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Intracellular Proteases of Bacillus stearothermophilus

机译:嗜热脂肪芽孢杆菌的细胞内蛋白酶

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Cell-free extracts of Bacillus stearothermophilus have been shown to exhibit proteolytic activity toward casein as well as specific activity to catalyze the hydrolysis of furylacryloylglycyl-l-leucine amide, furylacryloylglycine, and carbobenzoxyl-glycine-p-nitrophenyl ester, indicating the presence of a neutral proteinase, a carboxypeptidase-like enzyme, and an alkaline proteinase. The neutral proteinase and carboxypeptidase-like activities were separated by gel filtration over Bio-Gel P-60, and both were reversibly inhibited by 1, 10-phenanthroline. The esterase activity was inhibited by diisopropylfluorophosphate, which did not affect other enzymatic activities and was insensitive to 1, 10-phenanthroline and ethylenediaminetetra-acetic acid.
机译:嗜热脂肪芽孢杆菌的无细胞提取物已显示出对酪蛋白的蛋白水解活性以及催化呋喃基丙烯酰基甘氨酰基-1-亮氨酸酰胺,呋喃基丙烯酰基甘氨酸和羧苯甲酰基甘氨酸-甘氨酸对硝基苯酯水解的比活性。中性蛋白酶,羧肽酶样酶和碱性蛋白酶。通过Bio-Gel P-60凝胶过滤分离中性蛋白酶和羧肽酶样活性,并且它们均被1、10-菲咯啉可逆地抑制。酯酶活性被氟磷酸二异丙酯抑制,该酯不影响其他酶活性,并且对1,10-菲咯啉和乙二胺四乙酸不敏感。

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