Abstract
Physicochemical properties of soy proteins extracted from check soybean cultivar 5601T and four new Tennessee soybean lines TN03-349, TN04-5321, TN08-002, and TN08-015 were compared. The protein extracted from 5601T had the lowest content of total protein and the lowest denaturation temperature and enthalpy (P < 0.05). The lowest solubility was observed at pH 5.0 for 5601T, TN04-5321, and TN03-349, while it was at pH 6.0 for the other two, which agreed with zeta-potential data. TN04-5321 and TN08-002 extract powder had a higher content of total protein than the other three (P < 0.05). The TN04-5321 extract was absent in an acidic glycinin subunit which may be the cause of its best gelation properties. Despite difficulties in correlating structure and functionality, it was noted that the gel formed from TN04-5321 with CaCl2 at pH 7 was 6 times stronger than that of 5601T, which may be significant to bean curd products.
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