Purification and Characterization of beta 1,4-Glucanases from Penicillium simplicissimum H-11
نویسندگان
چکیده
منابع مشابه
Purification and Characterization of beta 1,4-Glucanases from Penicillium simplicissimum H-11
In this study, β-1, 4-endoglucanase from Penicillium simplicissimum H-11 was purified to homogeneity using ammonium sulfate followed by Sephadex G-100 chromatography. The purity of the enzyme was confirmed by HPLC and 12% SDS-PAGE, indicating a single peak with a molecular mass of 33.2 kDa. This protein had mostly α-helix structures, as confirmed by FTIR spectrometry. The optimum pH and tempera...
متن کاملProduction, purification and characterization of novel beta glucosidase from newly isolated Penicillium simplicissimum H-11 in submerged fermentation
β-Glucosidase is an important component of the cellulase complex. It not only hydrolyzes cellobiose and short-chain cellooligosaccharides to glucose, but also removes the inhibitory effect of cellobiose on the β-1, 4-endoglucanase and exoglucanase, thereby increasing the overall rate of cellulose biodegradation. β-glucosidasefrom culture supernatant of a fungus Penicillium simplicissimum was pu...
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The first dimeric catalase-peroxidase of eucaryotic origin, an intracellular hydroperoxidase from Penicillium simplicissimum which exhibited both catalase and peroxidase activities, has been isolated. The enzyme has an apparent molecular mass of about 170 kDa and is composed of two identical subunits. The purified protein has a pH optimum for catalase activity at 6.4 and for peroxidase at 5.4. ...
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A new antifungal antibiotic xanthoepocin was isolated from the culture broth of Penicillium simplicissimum IFO5762. Xanthoepocin was obtained from the culture fluid by solvent extraction and chromatographic purification. It showed antibiotic activity against Gram-positive bacteria and yeasts.
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Growth of Penicillium simplicissimum on anisyl alcohol, veratryl alcohol or 4-(methoxymethyl)phenol, is associated with the synthesis of relatively large amounts of the hydrogen peroxide producing flavoprotein vanillyl-alcohol oxidase (VAO). Immunocytochemistry revealed that the enzyme has a dual location namely in peroxisomes and in the cytosol. The C-terminus of the primary structure of VAO d...
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ژورنال
عنوان ژورنال: BioResources
سال: 2013
ISSN: 1930-2126
DOI: 10.15376/biores.8.3.3657-3671