Altmann F, März L, Stirm S, Unger F M
FEBS Lett. 1987 Aug 31;221(1):145-9. doi: 10.1016/0014-5793(87)80369-1.
Two bacteriophages degrading 3-deoxy-D-manno-2-octulosonic acid-(KDO)-containing capsules of Escherichia coli strains were identified. Using modifications of the thiobarbituric acid assay, it was shown that each phage contains a glycan hydrolase activity cleaving one type of ketosidic linkage of KDO. Thus, the enzyme from phage phi 95 catalyzes the hydrolysis of beta-octulofuranosidonic linkages of the K95 glycan; and phi 1092, the alpha-octulopyranosidonic linkages of the K? antigen of E. coli LP1092. No cross-reactivity of the phage enzymes with other KDO-containing capsular polysaccharides was observed.
鉴定出两种可降解大肠杆菌菌株中含3-脱氧-D-甘露糖-2-辛酮糖酸（KDO）荚膜的噬菌体。通过对硫代巴比妥酸测定法进行改进，结果表明每种噬菌体都含有一种聚糖水解酶活性，可切割KDO的一种酮糖苷键。因此，来自噬菌体phi 95的酶催化K95聚糖的β-辛酮呋喃糖苷键的水解；而噬菌体phi 1092的酶则催化大肠杆菌LP1092的K?抗原的α-辛酮吡喃糖苷键的水解。未观察到噬菌体酶与其他含KDO的荚膜多糖有交叉反应。
