Purification and Properties of Extracellular β-Mannanases Produced by Enterococcus casseliflavus FL2121 Isolated from Decayed Konjac

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概要

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• Two β-mannanases (M-I and M-II) were purified from the culture filtrate of Enterococcus casseliflavus FL by ammonium sulfate precipitation, column chromatography of DEAE-Toyopearl 650M and Phenyl-Toyopearl 650M and preparative polyacrylamide gel electrophoresis to homogenities. The molecular weights of M-I and M-II were estimated to be 142,000 and 137,000 by SDS-polyacrylamide gel electrophoresis and 127,000 and 113,000 by gel filtration, respectively. M-I and M-II exhibited an optimum pH at 6.0 and an optimum tmperature at 50℃. The enzymes were activated slightly by CoCl_2 and MnCl_2,and inhibited sotongly by AgNO_3,HgCl_2,EDTA, and N-bromosuccinimide. The K_m values of M-I and M-II for konjac β-1,4-glucomannan were 0.14 and 0.30 (mg/ml), and the maximum velocities were 1,110 and 1,700 (U/mg protein), respective. Both enzymes were endo-type β-mannanases hydrolyzing mannosides larger than β-1,4-D-mannotetraose.

• 社団法人日本生物工学会の論文
• 1993-07-25

著者

• ODA Yuji

  Department of Food Science, Obihiro University of Agriculture and Veterinary Medicine, Obihiro

• Oda Y

  National Agricultural Res. Center For Hokkaido Region Hokkaido Jpn

• TONOMURA KENZO

  Department of Agricultural Chemistry, College of Agriculture, University of Osaka Prefecture

• KOMAKI TOSHIAKI

  Department of Food Science and Technology, Fukuyama University

• Komaki Toshiaki

  Department Of Food Science & Technology Fukuyama University

• Tonomura Kenzo

  Department Of Agricultural Chemistry College Of Agriculture University Of Osaka Prefecture

• Oda Yuji

  Department Of Agricultural And Life Science Obihiro University Of Agriculture And Veterinary Medicin

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