Production, purification and characterization of HYI, an antiyeast substance, produced by Hansenula saturnus.
نویسندگان
چکیده
منابع مشابه
Purification 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 کاملCharacterization of an autostimulatory substance produced by Escherichia coli.
The recovery of dilute populations of stationary phase cells of Escherichia coli was studied using an automatic growth analyser. The addition of 30% supernatant from 2-d-old stationary phase cells of the organism reproducibly shortened the apparent lag times by 22-57.5%, depending on the age of the inoculum. True lag times, as determined by colony counts, of stationary phase cells were reduced ...
متن کاملPurification and characterization of a hemolysin produced by Vibrio cholerae biotype El Tor: another toxic substance produced by cholera vibrios.
A thermolabile direct hemolysin from an El Tor cholera vibrio strain has been isolated and partially characterized as a simple protein of ca. 20,000 molecular weight. In addition to its hemolytic activity, the hemolysin is cytotoxic, cardiotoxic, and rapidly lethal. In these respects it resembles the thermostable direct hemolysin/cytotoxin/cardiotoxin/lethal toxin of Vibrio parahaemolyticus and...
متن کاملAffinity Purification and Characterization of Recombinant Bacillus sphaericus Phenylalanine Dehydrogenase Produced by pET Expression Vector System
Cloning and expression of the L-phenylalanine dehydrogenase gene, from B. sphaericus in E. coli were done. The gene was cloned in the vector pET16b and transformed into E. coli BL21 (DE3). The functional form of the L-phenylalanine dehydrogenase enzyme was purified by affinity purification techniques, taking advantage of the ability of this enzyme to bind to the nucleotide site affinity dye, Re...
متن کاملPURIFICATION AND PROPERTIES OF AN EXTRACELLULAR PROTEASE PRODUCED BY PENICIUIUM EXPANSUM
Penicilliurn expamum grown in a medium with rice husk as a carbon source produced an extracellular protease. The protease enzyme was isolated from culture broth by fractionation with acetone and column chromatography on Sephadex G- 100 and DEAE A-50. The protease enzyme was purified about 17.47 fold, with a recovery of 14%. The purified protease was homogenous on SDS polyacrylarnide disc ge...
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: Agricultural and Biological Chemistry
سال: 1984
ISSN: 0002-1369,1881-1280
DOI: 10.1271/bbb1961.48.903