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J. Biochem, 1976, Vol. 80, No. 1 9-17
© 1976 Japanese Biochemical Society

research-article

Purification and Characterization of ß-N-Acetylhexosaminidases and ß-Galactosidase from Streptococcus 6646K1

Takao KIYOHARA*, Tadao TERAO*, Kohei SHIOIRI-NAKANO**,2 and Toshiaki OSAWA*

*Faculty of Pharmaceutical Sciences, University of Tokyo Bunkyo-ku, Tokyo 113
**Institute of Medical Science, University of Tokyo Minato-ku, Tokyo 108

Three ß-N-acetylhexosaminidases [EC 3. 2. 1. 52] and one ß-galactosidase [EC 3. 2. 1. 23] were purified from the culture filtrate of Streptococcus 6646 group K by a combination of column chromatographies on p-aminophenyl ß-D-thiogalactopyranoside-substituted Sepharose and N-(p-aminophenyl)oxamic acid-substituted Sepharose.

These ß-N-acetylhexosaminidases showed optimal activities between pH 5.0 and 5.5 and could hydrolyze synthetic and glycopeptidic substrates. Glycolipids such as GM2, asialo-GM2, and globoside I were not susceptible to these ß-hexosaminidases.

ß-Galactosidase, which was purified more than 11,000-fold, had a substrate specificity rather similar to that of ß-galactosidase from E. coli. This enzyme was inhibited by EDTA and activated by Mn2+, Ca2+, and Mg2+.

Problems pertinent to the application of affinity chromatography to the purification of glycosidases are also discussed.

1 This investigation was supported in part by a research grant from the Ministry of Education, Science and Culture, of Japan.

2 Present address: Jichi Medical School, Minamikawachimachi, Tochigi 392–04.


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