Lloyd A G, Large P J, Davies M, Olavesen A H, Dodgson K S
Biochem J. 1968 Jul;108(3):393-9. doi: 10.1042/bj1080393.
The growth of the mould Trichoderma viride on a defined medium containing either potassium d-glucose 6-O-sulphate or potassium d-galactose 6-O-sulphate as sole sources of both carbon and sulphur is marked by the production of an enzyme system capable of liberating inorganic SO(4) (2-) ions from either of the sulphate esters. The enzyme is not produced when the organism is grown with glucose (or galactose) and potassium sulphate or with glucose and methionine as sole sources of carbon and sulphur. Experimental conditions are described whereby inorganic SO(4) (2-) ions liberated from potassium glucose 6-O-sulphate by the growing mould appear in the culture medium after a constant lag period of 21-24hr. The enzyme has been shown to be a simple glycosulphatase that is active towards the 6-O-sulphate esters of d-glucose and d-galactose but not towards potassium glucose 3-O-sulphate. The properties of the crude glycosulphatase show the enzyme to be appreciably different from analogous molluscan enzymes that can degrade monosaccharide sulphate esters.
绿色木霉在以D-葡萄糖6-O-硫酸盐或D-半乳糖6-O-硫酸盐作为唯一碳源和硫源的特定培养基上生长时,其显著特征是产生一种能够从这两种硫酸酯中释放无机SO₄²⁻离子的酶系统。当该生物体以葡萄糖(或半乳糖)和硫酸钾或葡萄糖和蛋氨酸作为唯一碳源和硫源生长时,不会产生这种酶。文中描述了实验条件,在此条件下,生长的霉菌从D-葡萄糖6-O-硫酸盐中释放出的无机SO₄²⁻离子在21 - 24小时的恒定延迟期后出现在培养基中。已证明该酶是一种简单的糖硫酸酯酶,对D-葡萄糖和D-半乳糖的6-O-硫酸酯有活性,但对D-葡萄糖3-O-硫酸酯无活性。粗糖硫酸酯酶的特性表明该酶与能够降解单糖硫酸酯的类似软体动物酶明显不同。