Purification and Properties of 3-Deoxyglucosone Metabolizing Enzyme from S. cerevisiae Y_(Br-M)

LIANG Zhi qun, MO Bai li, LI Xiang ping, SU Gui jiao, PANG Zong wen,HUANG Shi hai

Chinese Journal of Biochemistry and Molecular Biology ›› 2000, Vol. 16 ›› Issue (01) : 106-109.

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PDF(207 KB)
Chinese Journal of Biochemistry and Molecular Biology ›› 2000, Vol. 16 ›› Issue (01) : 106-109.
Article

Purification and Properties of 3-Deoxyglucosone Metabolizing Enzyme from S. cerevisiae Y_(Br-M)

  • LIANG Zhi qun, MO Bai li, LI Xiang ping, SU Gui jiao, PANG Zong wen,HUANG Shi hai
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Abstract

Deoxyglucosone, a highly reactive and toxic compound, is a major intermediate in the Maillard reaction. An NADPH dependent 3 deoxyglucosone metabolizing enzyme from S. cerevisiae Y Br M was isolated and purified by ammoniun sulfate fractionation, DEAE cellulose 52 column chromatography, Hydroxyapatite column chromatography and DEAE sepharose CL 6B column chromatography. The molecular weight of the enzyme was estimated to be 44 000 dalton and the enzyme was a monomer. The optimum pH of the enzyme activity was 7 0. The K m for 3 deoxyglucosone was 2 25 mmol/L. The enzyme was stable at pH6 0-8 0. The enzyme was stable at 35℃. It lost 50% of its activity when incubated at 50℃ for 30 min. 2 Oxoaldehyde compounds were found to be good substrates and monocarbonyl compounds were poor substrates for this reductase. The enzyme activity was inhibited by iodoacetic acid and N ethylmaleimide; β Mercaptoethanol and dithiothreitol activated the activity of enzyme. The enzyme that specifically required NADPH was a coenzyme for activity and was inactive when NADH was substituted for NADPH.

Key words

Maillard reaction / 3 Deoxyglucosone / S. cerevisiae Y Br M / Purification

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LIANG Zhi qun, MO Bai li, LI Xiang ping, SU Gui jiao, PANG Zong wen,HUANG Shi hai. Purification and Properties of 3-Deoxyglucosone Metabolizing Enzyme from S. cerevisiae Y_(Br-M)[J]. Chinese Journal of Biochemistry and Molecular Biology, 2000, 16(01): 106-109

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