-transparent.png){kind=logo}
Three β-N-acetylglucosaminidases, GlcNAcase A, B, and C, were purified from the culture fluid of Lactobacillus casei ATCC 27092, and the molecular weights of these enzymes were estimated to be 54,000, 51,000, and 44,000, respectively, by SDS-PAGE. The production of these GlcNAcases was accelerated by the addition of N-acetylglucosamine to the culture. These enzymes had pIs of about 5.2, an optimum pH of 5.0-5.5, and an optimum temperature of 37-40°C. The K m values of GlcNAcase A, B, and C for p-nitrophenyl-β-N-acetylglucosamine were 0.85, 1.30, and 1.04 mM and those for p-nitrophenyl-β-N-acetylgalactosamine were 39.6, 57.7, and 60.8 mM, respectively.
| UI | MeSH Term | Description | Entries |
|---|
Related Publications
M Senba, and
N Kashige, and
F Miake, and
K Watanabe
April 1985,
Chemical & pharmaceutical bulletin,
M Senba, and
N Kashige, and
F Miake, and
K Watanabe
January 2018,
Applied microbiology and biotechnology,
M Senba, and
N Kashige, and
F Miake, and
K Watanabe
March 1984,
The Journal of biological chemistry,
M Senba, and
N Kashige, and
F Miake, and
K Watanabe
January 1963,
Biochemische Zeitschrift,
M Senba, and
N Kashige, and
F Miake, and
K Watanabe
February 1972,
Biochimica et biophysica acta,
M Senba, and
N Kashige, and
F Miake, and
K Watanabe
January 1996,
International journal of systematic bacteriology,
M Senba, and
N Kashige, and
F Miake, and
K Watanabe
August 1976,
European journal of biochemistry,
M Senba, and
N Kashige, and
F Miake, and
K Watanabe
October 1983,
The Journal of biological chemistry,
M Senba, and
N Kashige, and
F Miake, and
K Watanabe
August 2003,
Journal of dairy science,
M Senba, and
N Kashige, and
F Miake, and
K Watanabe
June 1977,
The Journal of biological chemistry,
