Purification and Characterization of 6-Phospho-β-galactosidase from Lactobacillus gasseri JCM 1031
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概要
- 論文の詳細を見る
6-Phospho-β-galactosidase from Lactobacillus gasseri JCM 1031 was purified from lactobacilli to homogeneity, about 118-fold,with 0.5% recovery by several chromatographies. The molecular mass and isoelectric point of the purified enzyme were 58 kDa and pI 5.5, respectively. The K_m and V_<max> for o-nitrophenyl-β-D-ga-lactopyranoside-6-phosphate were 0.8 mM and 116.4 μmol/min/mg,respectively. Reducing agent, Fe^<2+> ion, and EDTA activated but PCMB, Zn^<2+>, and Hg^<2+> ions strongly inhibited the enzymatic activity.
- 社団法人日本農芸化学会の論文
- 1996-01-23
著者
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Suzuki Megumi
Department Of Applied Biological Chemistry Faculty Of Agriculture Niigata University
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SAITO Tadao
Laboratory of Animal Products Chemistry, Graduate School of Agricultural Science, Tohoku University
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Itoh Tomoyuki
Department Of Biological Mechanisms And Functions Graduate School Of Bioagricultural Sciences Nagoya
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Suzuki M
Yamagata Univ. Yamagata Jpn
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ITOH Takatoshi
Laboratory of Animal Food Science, College of Bioresource Science, Nihon University
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Itoh T
Laboratory Of Animal Food Science College Of Bioresource Science Nihon University
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Suzuki Masakatsu
Laboratory Of Animal Products Chemistry
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Itoh T
Faculty Of Agriculture Iwate University
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Itoh T
Hiroshima Univ. Higashi-hiroshima Jpn
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Saito Tadao
Laboratory Of Animal Products Chemistry Graduate School Of Agricultural Science Tohoku University
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