Taniguchi H, Fujimura S, Takeuchi K, Nakamura T
Appl Environ Microbiol. 1983 Dec;46(6):1252-7. doi: 10.1128/aem.46.6.1252-1257.1983.
A mucopolysaccharidase in the cell extract of an oral strain of Bacteroides sp. was purified to homogeneity by ammonium sulfate precipitation, DEAE-cellulose column chromatography, gel filtration on Sephadex G-200, and isoelectric focusing. Specific activity increased 110-fold and recovery was 2%. The molecular weight was determined to be 89,000 by gel filtration, and the isoelectric point was 7.0. The optimum pH for the activity was 6.5. The enzyme was inactivated by heating at 60 degrees C for 5 min. The purified mucopolysaccharidase degraded hyaluronic acid more rapidly than chondroitin and chondroitin sulfate A and C. However, it had no activity against chondroitin sulfate B, heparin, and heparan sulfate. Since unsaturated disaccharides were derived from the enzyme substrate, this enzyme was considered to be a mucopolysaccharide lyase.
通过硫酸铵沉淀、DEAE - 纤维素柱层析、Sephadex G - 200凝胶过滤和等电聚焦，将一株口腔拟杆菌属菌株细胞提取物中的一种粘多糖酶纯化至同质。比活性提高了110倍，回收率为2%。通过凝胶过滤测定分子量为89,000，等电点为7.0。该酶活性的最适pH为6.5。该酶在60℃加热5分钟会失活。纯化的粘多糖酶降解透明质酸的速度比软骨素以及硫酸软骨素A和C更快。然而，它对硫酸软骨素B、肝素和硫酸乙酰肝素没有活性。由于不饱和二糖源自酶底物，因此该酶被认为是一种粘多糖裂解酶。
