期刊
FOOD AND BIOPROCESS TECHNOLOGY
卷 5, 期 5, 页码 1622-1629出版社
SPRINGER
DOI: 10.1007/s11947-010-0439-9
关键词
Jellyfish; Collagen; Angiotensin-I-converting enzyme; Hydrolysis; Response surface methodology
Collagen extracted from jellyfish (Rhopilema esculentum) was hydrolyzed with alcalase to prepare the ACE-inhibitory peptide. The optimal hydrolyzing conditions were determined using response surface methodology. The results showed that the optimal conditions were temperature of 52.7 A degrees C, pH of 8.63 and enzyme-to-substrate ratio (E/S) of 3.46%, and the ACE-inhibitory activity of the obtained hydrolysates could reach 81.7%. Jellyfish collagen peptide, UF3-B2, was purified from the hydrolysates using ultrafiltration, ion-exchange chromatography and gel filtration. The IC50 value of UF3-B2 was 43 mu g/ml, and the yield accounted for 6.25% of the hydrolysates. The molecular weight distribution of UF3-B2 was from 200 to 600 Da. Amino acid analyses showed that UF3-B2 was rich in Gly, Pro, Glu, Ala, and Asp.
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