Screening for the novel glycanase using fish mucus glycoprotein

0-聚糖酶是能够从0-聚糖如粘蛋白释放整个糖链的酶。 然而，由于已报道的酶仅作用于特定的结构，因此需要能够更普遍地从O-聚糖中释放糖链的酶。 本研究从鱼类粘液中分离得到具有新型糖链结构的O-聚糖，并以此为底物筛选O-聚糖酶产生菌。 我们测试了500多个样品，如土壤，环境水和鱼粘液，但我们无法检测到目标酶的活性。 然而，在聚糖的非还原末端经常观察到KDN的释放。 鱼粘液中含有的KDN O-聚糖被认为是环境微生物的保护屏障。

O-Glycanase is an enzyme which is capable of releasing entire sugar chains from O-glycan such as mucin. However, since the enzymes which were reported to data act only specific structures, those which could liberate sugar chains from O-glycans more universally are required. In this study, we isolated O-glycan from fish mucus with novel sugar chain structures, and used the O-glycan as the substrate for screening the O-glycanase-producing bacterium. We tested over 500 samples such as soil, environmental water, and fish mucus, but we could not detect the activity of the target enzyme. However, release of KDN at the non-reduing end of the glycan observed very often. KDN-containing O-glycan in the fish mucus is thought to be a protective barrier from the environmental microbes.