Heat stability of the phototransforming activity of Chenopodium chlorophyll protein

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概要

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• The protein moiety of the Chenopodium chlorophyll protein CP668 is indispensable in the formation of a water-soluble complex with chlorophyll and in the photooxidation of chlorophyll. The phototransforming activity of CP668 into CP743 was completely preserved even after drastic heat treatment at 100℃. The absorbance ratio of the 743-nm band peak to the 668-nm band peak somewhat increased after heat treatment. Initial velocities of the increase in the 743-nm band peak and the decrease in the 668-nm band peak were not appreciably influenced by heat treatment. Viscosity measurement suggested that the heat-treated CP668 was much smaller in particle size than the untreated one.

• 日本植物生理学会の論文

著者

• Yoshida Mizuki

  Institute Of Biophysics Faculty Of Agriculture Kyushu University

• Oku Tatsuo

  Institute Of Biophysics Faculty Of Agriculture Kyushu University

• Tomita Giiti

  Institute Of Biophysics Faculty Of Agriculture Kyushu University

• Oku Tatsuo

  Institute of Biophysics, Faculty of Agriculture, Kyushu University

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