HEAT DENATURATION OF SOYBEAN PROTEINS .2. INFLUENCE OF HEATING TEMPERATURE ON CONFORMATIONAL-CHANGES OF SOYBEAN PROTEINS

被引:69
作者
HASHIZUME, K
WATANABE, T
机构
[1] MINIST AGR & FORESTRY, NATL FOOD RES INST, TSUKUBA 30021, JAPAN
[2] KYORITSU WOMENS UNIV, CHIYODA KU, TOKYO, JAPAN
来源
AGRICULTURAL AND BIOLOGICAL CHEMISTRY | 1979年 / 43卷 / 04期
关键词
D O I
10.1080/00021369.1979.10863529
中图分类号
S3 [农学(农艺学)];
学科分类号
0901 ;
摘要
Changes of ultracentrifugal patterns of soybean proteins by heating up to 100°C were almost completed at SO°C at lower ionic strength and at 90°C at higher ionic strength. However, changes in DTNB reactive sulfhydryl groups, sulfite reducible disulfide bonds, ultraviolet difference spectra and turbidity of the protein solutions were still observed at temperatures higher than 80 or 90°C. These results suggest that 11S protein dissociates into subunits at a temperature below 80 or 90°C, and that the conformations of these subunits can change at a temperature above SO or 90°C. When heated at high ionic strength, the protein solution became turbid because of aggregation of proteins. SDS polyacrylamide gel electrophoresis showed that aggregated proteins separated by centrifugation as precipitates were formed from low-molecular-weight subunits of lIS protein and non-aggregated proteins remaining in the supernatant were from 7S protein and high-molecular-weight subunits of 11S protein. © 1979 Taylor & Francis Group, LLC.
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页码:683 / 690
页数:8
相关论文
共 18 条
[1]  
CARTER JR, 1959, J BIOL CHEM, V234, P1705
[2]  
CATSIMPOOLAS N, 1970, CEREAL CHEM, V47, P559
[3]  
CATSIMPOOLAS N, 1970, CEREAL CHEM, V47, P331
[4]   TISSUE SULFHYDRYL GROUPS [J].
ELLMAN, GL .
ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS, 1959, 82 (01) :70-77
[5]  
FUKUSHIMA D, 1969, CEREAL CHEM, V46, P156
[6]   DENATURATION OF SOYBEAN PROTEIN BY FREEZING .1. [J].
HASHIZUM.K ;
KAKIUCHI, K ;
KOYAMA, E ;
WATANABE, T .
AGRICULTURAL AND BIOLOGICAL CHEMISTRY, 1971, 35 (04) :449-&
[7]   HEAT DENATURATION OF SOYBEAN PROTEINS .1. INFLUENCE OF IONIC-STRENGTH ON CONFORMATION CHANGES OF SOYBEAN PROTEINS CAUSED BY HEATING, AND RELATIONSHIP OF ITS CONFORMATION CHANGES TO GEL FORMATION [J].
HASHIZUME, K ;
NAKAMURA, N ;
WATANABE, T .
AGRICULTURAL AND BIOLOGICAL CHEMISTRY, 1975, 39 (07) :1339-1347
[8]   RECOVERY OF INTACT STRUCTURE OF TAKA-AMYLASE A AFTER REDUCTION OF ALL DISULFIDE LINKAGES IN 8 M UREA [J].
ISEMURA, T ;
TAKAGI, T ;
YUTANI, K ;
MAEDA, Y .
JOURNAL OF BIOCHEMISTRY, 1963, 53 (02) :155-&
[9]  
ISHINO K, 1975, CEREAL CHEM, V52, P9
[10]   ISOLATION AND SOME PHYSICOCHEMICAL PROPERTIES OF ACIDIC SUBUNITS OF SOYBEAN 11S GLOBULIN [J].
KITAMURA, K ;
SHIBASAKI, K .
AGRICULTURAL AND BIOLOGICAL CHEMISTRY, 1975, 39 (05) :945-951