Earticle

초록

영어

We purified recombinant galactose 6-phosphate isomerase (LacAB) from Lactococcus lactis using HiTrap Q HP and Phenyl-Sepharose columns. The purified LacAB had a final specific activity of 1.79 units/mg to produce D-allose. The molecular mass of native galactose 6-phosphate isomerase was estimated at 135.5 kDa using Sephacryl S-300 gel filtration, and the enzyme exists as a hetero-octamer of LacA and LacB subunits. The activity of galactose 6-phosphate isomerase was maximal at pH 7.0 and 30°C, and enzyme activity was independent of metal ions. When 100 g/L of D-psicose was used as the substrate, 25 g/L of D-allose and 13 g/L
of D-altrose were simultaneously produced at pH 7.0 and 30°C after 12 h of incubation. The enzyme had broad specificity for various aldoses and ketoses. The interconversion of sugars with the same configuration except at the C2 position was driven by using a large amount of enzyme in extended reactions. The interconversion occurred via two isomerization reactions, i.e., the interconversion of D-allose↔D-psicose↔Daltrose, and D-allose to D-psicose reaction was faster than D-altrose to D-psicose reaction.

키워드

저자

• Ha-Young Park [ Department of Bioscience and biotechnology, Konkuk University ]
• Hye-Jung Kim [ Department of Bioscience and biotechnology, Konkuk University ]
• Seon-Won Kim [ Division of Applied Life Science, Gyeongsang National University ]
• Deok-Kun Oh [ Department of Bioscience and biotechnology, Konkuk University ]

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간행물

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• 간행물명

  한국생물공학회 학술대회

• 간기

  반년간

• 수록기간

  1985~2013

• 십진분류

  KDC 476 DDC 576