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. 1963 Jan;11(1):23-7.
doi: 10.1128/am.11.1.23-27.1963.

Characteristics of an intracellullar proteinase system of a Trichosporon species isolated from Trappist-type cheese

M L VORBECK, J F CONE

Characteristics of an intracellullar proteinase system of a Trichosporon species isolated from Trappist-type cheese

M L VORBECK et al. Appl Microbiol. 1963 Jan.

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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References

    1. J Bacteriol. 1954 Apr;67(4):503-4 - PubMed
    1. J Biol Chem. 1956 Aug;221(2):919-30 - PubMed

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