김 단백질 가수분해물의 Angiotensin Ⅰ 전환효소 저해 활성

Angiotensin Ⅰ Converting Enzyme(ACE) Inhibitory Activities of Laver(Porphyra tenera) Protein Hydrolysates

Angiotensin Ⅰ converting enzyme(ACE) inhibitory activities of laver(Porphyra tenera) protein hydrolysates were investigated by enzymes used for hydrolysis, molecular fractions and drying methods. For the enzymatic hydrolysis, crude laver protein, separated by filtration of water extract of dried laver extracted with 20 times(w/v) water for 3 hours at boiling temperature, were hydrolyzed with three commercial protease, Pepsin, alcalase and maxazyme NNP at optimal conditions. The yield of hydrolysis and ACE inhibitory activities of which were high in order of pepsin, alcalase and maxazyme NNP. ACE inhibitory activities of laver hydrolysates by molecular levels were high in order of 3 kDa > 10 kDa > 3∼10 kDa, and the IC/sub 50/ ACE inhibitory activities by molecular lebels were 4 mg/mL(3 kDa), 5 mg/mL(total hydrolysate), and 20 mg/mL(10 kDa), respectively. The storage stability of dried laver hydrolysates at 20℃ were strongly affected by drying methods, hot air dried of which were much stabler than freeze-dried one.