This present study investigated the ability of various soy protein hydrolysates (SPHs) in binding calcium. It was demonstrated that the amount of Ca-bound depended greatly on the SPHs obtained using different protease...This present study investigated the ability of various soy protein hydrolysates (SPHs) in binding calcium. It was demonstrated that the amount of Ca-bound depended greatly on the SPHs obtained using different proteases, which included: neutrase, flavourzyme, protease M and pepsin. The maximum level of Ca-bound (66.9 mg/g) occurred when protease M was used to hydrolyze soy protein. Peptide fragments exhibiting high Ca-binding capacity had molecular weights of either 14.4 or 8–9 kDa. The level of Ca-bound increased linearly with the increment of carboxyl content in SPHs, and further deamidation on SPHs from protease M improved Ca-binding of the hydrolysate.展开更多
To simplify the assessment method of soy protein isolate （SPI） functionalities, the viscosity and functionalities of commercial SPI products were studied. Viscosity value （y） increases With increasing concentrati...To simplify the assessment method of soy protein isolate （SPI） functionalities, the viscosity and functionalities of commercial SPI products were studied. Viscosity value （y） increases With increasing concentration （x） and exhibits a highly significant correlation with the exponential equation y = a. ebx. The b values of products are gradually enhanced from dispersion, emulsion and injected to gel type. Products with low b values （〈0.2）, and high dispersivity were dispersion-type. Products having high b values （〉0.4） and gel springiness were gel-type. The other products with centered b value （0.2-0.4）, high solubility and emulsifying capacity were emulsion-type.展开更多
文摘This present study investigated the ability of various soy protein hydrolysates (SPHs) in binding calcium. It was demonstrated that the amount of Ca-bound depended greatly on the SPHs obtained using different proteases, which included: neutrase, flavourzyme, protease M and pepsin. The maximum level of Ca-bound (66.9 mg/g) occurred when protease M was used to hydrolyze soy protein. Peptide fragments exhibiting high Ca-binding capacity had molecular weights of either 14.4 or 8–9 kDa. The level of Ca-bound increased linearly with the increment of carboxyl content in SPHs, and further deamidation on SPHs from protease M improved Ca-binding of the hydrolysate.
基金supported by the National Key Technologies Research and Development Program(No. 2012BAD34B04)Ministry of Science and Technology of the People's Republic of China
文摘To simplify the assessment method of soy protein isolate （SPI） functionalities, the viscosity and functionalities of commercial SPI products were studied. Viscosity value （y） increases With increasing concentration （x） and exhibits a highly significant correlation with the exponential equation y = a. ebx. The b values of products are gradually enhanced from dispersion, emulsion and injected to gel type. Products with low b values （〈0.2）, and high dispersivity were dispersion-type. Products having high b values （〉0.4） and gel springiness were gel-type. The other products with centered b value （0.2-0.4）, high solubility and emulsifying capacity were emulsion-type.
