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多粘芽孢杆菌的果胶酸裂解酶

Pectic acid lyases of Bacillus polymyxa.

作者信息

Nagel C W, Wilson T M

出版信息

Appl Microbiol. 1970 Sep;20(3):374-83. doi: 10.1128/am.20.3.374-383.1970.

Abstract

Four enzymes were separated from an extracellular preparation of Bacillus polymyxa by carboxymethylcellulose column chromatography. The pH optima were 8.3 to 8.5, 8.7 to 8.9, 9.2 to 9.4, and 9.5 to 9.6. All of the enzymes required calcium ion for maximum activity, whereas strontium ion was only partially effective in stimulating activity. Cobalt was the only other cation tested which was effective in two of the enzymes. The lyases seem to attack a calcium salt-bridged substrate. K(m) and V(m) data of the four enzymes on various oligomers are presented as well as paper chromatographic evidence of preferred sites of attack. All of the enzymes are endo-enzymes which, based upon their characteristics, were classed into two types.

摘要

通过羧甲基纤维素柱色谱法从多粘芽孢杆菌的细胞外制剂中分离出四种酶。最适pH值分别为8.3至8.5、8.7至8.9、9.2至9.4和9.5至9.6。所有这些酶都需要钙离子来达到最大活性,而锶离子仅部分有效地刺激活性。钴是所测试的唯一对其中两种酶有效的其他阳离子。这些裂解酶似乎作用于钙盐桥连的底物。给出了这四种酶对各种寡聚物的米氏常数(K(m))和最大反应速度(V(m))数据,以及优先作用位点的纸色谱证据。所有这些酶都是内切酶,根据其特性可分为两种类型。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/e030/376943/1127f90eb382/applmicro00107-0110-a.jpg

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