Applying the one-step process developed by Fujimaki.,
15N-methionine (
15N-Met) was incorporated into soy protein isolate (SPI) using Papain (EC 3.4.4.10) to obtain a
15N-Met incorporated plastein, with its Met level enhanced to that of whole egg protein.
This plastein contained 2.56mg Met/16mg N, which was equivalent to about twice that of the original SPI.
Ratios of Met to threonine (Thr) and of sulfur-containing amino acids to Thr in this plastein were higher than those in SPI and the essential amino acid pattern of this plastein was shown to be similar to that of whole egg Protein.
To examine the
in vitro digestion process of this plastein, gel filtration on Sephadex G-25 (fine) or G-15 was done With
in vitro digesta using Pepsin or pepsin-pancreatin. The
15N concentration was also determined on each fraction.
As the pepsin or pepsin-pancreatin digestion proceeded,
15N concentration in the fractions containing relatively small peptides increased.
Thus, this finding suggests that
15N-Met incorporated plastein is easily digested by these proteolytic enzymes.
Another experiment using these enzymes was undertaken to compare
in vitro digestibility of this Plastein with that of SPI.
It was demonstrated that this plastein contains low molecular weight peptides soluble in 10% trichloroacetic acid (TCA) than SPI. From the standpoint of the TCA insoluble proteins the
in vitro digestibility of SPI is higher than that of plastein.
In conclusion, the Met incorporated plastein appears to be a nutritionally excellent protein-like substance because the incorporated Met shows good digestibility in the
in vitro digestion process and contributes to an improvement of nutritional values of constituent amino acids.
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