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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Veröffentlicht in:	Applied and Environmental Microbiology 1995-09, Vol.61 (9), p.3454-3456
Hauptverfasser:	Rattray, F.P. (University College, Cork, Ireland.), Bockelmann, W, Fox, P.F
Format:	Artikel
Sprache:	eng
Schlagworte:	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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Zusammenfassung:	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