Purification and Identification of Angiotensin Convering Enzyme Inhibitory Peptides from Cobia Fish / 海鱺魚肉中具血管收縮素轉化酶抑制能力胜肽之純化與鑑定

碩士 / 國立澎湖科技大學 / 食品科學研究所 / 100 / In this study, Cobia fish was hydrolyzed by ten protease to investigate ACE inhibitory capacity of the hydrolyzate. The results show that all cobia fish hydrolyzates have ACE inhibitory capacity. Neutrase hydrolysate have the highest ACE inhibitory capacity (68.38%). Further explore the optimal hydrolysis conditions by response surface methodology. Central composite design was applied with response surface methodology to evaluate the effect of the enzyme and substrate ratio (E/S), hydrolysis temperature(℃), initial pH of hydrolysis on ACE inhibitory capacity and the degree of hydrolysis (DH). The results showed that at pH 7,the high concentration of E/S, the low hydrolysis temperature, the hydrolysate has the highest ACE inhibitory capacity and DH;the maximum ACE inhibitory capacity and DH obtained by hydrolysis temperature at 32.70℃, pH at 7.21, E/S ratio at 0.42%, the predicted ACE inhibitory capacity was 91.16% and the predicted DH was 73.87%. After run at the optimal conditions, the ACE inhibitory capacity was 88.51 % and the DH was 69.12%. F4-2A and F4-2B fractions isolated from Neutrase hydrolyzate were purified by membrane filtration system (<5000 Da), DEAE-Sepharose Fasy Flow, Sephadex G-25 and RP-HPLC, and speculated they may contain aromatic amino acids.

Identiferoai:union.ndltd.org:TW/100NPHT1252001
Date January 2012
CreatorsLai,Yushen, 賴昱燊
ContributorsHu,Hunghsi, 胡宏熙
Source SetsNational Digital Library of Theses and Dissertations in Taiwan
Languagezh-TW
Detected LanguageEnglish
Type學位論文 ; thesis
Format73

Page generated in 0.0134 seconds