scholarly journals Purification and Characterization of Isoperoxidases Elicited by Aspergillus flavus in Cotton Ovule Cultures

1991 ◽  
Vol 95 (1) ◽  
pp. 14-20 ◽  
Author(s):  
Jay E. Mellon
Keyword(s):  
Aspergillus Flavus ◽  
Purification And Characterization ◽  
Cotton Ovule

scholarly journals Purification and Characterization of Endoglucanase from local isolate of Aspergillus flavus

2013 ◽  
Vol 10 (3) ◽  
pp. 844-853
Author(s):  
Baghdad Science Journal
Keyword(s):  
Aspergillus Flavus ◽  
Specific Activity ◽  
Gel Filtration ◽  
Temperature Stability ◽  
Exchange Chromatography ◽  
Purification And Characterization ◽  
Original Activity ◽  
A Value ◽  
Optimum Ph

Endoglucanase produced from Aspergillus flavus was purified by several steps including precipitation with 25 % ammonium sulphate followed by Ion –exchange chromatography, the obtained specific activity was 377.35 U/ mg protein, with a yield of 51.32 % .This step was followed by gel filtration chromatography (Sepharose -6B), when a value of specific activity was 400 U/ mg protein, with a yield of 48 %. Certain properties of this purified enzyme were investigated, the optimum pH of activity was 7 and the pH of its stability was 4.5, while the temperature stability was 40 °C for 60 min. The enzyme retained 100% of its original activity after incubation at 40 °C for 60 min; the optimum temperature for enzyme activity was 40 °C.

Purification and characterization of an alkaline pectin lyase from Aspergillus flavus

2008 ◽  
Vol 43 (5) ◽  
pp. 547-552 ◽  
Author(s):  
Sangeeta Yadav ◽  
Pramod Kumar Yadav ◽  
Dinesh Yadav ◽  
Kapil Deo Singh Yadav
Keyword(s):  
Aspergillus Flavus ◽  
Pectin Lyase ◽  
Purification And Characterization

DEGRADATION OF RUTIN BY ASPERGILLUS FLAVUS. PRODUCTION, PURIFICATION, AND CHARACTERIZATION OF AN ESTERASE

1963 ◽  
Vol 9 (5) ◽  
pp. 653-664 ◽  
Author(s):  
J. J. Child ◽  
F. J. Simpson ◽  
D. W. S. Westlake
Keyword(s):  
Aspergillus Flavus ◽  
Tannic Acid ◽  
Absorption Maximum ◽  
Potassium Ferricyanide ◽  
Ethyl Butyrate ◽  
Dihydroxybenzoic Acid ◽  
Purification And Characterization

Aspergillus flavus produces an inducible esterase that hydrolyzes the depside, 2-(3′,4′-dihydroxybenzoyloxy)-4,6-dihydroxybenzoic acid. The activity of this enzyme may be followed by measurement of the rate of production of protocatechnic acid, which reacts with alkaline potassium ferricyanide to give a product with an absorption maximum at 540 mμ. Synthesis of the esterase is induced when the organism is grown on rutin, robinin, hyperosid, kaempferol, rhamnetin, myricetin, quercetin, and fisetin, but not when grown on apigenin, galangin, glucose, naringenin, morin, rhamnose, robinetin, or taxifolin. The esterase has been partially purified and separated from the rutinase and quercetinase enzymes. The esterase is most active at pH 4.5. Eighty percent of the activity remained after holding the enzyme for 10 minutes at 60 °C. The enzyme readily attacked the depside linkages in tannic acid but did not hydrolyze common ester substrates such as ethyl butyrate.

scholarly journals Purification and Characterization of Lipase from Aspergillus flavus PW2961 using Magnetic Nanoparticles.

2017 ◽  
Vol 32 (1) ◽  
pp. 77 ◽  
Author(s):  
S.O. Kareem ◽  
O.S. Adebayo ◽  
S.A. Balogun ◽  
A.I. Adeogun ◽  
S.B Akinde
Keyword(s):  
Magnetic Nanoparticles ◽  
Aspergillus Flavus ◽  
Purification And Characterization

DEGRADATION OF RUTIN BY ASPERGILLUS FLAVUS. PURIFICATION AND CHARACTERIZATION OF RUTINASE

1961 ◽  
Vol 7 (6) ◽  
pp. 921-932 ◽  
Author(s):  
G. W. Hay ◽  
D. W. S. Westlake ◽  
F. J. Simpson
Keyword(s):  
Aspergillus Flavus ◽  
Partial Purification ◽  
Dihydroxybenzoic Acid ◽  
Purification And Characterization ◽  
Dihydroxyphenylacetic Acid ◽  
The Common ◽  
Hydrolysis Of

Aspergillus flavus produces an adaptive glycosidase (rutinase) that hydrolyzes rutin to quercetin and rutinose. Production of rutinase occurs when the mold is grown on the glycosides rutin, hyperosid, and naringin, and on the aglycones quercetin, kaempferol, rhamnetin, 2,4-dihydroxybenzoic acid, and 3,4-dihydroxyphenylacetic acid, but not when grown on glucose, galactose, rhamnose, or rutinose. Rutinase, after partial purification, is relatively stable when stored at −20 °C, and is most stable and most active at pH 5.6. The enzyme is quite specific, hydrolyzing the 5-glucoside of sakuranetin, the 3-rutinoside and 3-galactoside of quercetin, but not the 3-L-rhamnoside nor any of the common glycosides. The hydrolysis of rutin is carried to completion aided by the insolubility of the aglycone quercetin in water.

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