一种细菌异淀粉酶的部分纯化及性质
Partial purification and properties of a bacterial isoamylase.
作者信息
Evans R M, Manners D J, Stark J R
出版信息
Carbohydr Res. 1979 Nov;76:203-13. doi: 10.1016/0008-6215(79)80019-1.
PMID:526954
Abstract
Isoamylase has been prepared by affinity chromatography of a commercial enzyme-preparation from a strain of Cytophaga (also known as a Flavobacterium or Polyangium). The enzyme was not very stable, but the stability could be improved by calcium ions. The enzyme had a very low but significant activity on pullulan and on alpha-dextrins having maltosyl side-chains. This observation, which is contrary to previous reports, has been related to the specificity of isoamylase and other bacterial debranching-enzymes.
摘要
异淀粉酶是通过对一株噬纤维菌（也称为黄杆菌或多囊粘菌）的商业酶制剂进行亲和层析制备的。该酶不太稳定，但钙离子可提高其稳定性。该酶对支链淀粉和具有麦芽糖浆侧链的α-糊精具有非常低但显著的活性。这一与先前报道相反的观察结果与异淀粉酶和其他细菌脱支酶的特异性有关。
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