Properties of NAD(P)H-Linked Aldose Reductase from Cryptococcus lactativorus

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概要

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• A yeast growing at 48℃ was isolated from soil and the strain was identified as Cryptococcus lactativorus. The aldose reductase which the strain produced was purified 114-fold with an overal recovery of 36%. The stability of the enzyme was higher than that of other aldose reductases. The half life of the enzyme was 800 h and 14 h at 30℃ and 50℃, respectively. The enzyme showed the best activity with D-xylose. L-Sorbose and D-fructose were also reduced by the enzyme. The enzyme was active with both NADPH and NADH as a coenzyme, and the activity with NADH was 1.25 times higher than that with NADPH. The K_m^<app> value for D-xylose was 8.6 mM and the V_<max>^<app> was 20.8 units/mg when NADH was used as a coenzyme. The K_m^<app> values for NADPH and NADH were 6 μM and 170 μM, respectively, when D-glucose was used as a substrate.

• 公益社団法人日本生物工学会の論文
• 1988-12-25

著者

• MAEDA Hidekatsu

  Department of Bioengineering, Faculty of Engineering, Soka University

• Maeda H

  Soka Univ. Tokyo Jpn

• Maeda Hidekatsu

  Fermentation Research Institute Agency Of Industrial Science And Technology

• Kise Shoichi

  Bioscience Research Laboratories Mitsui Petrochemical Industries

• KOIZUMI NORIAKI

  Cantral Research Laboratory, Denki Kagaku Kogyo Kabushiki kaisha

• Koizumi Noriaki

  Cantral Research Laboratory Denki Kagaku Kogyo Kabushiki Kaisha

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