Department of Botany and Plant Pathology, Oregon State University, Corvallis, Oregon 97331-2902.
Appl Environ Microbiol. 1984 Apr;47(4):699-703. doi: 10.1128/aem.47.4.699-703.1984.
Alginate lyases (EC 4.2.2.3) from two marine bacteria were isolated and partially characterized. A cell-bound lyase from isolate A3 had a molecular weight of approximately 100,000 and cleaved mannuronate blocks, apparently in an exo manner. A lyase recovered from the culture medium of isolate W3 was soluble in saturated ammonium sulfate, cleaved guluronate blocks, apparently in an endo manner, and had a molecular weight of 35,000. The thiobarbiturate test and urea-polyacrylamide gel electrophoresis were used to determine substrate specificity and mode of substrate cleavage by the enzymes.
从两种海洋细菌中分离并部分鉴定了海藻酸盐裂解酶(EC 4.2.2.3)。 分离株 A3 的细胞结合裂解酶的分子量约为 100,000,可明显以外向方式切割甘露糖醛酸块。 从分离株 W3 的培养液中回收的裂解酶可溶于饱和硫酸铵,可明显以内向方式切割古洛糖醛酸块,分子量为 35,000。 硫代巴比妥酸试验和脲-聚丙烯酰胺凝胶电泳用于确定酶的底物特异性和底物切割方式。