Purification and properties of an endo-(1→4)-β-d-xylanase from irpex lacteus (Polyporus tulipiferae)
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چکیده
منابع مشابه
Identification of an endo-beta-1,4-D-xylanase from Magnaporthe grisea by gene knockout analysis, purification, and heterologous expression.
Magnaporthe grisea, a destructive ascomycetous pathogen of rice, secretes cell wall-degrading enzymes into a culture medium containing purified rice cell walls as the sole carbon source. From M. grisea grown under the culture conditions described here, we have identified an expressed sequenced tag, XYL-6, a gene that is also expressed in M. grisea-infected rice leaves 24 h postinoculation with ...
متن کاملBiodegradation of 2,4,6-Trinitrotoluene by White-Rot Fungus Irpex lacteus
White-rot fungus Irpex lacteus degraded TNT significantly in proportion to the culture time. After 48 h incubation, about 95% of TNT was degraded. Two reduced metabolites were identified as 4-amino-2,6-dinitrotoluene (4-ADNT) and 2-amino-4,6-dinitrotoluene (2-ADNT) which was further degraded.
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Objective(s): Although bacteria and molds are the pioneering microorganisms for production of many enzymes, yet yeasts provide safe and reliable sources of enzymes with applications in food and feed. Materials and Methods: Single xylanase producer yeast was isolated from plant residues based on formation of transparent halo zones on xylan agar plates. The isolate showed much ...
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An extracellular xylanase produced by a cellulase-negative mutant strain of Streptomyces lividans 1326 was purified to homogeneity. The purified enzyme has an apparent Mr of 43,000 and pI of 5.2. The pH and temperature optima for the activity were 6.0 and 60 degrees C respectively, and the Km and Vmax. values, determined with a soluble oat spelts xylan, were 0.78 mg/ml and 0.85 mmol/min per mg ...
متن کاملPurification and Properties of an Endo-P-iv-acetylglucosaminidase
An enzyme that hydrolyzes di-N-acetylchitobiose linkages in oligosaccharides and glycoproteins was purified to homogeneity from cultural filtrates of Streptomyces griseus. The molecular weight of the enzyme, determined by sedimentation equilibrium analysis, is 27,200 f ZOO, and it appears to consist of a single polypeptide chain. This apparent endo/3-N-acetylglucosaminidase was completely stabl...
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ژورنال
عنوان ژورنال: Carbohydrate Research
سال: 1984
ISSN: 0008-6215
DOI: 10.1016/0008-6215(84)85092-2