Open AccessCharacteristics of an Intracellular Proteinase System of a Trichosporon Species Isolated from Trappist-Type Cheese
Author(s) -
Marie L. Vorbeck,
J. Frank Cone
Publication year - 1963
Publication title -
applied microbiology
Language(s) - English
Resource type - Journals
ISSN - 0003-6919
DOI - 10.1128/am.11.1.23-27.1963
Subject(s) - thermostability , chemistry , ethanol , intracellular , enzyme , chromatography , enzyme assay , ethanol precipitation , biochemistry , yield (engineering) , metallurgy , materials science
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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