITRIC ACID BY CELL-FREE EXTRACTS OF ASPERGILLUS NIGER

1954 ◽  
Vol 32 (4) ◽  
pp. 434-439 ◽  
Author(s):  
C. V. Ramakrishnan ◽  
S. M. Martin
Keyword(s):  
Citric Acid ◽  
Calcium Phosphate ◽  
Aspergillus Niger ◽  
Ammonium Sulphate ◽  
Enzymatic Synthesis ◽  
Coenzyme A ◽  
Acetyl Coenzyme A ◽  
Acetyl Coenzyme ◽  
Ammonium Sulphate Fractionation ◽  
Condensing Enzyme

Cell-free extracts of Aspergillus niger, N.R.C. 233, have been shown to contain the enzymes necessary to catalyze the synthesis of citrate from ATP, acetate, and oxalacetate. The "condensing enzyme", which catalyzes the condensation of acetyl-coenzyme A and oxalacetate to yield citrate, has been isolated and purified approximately 50-fold by a combination of steps involving ammonium sulphate fractionation and calcium phosphate gel adsorption.

THE ENZYMATIC SYNTHESIS OF CITRIC ACID BY CELL-FREE EXTRACTS OF ASPERGILLUS NIGER

1954 ◽  
Vol 32 (1) ◽  
pp. 434-439 ◽  
Author(s):  
C. V. Ramakrishnan ◽  
S. M. Martin
Keyword(s):  
Citric Acid ◽  
Calcium Phosphate ◽  
Aspergillus Niger ◽  
Ammonium Sulphate ◽  
Enzymatic Synthesis ◽  
Coenzyme A ◽  
Acetyl Coenzyme A ◽  
Acetyl Coenzyme ◽  
Ammonium Sulphate Fractionation ◽  
Condensing Enzyme

Cell-free extracts of Aspergillus niger, N.R.C. 233, have been shown to contain the enzymes necessary to catalyze the synthesis of citrate from ATP, acetate, and oxalacetate. The "condensing enzyme", which catalyzes the condensation of acetyl-coenzyme A and oxalacetate to yield citrate, has been isolated and purified approximately 50-fold by a combination of steps involving ammonium sulphate fractionation and calcium phosphate gel adsorption.

Kinetic Study on Crude Laccase of Marasmius sp. from Solid State Fermentation

2020 ◽  
Vol 840 ◽  
pp. 131-136
Author(s):  
Hendro Risdianto ◽  
Susi Sugesty
Keyword(s):  
Solid State ◽  
Kinetic Study ◽  
Solid State Fermentation ◽  
Sulfonic Acid ◽  
Room Temperature ◽  
Maximum Activity ◽  
Cold Temperatures ◽  
Fermentation Method ◽  
Optimum Ph ◽  
Kinetics Of

Crude laccase was produced by using the fermentation method of solid state fermentation and employed fungus Marasmius sp and rice straw as support media. The kinetics of laccase was investigated by using the substrate of 2,2’-azinobis-(3-ethylbenzothiazoline-6-sulfonic acid) (ABTS). Laccase exhibits the maximum activity (Vm) of 1.45 mM/min and Michaelis-Menten (Km) constant value of 4.11 mM. The effect of pH and temperature has also been evaluated. The results showed that this enzyme had an optimum pH of 4.6 and temperature of 60 °C. Decreased stability of laccases is found to be faster when stored at room temperature than cold temperatures.

Comparative Labelling and Biokinetic Studies of 99mTc-EDTA(Sn) and 99mTc-DTPA(Sn)

1977 ◽  
Vol 16 (01) ◽  
pp. 30-35 ◽  
Author(s):  
N. Agha ◽  
R. B. R. Persson
Keyword(s):  
Complex Formation ◽  
Significant Influence ◽  
Room Temperature ◽  
Ph Value ◽  
Maximum Activity ◽  
Reduction Step ◽  
Labelling Yield ◽  
Different Temperatures ◽  
Kinetics Of

SummaryGelchromatography column scanning has been used to study the fractions of 99mTc-pertechnetate, 99mTcchelate and reduced hydrolyzed 99mTc in preparations of 99mTc-EDTA(Sn) and 99mTc-DTPA(Sn). The labelling yield of 99mTc-EDTA(Sn) chelate was as high as 90—95% when 100 μmol EDTA · H4 and 0.5 (Amol SnCl2 was incubated with 10 ml 99mTceluate for 30—60 min at room temperature. The study of the influence of the pH-value on the fraction of 99mTc-EDTA shows that pH 2.8—2.9 gave the best labelling yield. In a comparative study of the labelling kinetics of 99mTc-EDTA(Sn) and 99mTc- DTPA(Sn) at different temperatures (7, 22 and 37°C), no significant influence on the reduction step was found. The rate constant for complex formation, however, increased more rapidly with increased temperature for 99mTc-DTPA(Sn). At room temperature only a few minutes was required to achieve a high labelling yield with 99mTc-DTPA(Sn) whereas about 60 min was required for 99mTc-EDTA(Sn). Comparative biokinetic studies in rabbits showed that the maximum activity in kidneys is achieved after 12 min with 99mTc-EDTA(Sn) but already after 6 min with 99mTc-DTPA(Sn). The long-term disappearance of 99mTc-DTPA(Sn) from the kidneys is about five times faster than that for 99mTc-EDTA(Sn).

Effects of metal ions on simultaneous production of glucose oxidase and catalase by Aspergillus niger

2001 ◽  
Vol 32 (1) ◽  
pp. 16-19 ◽  
Author(s):  
J.-Z. Liu ◽  
Y.-Y. Huang ◽  
J. Liu ◽  
L.-P. Weng ◽  
L.-N. Ji
Keyword(s):  
Aspergillus Niger ◽  
Metal Ions ◽  
Glucose Oxidase ◽  
Simultaneous Production
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