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Appl Environ Microbiol. 1963 January; 11(1): 23-27

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

The Pennsylvania State University, University Park, Pennsylvania

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.

² Present address: Department of Biochemistry, School of Medicine and Dentistry, The University of Rochester, Rochester, N.Y.

¹ Authorized for publication 25 May 1962 as paper no. 2672 in the Journal series of the Pennsylvania Agricultural Experiment Station.