Intrazelluläre Proteasen aus Thermoactinomyces vulgaris 2. Mitt. Biochemische Charakterisierung der Proteasen des Zellextraktes

Abstract

The intracellular proteases (IP) of the cellular extract of Thermoactinomyces vulgaris are characterized as to the biochemical properties compared with the corresponding extracellular proteases (EP). According to that, the storage stability and the temperature and pH behaviour (optimum, stability) of both of the proteases are identical. Nevertheless, differences were detected between IP and EP after the action of several effectors and different substrates. As could be seen after a column chromatographic separation of the IP of the cellular extract, it is composed of at least 3 proteases, two of them are serine proteases which can be inhibited moreover unspecifically by p-chloromercuri benzoate. The purified proteases (IP) are very instable and therefore not yet characterized in detail.

Thermoflavimicrobium dichotomicum as a novel thermoalkaliphile for production of environmental and industrial enzymes

“…Thermostable enzymes could catalyze important chemical reactions in several industrial and research fields including food, agricultural, pharmaceutical, cosmetic, as well as several other vital economic aspects [35]. Extremophilic actinomyces species could be a source of thermostable enzymes, which are not only heat resistant, but also stable under highly alkaline conditions [36,37]. It has been reported before that Thermoflavimicrobium dichotomicum genus could produce several vital thermostable enzymes such as lipase and proteinase [38], these facts drove us to explore the ability of the isolated novel Thermoflavimicrobium dichotomicum to produce lipase, amylase, cellulase, pectinase and proteinase enzymes.…”

Identification and characterization of a novel spore-associated subtilase from Thermoactinomyces sp. CDF

“…In addition, intracellular alkaline proteases have been described for Thermoactinomyces sp. HS682 (Tsuchiya et al, 1997) and T. vulgaris (Schalinatus et al, 1983b). Besides the proteases that are present in soluble forms, minor proteases have also been found to be linked to the cytoplasmic membrane of T. vulgaris (Schalinatus et al, 1983a).…”