Bernardinelli S E, Bottaro Castilla H R, Waehner R S, Muse J, Fraile E R
Departamento de Tecnología Farmacéutica, Facultad de Farmacia y Bioquímica, Universidad de Buenos Aires, Argentina.
Rev Argent Microbiol. 1983;15(2):95-104.
Milk-clotting enzyme from a strain of Mucor varians Pispek selected in a previous work was obtained by solid culture followed by water extraction. Moistened wheat bran (120% water on dry bases) proved to be a good medium for the production of the milk-clotting enzyme. The production may be related to growth and 4,000 U milk-clotting activity by g of wheat bran was achieved. The milk-clotting enzyme was easily extracted with water from the cultures and could be precipitated by salting out with ammonium sulfate or by mixing with ethanol, methanol or acetone. The crude enzyme is an acid protease having optimal activity at pH: 3.0. Like calf rennet, this crude enzyme from M. varians loses activity with heat treatment. The level of lipolytic activity of the crude enzyme is similar to some commercial preparations and neither an antibiotic nor an amylase activity was demonstrated in the crude extracts.
通过前期工作筛选出的变异毛霉(Mucor varians Pispek)菌株所产的凝乳酶,是采用固体培养后水提取的方法获得的。湿麦麸(干基含水量120%)被证明是生产凝乳酶的良好培养基。该酶的产生可能与生长有关,每克麦麸可实现4000 U的凝乳活性。凝乳酶很容易从培养物中用水提取出来,并且可以通过硫酸铵盐析或与乙醇、甲醇或丙酮混合来沉淀。粗酶是一种酸性蛋白酶,在pH值为3.0时具有最佳活性。与小牛凝乳酶一样,这种来自变异毛霉的粗酶经热处理后会失去活性。粗酶的脂肪分解活性水平与一些商业制剂相似,并且在粗提取物中未检测到抗生素或淀粉酶活性。