Croux C, Paquet V, Goma G, Soucaille P
Département de Génie Biochimique et Alimentaire, UA-Centre National de la Recherche Scientifique no. 544, Institut National des Sciences Appliquées, Toulouse, France.
Appl Environ Microbiol. 1990 Dec;56(12):3634-42. doi: 10.1128/aem.56.12.3634-3642.1990.
Acidolysin an extracellular protease produced by Clostridium acetobutylicum ATCC 824 was purified to homogeneity by anion-exchange chromatography with a recovery of 91%. The enzyme was a monomeric protein with a molecular weight of 44,000 as estimated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and an acidic isoelectric point of 3.3. Acidolysin was very sensitive to metal-chelating agents and phosphoramidon and was unaffected by sulfhydryl reagents. It was shown to be a calcium- and zinc-containing protease. It exhibited optimal activity against Azocoll at pH 5 and 45 degrees C. It was stable at low pH and heat labile above 50 degrees C. It exhibited specificity toward peptide bonds formed by the amino group of hydrophobic amino acids (isoleucine, leucine, and phenylalanine) and its NH2-terminal amino acid sequence showed a high degree of similarity with that of Bacillus subtilis neutral metalloprotease A. Acidolysin is the first phosphoramidon-sensitive, acidic zinc metalloprotease reported.
酸溶素是丙酮丁醇梭菌ATCC 824产生的一种细胞外蛋白酶，通过阴离子交换色谱法纯化至同质，回收率为91%。通过十二烷基硫酸钠-聚丙烯酰胺凝胶电泳估计，该酶是一种分子量为44,000的单体蛋白，酸性等电点为3.3。酸溶素对金属螯合剂和磷酰胺素非常敏感，不受巯基试剂的影响。它被证明是一种含钙和锌的蛋白酶。它在pH 5和45℃时对偶氮酪蛋白表现出最佳活性。它在低pH下稳定，在50℃以上热不稳定。它对由疏水氨基酸（异亮氨酸、亮氨酸和苯丙氨酸）的氨基形成的肽键具有特异性，其NH2末端氨基酸序列与枯草芽孢杆菌中性金属蛋白酶A的序列高度相似。酸溶素是报道的第一种对磷酰胺素敏感的酸性锌金属蛋白酶。
