De Mot R, Verachtert H
Can J Microbiol. 1986 Jan;32(1):47-51. doi: 10.1139/m86-009.
Trichosporon pullulans IGC 3488 produced extracellular alpha-amylase and glucoamylase activities when grown in batches in a medium containing corn steep liquor and soluble starch or corn starch. alpha-Amylase, unlike glucoamylase activity, was secreted biphasically. For both amylases the maximum concentration was found in stationary phase cultures. The amylolytic enzymes, previously concentrated by ammonium sulfate precipitation, were separated into a glucoamylase fraction and an alpha-amylase fraction by Ultrogel AcA 54 gel filtration. Pullulanase activity was located in the glucoamylase fraction, whereas cyclodextrinase activity was restricted to the alpha-amylase fraction. Isoamylase and alpha-glucosidase were not detected. Electrophoretic analysis showed that alpha-amylase activity was due to a single protein. Glucoamylase, however, occurred in multiple forms. The four glucoamylases and the alpha-amylase were glycoproteins.
在含有玉米浆和可溶性淀粉或玉米淀粉的培养基中分批培养时，普鲁兰短梗霉IGC 3488产生细胞外α-淀粉酶和糖化酶活性。与糖化酶活性不同，α-淀粉酶以双相方式分泌。对于这两种淀粉酶，最大浓度出现在稳定期培养物中。之前通过硫酸铵沉淀浓缩的淀粉分解酶，通过Ultrogel AcA 54凝胶过滤被分离成糖化酶部分和α-淀粉酶部分。支链淀粉酶活性位于糖化酶部分，而环糊精酶活性仅限于α-淀粉酶部分。未检测到异淀粉酶和α-葡萄糖苷酶。电泳分析表明，α-淀粉酶活性归因于一种单一蛋白质。然而，糖化酶以多种形式存在。四种糖化酶和α-淀粉酶都是糖蛋白。
