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PMID: 5451908 Published · ppublish English Journal Article

Proteolytic enzymes of Saccharomyces carlsbergensis.

The Biochemical journal ·Vol. 117 ·No. 5 ·1970-05-00 ·Pages 843-52

Maddox IS, Hough JS

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
References (13)
13 references, click to expand
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Article Info
Journal
The Biochemical journal
Abbr.
Biochem J
ISSN
0264-6021
Published
1970-05-00
Pages
843-52
Language
English
Region
England
NLM ID
2984726R
PMCID
PMC1179043
Subset
IM
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