Selvakumar P, Ashakumary L, Helen A, Pandey A
Biotechnology Unit, Regional Research Laboratory, Council of Scientific and Industrial Research, Trivandrum, India.
Lett Appl Microbiol. 1996 Dec;23(6):403-6. doi: 10.1111/j.1472-765x.1996.tb01346.x.
Glucoamylases produced by Aspergillus niger grown on wheat brain in solid cultures were purified. Four different forms, GA I, GA I', GA II and GA III, were found having apparent molecular weights of 112,000, 104,000, and 74,000 and 61,000 Da respectively. The enzymes are glycoproteins with a carbohydrate content of 16%, and optimal activity at 60 degrees C and pH 4.4. Activity was strongly inhibited by Hg2+ while Mn2+ and Fe2+ were stimulatory. The Km values for the degradation of starch and maltose were 3.5 and 7.8 mg ml-1, respectively.
对黑曲霉在固体培养的小麦麸皮上生长所产生的糖化酶进行了纯化。发现了四种不同形式,即GA I、GA I'、GA II和GA III,其表观分子量分别为112,000、104,000、74,000和61,000道尔顿。这些酶是糖蛋白,碳水化合物含量为16%,在60摄氏度和pH 4.4时具有最佳活性。Hg2+强烈抑制其活性,而Mn2+和Fe2+具有刺激作用。淀粉和麦芽糖降解的Km值分别为3.5和7.8毫克/毫升。