THE PROTEOLYTIC ENZYMES OF MICROORGANISMS: IV. PARTIAL PURIFICATION AND SOME PROPERTIES OF EXTRACELLULAR PROTEASE FROM MORTIERELLA RENISPORA DIXON-STEWART
- 1 November 1952
- journal article
- research article
- Published by Canadian Science Publishing in Canadian Journal of Botany
- Vol. 30 (6) , 685-692
- https://doi.org/10.1139/b52-047
Abstract
A protease concentrate was obtained from the culture medium of Mortierella renispora Dixon-Stewart (PRL 26) by repeated precipitation with ammonium sulphate. The specific activity of the mold protease compared favorably with that of crystalline trypsin. The pH optimum was broad, with a maximum at a pH of 7.5 when hemoglobin was used as the substrate. A study of the pH stability characteristics showed that it was stable over a wide range (4.9 to 9.5) at 1 °C. and 25 °C. Ferrous ions caused a considerable increase in the activity of the enzyme preparations, other metals were ineffective as activators.This publication has 2 references indexed in Scilit:
- PROTEOLYTIC ACTIVITY OF PITUITARY EXTRACTSJournal of Biological Chemistry, 1951
- THE PROTEOLYTIC ENZYMES OF MICROORGANISMS: III. SOME CHARACTERISTICS OF EXTRACELLULAR PROTEASES PRODUCED IN SUBMERGED CULTURECanadian Journal of Research, 1950