English  |  正體中文  |  简体中文  |  Items with full text/Total items : 27287/39131
Visitors : 2446139      Online Users : 33
RC Version 4.0 © Powered By DSPACE, MIT. Enhanced by NTU Library IR team.
Scope Adv. Search
LoginUploadHelpAboutAdminister

Please use this identifier to cite or link to this item: http://ntour.ntou.edu.tw:8080/ir/handle/987654321/14695

Title: 文蛤水解物中胜肽對血管升壓素轉換酶之抑制與其純化
Inhibition of Angiotensin I Converting Enzyme and Purification of Peptides from Protein Hydrolysate of Hard Clam
Authors: Jia-Ling Chen
陳佳伶
Contributors: NTOU:Department of Food Science
國立臺灣海洋大學:食品科學系
Keywords: 血管升壓素轉換酶
Hard Clam;Angiotensin I- Converting Enzyme
Date: 2004
Issue Date: 2011-06-30T07:42:12Z
Abstract: 將本省產生鮮文蛤肉以熱水抽出法處理,剩餘殘肉經由凍乾成粉末後,分別用不同蛋白酶Protease N( PN )、Prozyme 6( P6 )及Protamex( PX )於50℃進行一次水解5小時,或以Flavourzyme二次水解0.5小時,探討文蛤肉水解物對血管升壓素轉換酶 (ACE) 之抑制及其調節血壓的生理效果。文蛤肉水解物中只有以Protease N水解之產物具苦味,其餘皆不具苦味。胜肽含量以Prozyme 6經一次及二次水解最高,為523 mg/g。對ACE抑制能力而言,以Protamex 水解5小時者 (PX5) 最佳,IC50值為0.036 mg/ml。將不具苦味且抑制ACE能力效果佳之水解物 ( PX5)與Captopril (治療高血壓的藥物)比較,顯示文蛤水解物是屬於混合型之抑制類型,Ki值為0.027 mg/ml,而Captopril則為競爭型之抑制劑,Ki值為0.0067 μg/ml。 文蛤水解物(PX5)經腸胃道酵素作用後,IC50值由0.036升至0.060 mg/ml,對ACE之抑制活性下降。PX5以膠體層析法進行劃分,得五個主要劃分區,其中以分子量介於350至300Da間之劃分物具有最強的ACE抑制活性。PX5之劃分收集物E1及E2,經鑑定序列分別為Val-Arg-Lys及Tyr-Asn。
Fresh hard clam meat was extracted using hot water. The meat residue was freeze dried then hydrolyzed by Protease N (PN)、Prozyme 6 (P6) or Protamex (PX) as primary hydrolysis followed by a secondary hydrolysis (Flavourzyme, F) at 50℃. The effects of hard clam hydrolysates on inhibitory activity against angiotensin I converting enzyme (ACE) and regulating blood pressure were investigated.Only the PN hydrolyzed product tasted bitter. The maximal peptide content (523 mg/g) of hydrolysate was obtained from P6 hydrolysis for 5 hr followed by F hydrolysis for 0.5 hr. However, the lowest IC50 of hydrolysate on ACE (0.036 mg/ml) was obtained by PX hydrolysis for 5 hr (PX5). The kinetics of the hydrolysate on ACE-inhibition indicated that PX5 and Captopril (drug for hypertensive) indicated a mixed-type inhibition and competitive-type inhibition, respectively. Their Ki values were 0.027 mg/ml and 0.0067 μg/ml, repectively. The hydrolysate of PX5 was digested by gastrointestinal proteases, and the IC50 of ACE was increased from 0.036 to 0.060 mg/ml. The hydrolysate of PX5 was fractionated by gel permeation chromatography with Sephadex G-25. A fraction of 350-300 Da was found with the highest inhibitory efficiency ratio being 5831.7 %/mg/ml. The E1 and E2 amino acid sequences of PX5 were Val-Arg-Lys and Tyr-Asn, respectively.
URI: http://ethesys.lib.ntou.edu.tw/cdrfb3/record/#G0M92320022
http://ntour.ntou.edu.tw/ir/handle/987654321/14695
Appears in Collections:[食品科學系] 博碩士論文

Files in This Item:

File Description SizeFormat
index.html0KbHTML107View/Open


All items in NTOUR are protected by copyright, with all rights reserved.

 


著作權政策宣告: 本網站之內容為國立臺灣海洋大學所收錄之機構典藏,無償提供學術研究與公眾教育等公益性使用,請合理使用本網站之內容,以尊重著作權人之權益。
網站維護: 海大圖資處 圖書系統組
DSpace Software Copyright © 2002-2004  MIT &  Hewlett-Packard  /   Enhanced by   NTU Library IR team Copyright ©   - Feedback