Abstract
1) Detection of water-extractable protein fractions of Mame-miso was made by the use of electrophoresis and gel-filtration with consideration of concentration and pH conditions of proteins.
2) The water-extracted protein has given the same migration value as that of prealubumin of bovine alubumine. The protein was estimated as of spherocolloid from the viscosity determination.
3) It was recognized that the peptides showing protenoid behavior were much contained in Miso.
4) Zero-charge point of the water-extracted protein was estimated pH 4. 6-4.7 and pH 4.2-4.3 by viscosity and solubility measurements.
5) The water-extracted protein and peptides were found under solvation at high concentration, of which conditions was unstable in alkaline medium, but relatively stable in acid medium.
