Purification and characterization of an extracellular proteinase from Brevibacterium linens ATCC 9174

An extracellular serine proteinase from Brevibacterium linens ATCC 9174 was purified to homogeneity. pH and temperature optima were 8.5 and 50 degrees C, respectively. The results for the molecular mass of the proteinase were 56 kDa by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and 12...

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Bibliographic Details
Published in:Applied and Environmental Microbiology 1995-09, Vol.61 (9), p.3454-3456
Main Authors: Rattray, F.P. (University College, Cork, Ireland.), Bockelmann, W, Fox, P.F
Format: Article
Language:English
Subjects:
ACTIVIDAD ENZIMATICA
ACTIVITE ENZYMATIQUE
Bacteriology
Biological and medical sciences
Biology of microorganisms of confirmed or potential industrial interest
Biotechnology
BREVIBACTERIUM LINENS
Cellular biology
COMPOSICION QUIMICA
COMPOSITION CHIMIQUE
Enzymes
Fundamental and applied biological sciences. Psychology
Mission oriented research
Physiology and metabolism
PROTEASAS
PROTEASE
Proteins
PROTEOLISIS
PROTEOLYSE
PURIFICACION
PURIFICATION
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Summary:An extracellular serine proteinase from Brevibacterium linens ATCC 9174 was purified to homogeneity. pH and temperature optima were 8.5 and 50 degrees C, respectively. The results for the molecular mass of the proteinase were 56 kDa by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and 126 kDa by gel filtration, indicating that the native enzyme exists as a dimer. Mg2+ and Ca2+ activated the proteinase, as did NaCl; however, Hg2+, Fe2+, and Zn2+ caused strong inhibition. The sequence of the first 20 N-terminal amino acids H2-Ala-Lys-Asn-Asp-Ala-Val Gly-Gly-Met-Gly-Tyr-Leu-Ser-Met-Ile-Pro-Ser-Gln-pro-Gly
ISSN:0099-2240
1098-5336
DOI:10.1128/aem.61.9.3454-3456.1995