Purification and Characterization of an Extracellular Proteinase from Brevibacterium-Linens ATCC-9174

Research output: Other contribution › Research

  • F P Rattray
  • W Bockelmann
  • P F Fox
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 was NH2-Ala-Lys- Asn-Asp-Ala-Val-Gly-Gly-Met-Gly-Tyr-Leu-Ser-Met-IIe-Pro-Ser-Gln- Pro-Gly
Original languageEnglish
Publication date1995
VolumeVol 61
Number of pages3
Publication statusPublished - 1995

    Research areas

  • ACID, ACIDS, AMINO-ACID, AMINO-ACIDS, Amino Acid, Amino Acids, Brevibacterium, CHEESE, Characterization, ENZYME, Electrophoresis, Extracellular Proteinase, GEL-ELECTROPHORESIS, Gel, INHIBITION, KDA, Molecular, PROTEINASE, PURIFICATION, SEQUENCE, SERINE PROTEINASE, Serine, Temperature, Zn2+

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