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. 1975 Nov;30(5):738–745. doi: 10.1128/am.30.5.738-745.1975

Purification and Properties of Intracellular Proteinase from Streptococcus cremoris

Kunio Ohmiya 1, Yasushi Sato 1
PMCID: PMC187264  PMID: 16350038

Abstract

Proteolytic activity in the extract from the cells of Streptococcus cremoris increased in the presence of casein, lactose, glucose, and CaCl2 in the media but was negligibly detectable in the extract of the cells harvested from the culture containing succinate or citrate. The intracellular proteinase from S. cremoris harvested from tomato medium was purified 150-fold in this experiment. The enzyme had a molecular weight of 140,000, optimum pH at 6.5 to 7.0, and maximum activity at 30 C. The proteinase was activated by Ca2+ and inhibited by Zn2+, Cu2+, Hg2+, Fe2+, ethylenediaminetetraacetate, and sodium lauryl sulfate. The Km value of the enzyme towards each casein fraction was almost the same, and the Vmax of the enzyme towards αs-casein was smaller than those towards the other casein fractions.

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Selected References

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

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