어육 단백질의 효소 분해에 의한 peptide 생산에 관한 연구

Peptide production by enzymatic hydrolysis of fish-protein

This study was conducted to invastigate the purification and characteristic of peptides separated from fish-paste protein of Alaska Pollak(Theragria chalcogramma). The results were as follow. The hydrolitic decomposition rate of 0.5% concentration of fish-paste by protease was 45% The crude peptide contents by Dowex 50w(H+) column chromatography were the highest by 2.2~2.4㎎/ml in range of fraction no. 32~33 and molecular weights of the crude peptide by Sephadex G-25 column chromatograhy were in range of 500~50,000 Da. The purified peptide contents by SP-Sephadex C-25(H+) column chromatography were the highest by 2.0~7.8㎎/ml in range of fraction number 21~32. molecular weight of each SP-fractions according to Sephadex G-25 column chromatography was the broad distribution from 12.000 Da to 500 Da in the order of sp-4> sp-3> sp-2> sp-1. When the peptides were eluted with 0.6~0.9% and 1.2~2.0% NaCl, these peptides composed of weakly basic amino acid and strongly basic amino acid were respectively eluted. Peptides contained a large quantity of glutamic acid aspartic acid, and lycine in peptide and its sp-fractions, respectively.