Transglycosylation reaction of a chitinase purified from Nocardia orientalis.
Transglycosylation reaction of a chitinase purified from Nocardia orientalis.
复制标题
从东方诺卡氏菌中纯化的几丁质酶的转糖基反应。
DOI:
10.1016/0304-4165(87)90017-1
复制
发表时间:
1987
期刊:
影响因子:
--
通讯作者:
Y. Ishido
中科院分区:
文献类型:
--
作者:
T. Usui;Y. Hayashi;F. Nanjo;K. Sakai;Y. Ishido
Chitinase from the culture filtrates ofNocardia orientalisIFO 12806 was purified to apparent homogeneity by precipitation with ammonium sulfate followed by successive chromatography on CM-Sephadex and Bio-Gel P-60, and finally by affinity chromatography on a phenyl-Sepharose CL-4B column. The enzyme, which is essentially a hydrolase, also catalyzed a transglycosylation reaction on tetra-N-acetyl-chitotetraose (GlcNAc)4and penta-N-acetyl-chitopentaose (GlcNAc)5. The enzyme converted the tetrasaccharide into hexa-N-acetyl-chitohexaose (GlcNAc)6(21%) and di-N-acetyl-chitobiose (GlcNAc)2(63%) as the major products. The corresponding values for penta-N-acetyl-chitopentaose (GlcNAc)5were hepta-N-acetyl-chitoheptaose (glcNAc)723% and tri-N-acetyl-chitotriose (GlcNAc)359%. The rate of the transglycosylation depended on the temperature, the concentration of substrate and the pH.