Purification and characterization of two milk-clotting enzymes from Irpex lacteus.
نویسندگان
چکیده
منابع مشابه
Milk-clotting Enzymes from Microorganisms.
A total of 230 cultures of fungi and 43 cultures of bacteria, isolated from such sources as soil, butter, and milk, were screened for their milk-clotting activity. The fungi were cultivated on semisolid media, and the bacteria were grown in milk media in shake culture. Phytic acid, added as calcium phytate, was found to stimulate production of the enzyme in most of the bacterial isolates. Prote...
متن کاملPurification and Characterization of Milk Clotting Enzyme Produced by Rhizomucor Rmiehei
Milk clotting enzyme (M CE) produced by: Rhizomucor miehei was purified and characterized.The enzyme was purified 220.29-fold with specific activity about 14444.2 U/mg protein byultrafiltration, ammonium sulfate fractionation, Sephacryl S-300 chromatography. The maximumenzyme activity was at 65°C.The milk clotting activity was decreased steadily as pH is increased and indicated maximumactivity ...
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.
متن کاملInduction, Purification and Characterization of a Novel Manganese Peroxidase from Irpex lacteus CD2 and Its Application in the Decolorization of Different Types of Dye
Manganese peroxidase (MnP) is the one of the important ligninolytic enzymes produced by lignin-degrading fungi which has the great application value in the field of environmental biotechnology. Searching for new MnP with stronger tolerance to metal ions and organic solvents is important for the maximization of potential of MnP in the biodegradation of recalcitrant xenobiotics. In this study, it...
متن کاملpurification and characterization of milk clotting enzyme produced by rhizomucor rmiehei
milk clotting enzyme (m ce) produced by: rhizomucor miehei was purified and characterized.the enzyme was purified 220.29-fold with specific activity about 14444.2 u/mg protein byultrafiltration, ammonium sulfate fractionation, sephacryl s-300 chromatography. the maximumenzyme activity was at 65°c.the milk clotting activity was decreased steadily as ph is increased and indicated maximumactivity ...
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ژورنال
عنوان ژورنال: Agricultural and Biological Chemistry
سال: 1983
ISSN: 0002-1369,1881-1280
DOI: 10.1271/bbb1961.47.551