NIPPON SHOKUHIN KOGYO GAKKAISHI
Print ISSN : 0029-0394
Determination of Hydrophobic Region in Soybean Globulin
Heat Denaturation of Soybean Protein. Part 1
SEISHI TAKAGIMOTONARI AKASHIKATSUHARU YASUMATSU
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1979 Volume 26 Issue 3 Pages 133-138

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Abstract

(1) A method for determination of the hydrophobic region in soybean globulin was established using 1-Anilinonaphthalene-8-sulfonate (ANS) as a probe. (2) In the native and the denatured soybean globulin heated at 90°C in the neutral solution, the maximum amount of ANS bound to 106g of them were 15 moles and 33 moles, and also the relative values of fluorescence intensity occuring by binding them to ANS were 100 and 200, respectively. Thus, the hydrophobic region in the denatured soybean globulin by heat treatment increased to two times of that in the native soybean globulin. (3) It was found that the native protein content decreased with heating the soybean globulin solution, on the other side the hydrophobic region simultaneously increased,

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© Japanese Society for Food Science and Technology
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