scholarly journals Purification and properties of polyphenol oxidase from Chaetomium thermophile, a thermophilic fungus.

1986 ◽  
Vol 32 (4) ◽  
pp. 293-301 ◽  
Author(s):  
TADASHI ISHIGAMI ◽  
YUZO YAMADA
Keyword(s):  
Polyphenol Oxidase ◽  
Thermophilic Fungus ◽  
Purification And Properties

scholarly journals Characterization of polyphenol oxidase from Chaetomium thermophile, a thermophilic fungus.

1988 ◽  
Vol 34 (5) ◽  
pp. 401-407 ◽  
Author(s):  
TADASHI ISHIGAMI ◽  
YOSHITERU HIROSE ◽  
YUZO YAMADA
Keyword(s):  
Polyphenol Oxidase ◽  
Thermophilic Fungus

scholarly journals Purification and properties of Penicillium glucose 6-phosphate dehydrogenase

1972 ◽  
Vol 128 (4) ◽  
pp. 817-831 ◽  
Author(s):  
A. Anne Malcolm ◽  
M. G. Shepherd
Keyword(s):  
Molecular Weight ◽  
Thermal Inactivation ◽  
Gradient Centrifugation ◽  
Sucrose Density Gradient ◽  
Thermophilic Fungus ◽  
Sucrose Density Gradient Centrifugation ◽  
Coenzyme Specificity ◽  
Heat Stable ◽  
Purification And Properties ◽  
Glucose 6 Phosphate Dehydrogenase

1. Glucose 6-phosphate dehydrogenase was isolated and partially purified from a thermophilic fungus, Penicillium duponti, and a mesophilic fungus, Penicillium notatum. 2. The molecular weight of the P. duponti enzyme was found to be 120000±10000 by gelfiltration and sucrose-density-gradient-centrifugation techniques. No NADP+- or glucose 6-phosphate-induced change in molecular weight could be demonstrated. 3. Glucose 6-phosphate dehydrogenase from the thermophilic fungus was more heat-stable than that from the mesophile. Glucose 6-phosphate, but not NADP+, protected the enzyme from both the thermophile and the mesophile from thermal inactivation. 4. The Km values determined for glucose 6-phosphate dehydrogenase from the thermophile P. duponti were 4.3×10−5m-NADP+ and 1.6×10−4m-glucose 6-phosphate; for the enzyme from the mesophile P. notatum the values were 6.2×10−5m-NADP+ and 2.5×10−4m-glucose 6-phosphate. 5. Inhibition by NADPH was competitive with respect to both NADP+ and glucose 6-phosphate for both the P. duponti and P. notatum enzymes. The inhibition pattern indicated a rapid-equilibrium random mechanism, which may or may not involve a dead-end enzyme–NADP+–6-phosphogluconolactone complex; however, a compulsory-order mechanism that is consistent with all the results is proposed. 6. The activation energies for the P. duponti and P. notatum glucose 6-phosphate dehydrogenases were 40.2 and 41.4kJ·mol−1 (9.6 and 9.9kcal·mol−1) respectively. 7. Palmitoyl-CoA inhibited P. duponti glucose 6-phosphate dehydrogenase and gave an inhibition constant of 5×10−6m. 8. Penicillium glucose 6-phosphate dehydrogenase had a high degree of substrate and coenzyme specificity.

scholarly journals Purification and properties of the cellulases from the thermophilic fungus Thermoascus aurantiacus

1980 ◽  
Vol 191 (1) ◽  
pp. 83-94 ◽  
Author(s):  
C C Tong ◽  
A L Cole ◽  
M G Shepherd
Keyword(s):  
Culture Filtrate ◽  
Filter Paper ◽  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Thermophilic Fungus ◽  
Thermoascus Aurantiacus ◽  
Purification And Properties ◽  
Beta Glucosidase ◽  
Carbohydrate Contents

Three cellulases and a beta-glucosidase were purified from the culture filtrate of the thermophilic fungus Thermoascus aurantiacus. The isolated enzymes were all homogeneous on polyacrylamide-disc-gel electrophoresis. Data from chromatography on Bio-Gel P-60 and sodium dodecyl sulphate/polyacrylamide-gel electrophoresis indicated mol.wts. of 87000 (beta-glucosidase), 78000 (cellulase I), 49000 (cellulase II) and 34000 (cellulase III); the carbohydrate contents of the enzymes were 33.0, 5.5, 2.6 and 1.8% (w/w) respectively. Although the three purified cellulases were active towards filter paper, only cellulases I and III were active towards CM(carboxymethyl)-cellulose. Cellulase I was also active towards yeast glucan. The Km and catalytic-centre-activity values for the enzymes were as follows; 0.52 mumol/ml and 6.5 × 10(4) for beta-glucosidase on p-nitrophenyl beta-D-glucoside, 3.9 mg/ml and 6.3 for cellulase I on CM-cellulose, 1.2 mg/ml and 1.1 for cellulase I on yeast glucan, 35.5 mg/ml and 0.34 for cellulase II on filter paper, and 1.9 mg/ml and 33 for cellulase III on CM-cellulose.

Purification and Properties of Polyphenol Oxidase from Cabbage (Brassica oleracea L.)

1995 ◽  
Vol 43 (5) ◽  
pp. 1138-1142 ◽  
Author(s):  
Shuji Fujita ◽  
Nazamid bin Saari ◽  
Mitsuru Maegawa ◽  
Toshisuke Tetsuka ◽  
Nobuyuki Hayashi ◽  
...  
Keyword(s):  
Brassica Oleracea ◽  
Polyphenol Oxidase ◽  
Purification And Properties ◽  
Brassica Oleracea L
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