碩士 / 國立臺灣海洋大學 / 食品科學系 / 92 / Abstract
The objectives of this research was to study the function of physiological active peptides from neritic squid (Loligo edulis Hoyle) sarcoplasmic protein hydrolysate. The neritic squid sarcoplasmic protein was hydrolyzed with papain, bromelin, protease Type XIV, protease Type XXIII and autolysis. The antioxidant activities of protein hydrolysates were measured by four methods inculding the Trolox equivalent antioxidant capacity, scavenging effect of DPPH(α, α-diphanyl-β- picrylhydrazyl) radical, reducing power and chelating Cu2+ effect. As results, the hydrolysate, treated with 0.03% papain 12h, showed the best antioxidativity. The papain hydrolysates were separated by using Amicon, Sephadex G-25 and DEAE Sephadex A-50 chromatography. All the steps were monitored antioxidativity. Using the four antioxidant methods, the papain hydrolysate (MW<5kDa) was found having the best antioxidativity. It was further separated by Sephadex G-25 gel filtration chromatography, and five major fractions: A (MW>1355Da), B, C, D (MW 1355~204Da) and E (MW<204Da) were obtained. The fractions (C and E) showed the best TEAC antioxidant capacity, the fraction D showed the best scavenging effect of DPPH radical and reducing power, the fractions (B and E) showed the best chelating Cu2+ effect. After DEAE Sephadex A-50 and Sephadex G-25 chromatography, the MW of fraction D was about 800Da. According to amino acid analysis, the major amino acid of fraction D was Gly (63.8%); then His (14.6%) and Tyr (14%).
| Identifer | oai:union.ndltd.org:TW/092NTOU5253021 |
| Date | January 2004 |
| Creators | Yan-Jun Hu, 胡燕君 |
| Contributors | Ching-Yu Tsao, 曹欽玉 |
| Source Sets | National Digital Library of Theses and Dissertations in Taiwan |
| Language | zh-TW |
| Detected Language | English |
| Type | 學位論文 ; thesis |
| Format | 83 |
Page generated in 0.0016 seconds