Structural Contribution of the Carbohydrate Moiety to the Alkaline Hydrolysis of Aryl Glycosylamine Linkages |
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Authors: | Shigehiro Hirano Sumiyo Kondo |
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Affiliation: | Department of Agricultural and Biological Chemistry, Tottori University, Tottori 680 |
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Abstract: | Differential scanning calorimetry (DSC) thermograms of soybean protein isolate developed two peaks corresponded to 11S and 7S globulin, the denaturation temperatures of which were 93.3 and 76.5°C, respectively, with 94% water. These peaks shifted to higher temperatures with lower water contents of the sample. At 47% water, there were two peaks, at 149 and 118.7°C, and at 11% water, there was one peak at 180°C. The DSC thermogram measured during cooling and reheating gave no peak. The soybean protein isolate was heated with 24.5% water at 100°C and then mixed with more water to the water contents of 94%. This sample gave two peaks at temperatures close to those of the original soybean protein, indicating that the soybean protein was not denatured at temperatures even above 100°C when the water content was low. |
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Keywords: | endoglucanase glycoside hydrolase family 45 temperature profile Humicola grisea Rhizopus oryzae |
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