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. 1963 Jan;11(1):23–27. doi: 10.1128/am.11.1.23-27.1963

Characteristics of an Intracellular Proteinase System of a Trichosporon Species Isolated from Trappist-Type Cheese1

Marie L Vorbeck 1,2, J Frank Cone 1
PMCID: PMC1057930  PMID: 13997895

Abstract

A greater yield of the active principle was obtained when the cells were allowed to autolyze than when mechanical methods of cell disruption were used. A marked increase in activity was obtained when the crude cell extracts were held for 18 hr at 25 C after acidification to pH 5.0. The activated enzyme was partially purified by precipitation with 95% ethanol. This partially purified extract was most active at pH 5.8, and showed activity over a temperature range of 10 to 42 C. Its rate of activity was markedly decreased by sulfhydryl-binding agents. It exhibited its greatest degree of thermostability at pH 5.0.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. LAMANNA C., MALLETTE M. F. Use of glass beads for the mechanical rupture of microorganisms in concentrated suspensions. J Bacteriol. 1954 Apr;67(4):503–504. doi: 10.1128/jb.67.4.503-504.1954. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. LENNEY J. F. A study of two yeast proteinases. J Biol Chem. 1956 Aug;221(2):919–930. [PubMed] [Google Scholar]

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