Characterization of endo-alpha-N-acetylgalactosaminidase from Bacillus sp. and syntheses of neo-oligosaccharides using its transglycosylation activity.
Characterization of endo-alpha-N-acetylgalactosaminidase from Bacillus sp. and syntheses of neo-oligosaccharides using its transglycosylation activity.
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芽孢杆菌属内切-α-N-乙酰氨基半乳糖苷酶的表征。
DOI：
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发表时间：
2000
影响因子：
3.9
通讯作者：
H. Kumagai
中科院分区：
文献类型：
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作者：
H. Ashida;K. Yamamoto;T. Murata;T. Usui;H. Kumagai
从芽孢杆菌培养液中将内切-α-N-乙酰半乳糖胺酶纯化至同质。从土壤中分离并表征。该酶的分子量估计为 110 kDa。该酶在 pH 4.0-10.0 范围内稳定，最高可达 55°C，并且在 pH 5.0 时最活跃。 The substrate specificity of the enzyme was strict for the disaccharide, galactosyl beta1, 3 N-acetyl-d-galactosamine, bound to aglycone in alpha configuration.另一方面，酶对糖苷配基结构的特异性相当宽松。该酶可以将二糖从对硝基苯基底物转移到各种受体，例如单糖、二糖和糖醇。利用糖苷内切酶的这种转糖基活性，可以合成新寡糖。
Endo-alpha-N-acetylgalactosaminidase was purified to homogeneity from the culture fluid of Bacillus sp. isolated from soil and characterized. The molecular mass of the enzyme was estimated as 110 kDa. The enzyme was stable at pH 4.0-10.0, up to 55 degrees C, and was most active at pH 5.0. The substrate specificity of the enzyme was strict for the disaccharide, galactosyl beta1, 3 N-acetyl-d-galactosamine, bound to aglycone in alpha configuration. On the other hand, the specificity of the enzyme for the aglycone structure was fairly relaxed. The enzyme could transfer the disaccharide from para-nitrophenyl substrate to various acceptors, such as monosaccharides, disaccharides, and sugar alcohols. Using this transglycosylation activity of the endoglycosidase, it may be possible to synthesize neo-oligosaccharides.
肺炎双球菌（链球菌）内切-α-N-乙酰基-D-半乳糖胺酶的转糖基化和转移反应活性。
DOI：
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发表时间：
1989
期刊：
The Journal of biological chemistry
影响因子：
--
作者：
Bardales,RM;Bhavanandan,VP
通讯作者：
Bhavanandan,VP