Abstract
1. Of four proteolytic enzymes isolated from autolysing Saccharomyces carlsbergensis, one is inactivated at about 45 degrees C, whereas the others are stable at 50 degrees C. pH optima for activity are from 3.0 to 8.0 but maximum stability is between pH6.0 and 6.5. All appear to be glycoproteins, the carbohydrate moiety containing glucose and mannose residues. 2. Lysed protoplasts of the same yeast release four proteolytic enzymes each of which have two pH optima at pH3.0 and 7.0 approximately. Compared with the enzymes from autolysed yeast, resistance to high temperature is much less, and they are not glycoprotein in nature. 3. The same yeast grown with N-acetyltyrosine ethyl ester as nitrogen source secretes into the medium four proteases believed to be glycoprotein in nature. Generally they resemble the enzymes from lysed protoplasts more than those from autolysing yeast.
MeSH Terms
Autolysis
Caseins/metabolism
Chromatography, DEAE-Cellulose
Electrophoresis
Glucose/metabolism
Glycoproteins/analysis
Hydrogen-Ion Concentration
Mannose/metabolism
Nitrogen/metabolism
Peptide Hydrolases/analysis
Saccharomyces/enzymology,metabolism
Temperature
Chemicals
Caseins
Glycoproteins
Peptide Hydrolases
Glucose
Nitrogen
Mannose
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Maddox I S
Hough J S
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