Bakhmatova I V, Bal'sis A B, Chiurlis T K, Glemzha A A, Ianulaĭtene K K
Prikl Biokhim Mikrobiol. 1984 Nov-Dec;20(6):804-9.
Extracellular alpha-amylases were isolated from the culture medium filtrates of Bacillus subtilis R-623 morphological variants R, P and S by means of biospecific chromatography on artificial sorbents and then purified to homogeneity. Some properties of purified alpha-amylases were being studied. The molecular weight of alpha-amylases from Bacillus subtilis variants R, P and S equals 57,000, 58,000 and 56,000, and the isoelectric points are at pH 5.4, 5.6 and 5.1, respectively. pH optimum for alpha-amylase from variants R and P is 4.5, and for that from variant S--5.0. alpha-Amylases from Bacillus subtilis R-623 morphological variants are thermostable enzymes. According to the properties studied, they correspond to Bacillus subtilis alpha-amylases that were isolated and described by other researchers.
通过在人工吸附剂上进行生物特异性色谱法，从枯草芽孢杆菌R - 623形态变体R、P和S的培养基滤液中分离出细胞外α -淀粉酶，然后将其纯化至同质。对纯化后的α -淀粉酶的一些性质进行了研究。枯草芽孢杆菌变体R、P和S的α -淀粉酶分子量分别为57,000、58,000和56,000，其等电点分别为pH 5.4、5.6和5.1。变体R和P的α -淀粉酶的最适pH为4.5，变体S的为5.0。枯草芽孢杆菌R - 623形态变体的α -淀粉酶是热稳定酶。根据所研究的性质，它们与其他研究人员分离和描述的枯草芽孢杆菌α -淀粉酶相对应。
