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Appl Environ Microbiol. 1986 May; 51(5): 1019-1023
Copyright © 1986, American Society for Microbiology. All Rights Reserved.

Purification and Properties of ß-N-Acetylhexosaminidase from Mucor fragilis Grown in Bovine Blood

Kenji Yamamoto*, Yasunobu Tsuji, Sawako Matsushita, Hidehiko Kumagai and Tatsurokuro Tochikura

1 Department of Food Science and Technology, Faculty of Agriculture, Kyoto University, Kyoto 606, and Institute of Soy Sauce, Higashimaru Shoyu Co. Ltd., Tatsuno, Hyogo 679-41, 2 Japan

ABSTRACT

Mucor fragilis grown on bovine blood powder as the sole carbon source abundantly produced ß-N-acetylhexosaminidase. The enzyme activity was several times higher than that of a culture obtained with glucose medium. The enzyme had two different molecular weight forms. The high-molecular-weight form had somewhat higher ß-N-acetylgalactosaminidase activity than the lower-molecular-weight enzyme which had ß-N-acetylgalactosaminidase activity equivalent to about 40% of its ß-N-acetylglucosaminidase activity. Bovine blood seemed to induce both enzymes, but N-acetylamino sugars specifically induced the low-molecular-weight form. N-Acetylgalactosamine had an especially marked effect on activity. The low-molecular-weight form of enzyme was purified from the culture filtrate by fractionation with ammonium sulfate and various column chromatographies. The purified enzyme was found to be homogeneous by polyacrylamide gel electrophoresis. The optimum pH was 4.0 to 5.0 for ß-N-acetylglucosaminidase activity and 5.5 to 6.5 for ß-N-acetylgalactosaminidase activity. The enzyme hydrolyzed natural substrates such as di-N-acetylchitobiose, tri-N-acetylchitotriose, and a glycopeptide obtained by modification of fetuin.

FOOTNOTES

* Corresponding author.

Appl Environ Microbiol. 1986 May; 51(5): 1019-1023
Copyright © 1986, American Society for Microbiology. All Rights Reserved.



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Copyright © 1986 by the American Society for Microbiology. All rights reserved.