Effects of relative humidity on aggregation of soybean 7S and 11S globulins.

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概要

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• Soybean 7S and 11S globulins were stored at relative humidities (RHs) of 11% and 96% at 50°C. The redispersibility of the proteins at RH 96% decreased in a short time. However, it did not decrease, when stored for 45 days at RH 11%. Gel filtration showed that the proteins polymerized during storage. The effects of urea, sodium dodecyl sulfate (SDS) and 2-mercaptoethanol (2-ME) on the redispersibilities of the proteins at RH 96% showed that the hydrogen, hydrophobic and disulfide bonds participate in the polymerization of 7S globulin, and that the disulfide bond is strongly related to the polymerization of 11S globulin. Redispersibility was restored with 2-ME in both the 7S and 11S globulins and some of the proteins in the supernatant redispersed with 2-ME were observed to be similar to the native ones with respect to the gel filtration, electrophoretic behavior and circular dichroism spectrum.

• 公益社団法人 日本農芸化学会の論文

著者

• HOSHI Yuji

  Department of Food Chemistry, Faculty of Agriculture, Tohoku University

関連論文

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• Determination of Sulfhydryl and Disulfide Contents of Soybean 11S Globulin and Their Change by Lyophilization
• Effects of relative humidity on aggregation of soybean 7S and 11S globulins.

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