Production, Purification, and Properties of a Pectin Lyase from Pseudomonas marginalis N6301

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概要

• 論文の詳細を見る

• Pseudomonas marginalis N6301 produced pectin lyase (EC 4. 2. 2. 10) in the medium with cell lysis when the culture was treated with mitomycin C. We purified the enzyme by carboxymethyl-cellulose, hydroxylapatite, and gel-filtration column chromatog-raphies. The enzyme had a molecular weight of 34, 000 by SDS polyacrylamide gel electrophoresis and was mostly stable around pH 6.5. The optimum pH and temperature for the enzyme activity were 8.0 and 30℃, respectively. The activity was inhibited severely by 2mM N-ethylmaleimide, maleic anhydride, and p-chloromercuri-phenylsulfonic acid. Further, the pectin lyase produced in a medium containing glycerol was purified. The molecular weight of the enzyme was identical to that of the enzyme produced in the presence of mitomycin C.

• 社団法人日本農芸化学会の論文
• 1995-02-23

著者

• IZAKI Kazuo

  Department of Agricultural Chemistry, Faculty of Agriculture, Tohoku University

• KAMIO Yoshiyuki

  Department of Applied Microbiology, Graduate School of Agricultural Science, Tohoku University

• NIKAIDOU Naoki

  Department of Applied Biological Chemistry, Faculty of Agriculture, Niigata University

• Izaki K

  Department Of Applied Biological Chemistry Faculty Of Agriculture Tohoku University

• Izaki Kazuo

  Department Of Agricultural Chemistry Faculty Of Agriculture Tohoku University

• Nikaidou N

  Department Of Applied Biological Chemistry Faculty Of Agriculture Niigata University

• Nikaidou Naoki

  Department Of Applied Biological Chemistry Faculty Of Agriculture Tohoku University

• Nikaidou Naoki

  Department Of Applied Biological Chemistry Faculty Of Agriculture Niigata University

• Kamio Yoshiyuki

  Department Of Agricultural Chemistry Tohoku University

• Naganuma Takatoshi

  Department of Applied Biological Chemistry, Faculty of Agriculture, Tohoku University

• Naganuma Takatoshi

  Life Environment Medical Engineering Division Of Medical And Engineering Science Interdisciplinary G

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