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- W4246131699 abstract "The thermophilic fungus Malbranchea pulchella var. sulfurea produces a single extracellular, thermostable, “serine” protease, which was originally called thermomycolase and is now called thermomycolin. While many microbial proteases have been studied in detail, only a few proteases produced by thermophilic fungi have been examined. Although subject to stringent control via catabolite repression, 2,5 quantities of protease are readily produced by submerged cultures (8–150 liters) using a relatively inexpensive growth medium of 1–2% casein and salts. A simple purification gives a high yield of homogeneous protease which can be stored as a stable ammonium sulfate precipitate. Stoichiometric inhibition with DFP 7 allows physiochemical studies of this small, globular protease to be made in the absence of significant autolysis. Thermomycolin is particularly thermostable in the presence of Ca, is an endoproteinase with a general specificity for apolar residues, and is a member of the subtilisin family of alkaline serine proteases. In this chapter the occurrence and taxonomy of the thermophilic fungus M. pulchella have been described, as has the maintenance of stock cultures. An assay of the enzyme based the principle: the most convenient assay for thermomycolin is based upon the speetrophotometric determination of the ρ-nitrophenol produced by the hydrolysis of a synthetic ester substrate, has been elaborated in the chapter." @default.
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- W4246131699 date "1976-01-01" @default.
- W4246131699 modified "2023-09-26" @default.
- W4246131699 title "[34] Thermomycolin" @default.
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- W4246131699 doi "https://doi.org/10.1016/s0076-6879(76)45037-1" @default.
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