Davidson I W, Lawson C J, Sutherland I W
J Gen Microbiol. 1977 Jan;98(1):223-9. doi: 10.1099/00221287-98-1-223.
The alginate depolymerase associated with bacteriophage infection of Azotobacter vinelandii has been used in the analysis of sodium alginate. The enzyme degraded the polysaccharide to a series of oligouronides each containing a terminal 4-deoxy-alpha-L-erythro-hex-4-enopyranuronosyl residue. Analysis of these oligouronides, together with kinetic information, indicated that the enzyme was specific for mannuronic acid-containing regions of the polyuronide. The specificity of the enzyme made it possible to determine the primary structure of the macro-molecule. The phage-induced enzyme was shown to be distinct from the alginate lyase elaborated by the host organisms by its pH optimum, molecular weight, Michaelis constant and stability.
与棕色固氮菌噬菌体感染相关的藻酸盐解聚酶已被用于分析海藻酸钠。该酶将多糖降解为一系列寡糖醛酸,每个寡糖醛酸都含有一个末端4-脱氧-α-L-赤藓糖-己-4-烯吡喃糖醛酸残基。对这些寡糖醛酸的分析以及动力学信息表明,该酶对聚糖醛酸中含甘露糖醛酸的区域具有特异性。该酶的特异性使得确定大分子的一级结构成为可能。经证明,噬菌体诱导的酶在最适pH值、分子量、米氏常数和稳定性方面与宿主生物体产生的藻酸盐裂解酶不同。