期刊
JOURNAL OF FOOD SCIENCE
卷 69, 期 4, 页码 C303-C311出版社
WILEY
DOI: 10.1111/j.1365-2621.2004.tb06332.x
关键词
soybeans; soy protein; protein functionality; pilot plant; glycinin; beta-conglycinin
Glycinin and beta-conglycinin have unique functionality characteristics that contribute important properties in soy foods and soy ingredients. Limited functionality data have been published for glycinin and beta-conglycinin fractions produced in pilot-scale quantities. Protein extraction conditions were previously optimized for our pilotscale fractionation process to maximize protein solubilization and subsequent product recovery. Glycinin, beta-conglycinin, and intermediate (mixture of glycinin and beta-conglycinin) fractions were prepared using optimizedprocess (OP) extraction conditions (10:1 water-to-flake ratio, 45 degreesC) andprevious conditions termed Wu process (WP) (15:1, 20 degreesC). Viscosity, solubility, gelling, foaming, emulsification capacity, and emulsiflication activity and stability of the fractionated proteins, and soy protein isolate (SPI) produced from the same clefatted soy white flakes were compared to evaluate functional properties of these different protein fractions. Differential scanning calorimetry, sodium doclecylsulfate-polyacrylamide gel electrophoresis, and surface hydrophobicity data were used to interpret functionality differences. OP beta-conglycinin had more glycinin contamination than did the WP beta-conglycinin. OP and WP solubility profiles were each similar for respective glycinin and beta-conglycirtin fractions. Emulsification activities and stabilities were higher for OP beta-conglycinin and OP intermediate fractions compared with respective WP fractions. beta-Conglycinin and SPI emulsification capacities (ECs) mirrored solubility profile, whereas glycinin ECs did not. OP glycinin had a higher foaming capacity than WP glycinin. OP and WP intermediate fraction apparent viscosities trended higher than those of other protein fractions. beta-Conglycinin dispersions at pH 3 and 7 produced firm gels at 80 degreesC, whereas glycinin dispersions formed weaker gels at 99 degreesC and did not gel at 80 degreesC.
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