Schalinatus E, Behnke U, Ruttloff H
Nahrung. 1983;27(4):371-7. doi: 10.1002/food.19830270409.
The investigation concerning the localization of proteolytically active enzymes in the cells of Thermoactinomyces vulgaris show that the enzymes are present in a dissolved form in the cellular extract (75%) as well as linked to the solid cell components (25%). The ratio of the activities of the soluble periplasmatical fraction to the soluble cytoplasmatical fraction to the insoluble cytoplasmatical membrane fraction was found to be 2:1:1. The formation of the proteins during the cultivation is measured by detecting the activity in the cellular extract. As soon as enough of biomass is present (weighable) in the medium, the protease activity can be detected in the cellular extract. It increases during the fermentation and amounts to 1 to 2% of the activity of the proteases in the medium between the 10th and the 24th hour. A correlation between the formation of biomass and enzymes does not exist.
对普通嗜热放线菌细胞中蛋白水解活性酶定位的研究表明，这些酶以溶解形式存在于细胞提取物中（75%），也与固体细胞成分相连（25%）。发现可溶性周质部分、可溶性细胞质部分与不溶性细胞质膜部分的活性比为2:1:1。通过检测细胞提取物中的活性来测定培养过程中蛋白质的形成。一旦培养基中存在足够量（可称重）的生物量，就可以在细胞提取物中检测到蛋白酶活性。它在发酵过程中增加，在第10小时到第24小时之间相当于培养基中蛋白酶活性的1%到2%。生物量的形成与酶之间不存在相关性。
