With the different quality ratio of 1:0, 1:1, 1:2, 2:1
and 0:1 (drying basis), co-precipitation protein was prepared from tilapia
muscle and defatted soybean meal by pH-shifting. Tilapia protein isolate (FPI),
co-precipitation protein (CoPP-1:1, CoPP-1:2, CoPP-2:1) and soybean protein
isolate (SPI) of 18 kinds of protein powder were prepared by freeze drying. Its
basic components, solubility, whiteness and amino acid composition were
analyzed. Results showed that the content of the crude protein of co-precipitation
protein was above 80%, and fat content was less than 1.07%, with being more
than or near to the crude protein and fat content of FPI and SPI. The
solubility of co-precipitation protein was poor at pH 4.0-6.0, it increased
when the pH value was below 4.0 or above 6.0 and reached the maximum value at
the extreme pH environment. Relatively, the solubility of CoPP-1:1 and CoPP-1:2
at pH 7.0-8.0 was higher than that of CoPP-2:1 and FPI, but both of them were
lower than the solubility of SPI in water and the whiteness of co-precipitation
protein was better. The results showed that the composition of CoPP-1:1 and
CoPP-1:2 are closer to SPI. SPI mainly consists of water soluble globulin, and
has higher solubility in water. The composition of essential amino acid of
co-precipitation protein was complete, and the total essential amino acids were
about 42 percent of total amino acids, which belonged to high quality protein.
Therefore, pH-shifting process could extract high protein content and high
nutritional value of co-precipitation protein.
QI Hui-hong et al
. Co-precipitated protein from tilapia muscle and soybean meal and its solubility and amino acid composition analysis[J]. Food and Fermentation Industries, 2018
, 44(1)
: 166
.
DOI: 10.13995/j.cnki.11-1802/ts.014795