Abstract
Proteins of Perilla frutescens seeds were step-extracted with 20 mmol/L phosphate buffer, 0.5 mol/L NaCl, 70% ethanol, and 3% acetic acid. The total amount of extracted proteins from 1 g of seeds was 138.6 mg and 96.7% of the amount of proteins was water- and NaCl-soluble. The water- and NaCl-soluble perilla proteins contained large amounts of Glu, Gly, Asp, Val, and Arg, but lower amounts of Met and His. The water- and NaCl-soluble perilla proteins were immediately digested in simulated gastric fluid containing pepsin. The water-soluble perilla proteins had less trypsin-inhibitive activity compared with soybean and the NaCl-soluble perilla protein had no trypsin- inhibitive activity.
