Degradation of Casein by Crystalline Low-Temperature-Active Proteinase from Streptococcus lactis
نویسندگان
چکیده
منابع مشابه
Extracellular Proteinase of Streptococcus Lactis.
Williamson, W. T. (North Carolina State of the University of North Carolina, Raleigh), S. B. Tove, and M. L. Speck. Extracellular proteinase of Streptococcus lactis. J. Bacteriol. 87:49-53. 1964.-Streptococcus lactis was shown to produce an extracellular proteolytic enzyme(s). A 120-fold purification of the proteinase was obtained from the cell-free culture medium by ammonium sulfate fractionat...
متن کاملLOW TEMPERATURE MOLTEN SALT SYNTHESIS OF NANO CRYSTALLINE MgAl2O4 POWDER
Abstract: composition of MgO and nano boehmite. The reactant and potassium chloride, as the reaction media, were fired at800-1000 °C at different dwell times (0.5-5 h) in the ambient atmosphere. After washing and filtration, the spinel nanopowder was characterized by X-ray diffraction (XRD), Scanning electron microscopy (SEM), and Brunauer-Emmett-Teller (BET) techniques. It was demonstrated tha...
متن کاملApplication of Asian pumpkin (Cucurbita ficifolia) serine proteinase for production of biologically active peptides from casein.
The main objective of this study was to determine potential application of a serine proteinase derived from Asian pumpkin for obtaining biologically active peptides from casein. The course of casein hydrolysis by three doses of the enzyme (50, 150, 300 U/mg of protein) was monitored for 24 hours by the determinations of: hydrolysis degree DH (%), free amino group content (μmole Gly/g), RP HPLC ...
متن کاملPartial Isolation and Degradation of Caseins by Cell Wall Proteinase(s) of Streptococcus cremoris HP.
The cell wall proteinase fraction of Streptococcus cremoris HP has been isolated. This preparation did not exhibit any activity due to either specific peptidases known to be located near the outside surface of and in the membrane or intracellular proteolytic enzymes. By using thin-layer chromatography for the detection of relatively small hydrolysis products which remain soluble at pH 4.6, it w...
متن کاملMechanism of Proteinase Release from Lactococcus lactis subsp. cremoris Wg2.
The procedure generally used for the isolation of extracellular, cell-associated proteinases of Lactococcus lactis species is based on the release of the proteinases by repeated incubation and washing of the cells in a Ca-free buffer. For L. lactis subsp. cremoris Wg2, as many as five incubations for 30 min at 29 degrees C are needed in order to liberate 95% of the proteinase. Proteinase releas...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Nihon Chikusan Gakkaiho
سال: 1985
ISSN: 1346-907X,1880-8255
DOI: 10.2508/chikusan.56.56