Norouzian Dariush, Akbarzadeh Azim, Scharer Jeno M, Moo Young Murray
Department of Chemical Engineering, University of Waterloo, Ontario, Canada.
Biotechnol Adv. 2006 Jan-Feb;24(1):80-5. doi: 10.1016/j.biotechadv.2005.06.003. Epub 2005 Aug 8.
Fungi are employed to produce industrially important glucoamylases. Most glucoamylases are glycosylated. Glycosylation enhances the enzyme stability. Glucoamylases contain both starch binding and catalytic binding domains, the former being responsible for activity on raw (insoluble) starch. Proteases may act on this domain causing the enzyme to lose its activity on insoluble starch. Optimal activity is observed at pH 4.5 to 6.5 and 50 to 70 degrees C. Glucoamylases contain up to 7 sub-sites with highly varying affinity. They can be produced by different methods including submerged, solid state and semi-solid state fermentation processes.
真菌被用于生产具有重要工业价值的糖化酶。大多数糖化酶都进行了糖基化修饰。糖基化可增强酶的稳定性。糖化酶包含淀粉结合结构域和催化结构域，前者负责对生（不溶性）淀粉的活性。蛋白酶可能作用于该结构域，导致酶失去对不溶性淀粉的活性。在pH 4.5至6.5以及50至70摄氏度下观察到最佳活性。糖化酶含有多达7个亲和力差异很大的亚位点。它们可以通过不同方法生产，包括深层发酵、固态发酵和半固态发酵工艺。
