酪蛋白抗血栓活性肽的制备及其鉴定
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- 英文论文题名：Preparation and characterization of Casein peptides with antithrombotic activity
- 论文作者：涂茂林 ; 冯立婷 ; 刘宏伟 ; 卢卫红 ; 杜明
- 英文论文作者：Tu Maolin ; Feng Liting ; Liu Hongwei ; Lu Weihong ; Du Ming ; School of Chemistry and Chemical Engineering ; Harbin Institute of Technology ; School of Food Science and Technology ; Dalian Polytechnic University ; National Engineering Research Center of Seafood
- 年：2016
- 作者机构：哈尔滨工业大学化工与化学学院;大连工业大学食品科学与工程学院;国家海洋食品工程技术研究中心;
- 论文关键词：酪蛋白 ; 水解 ; 抗血栓 ; 活性肽 ; 分析鉴定
- 英文论文关键词：casein ; hydrolysis ; antithrombotic ; bioactive peptides ; analysis and identification
- 会议召开时间：2016-11-09
- 会议录名称：中国食品科学技术学会第十三届年会论文摘要集
- 英文会议录名称：Abstracts of the 13th Annual Meeting of CIFST
- 语种：中文
- 分类号：TS201.2
- 学会代码：ZGSP
- 会议名称：中国食品科学技术学会第十三届年会
- 会议地点：中国北京
- 主办单位：中国食品科学技术学会
- 学会名称：中国食品科学技术学会
- 页数：2
- 文件大小：113k
- 原文格式：O
- 会议级别：全国
摘要
血栓是当代社会严重危害人类生命健康的疾病之一,现有的抗血栓药物大多存在较大的副作用。因而,开发出具有抗血栓功能的活性肽具有重要的意义。酪蛋白是牛乳中含量最高的一类蛋白质,约占牛乳总蛋白的80%。本研究旨在以酪蛋白为原料,采用胰蛋白酶进行水解,恒定水解温度37℃,pH 8.0,底物浓度4%,通过改变酶解体系中加酶量(1000~5000u/g)及水解时间(0.5~4h),以水解产物中抗凝血活性为评价指标,确定出最佳加酶量及水解时间。同时,对最优条件进行水解度测定,再利用Q+TOF对水解产物进行分析鉴定。结果表明,当加酶量为4000u/g,水解时间为3h时,水解产物的活性最高,对凝血酶的抑制率为76.25%,此时水解度为12.34%;同时,Q+TOF鉴定出丰度较大的十种肽,其中序列为HQGLPQEVLNENLLR、FFVAPFPEVFGK、EDVPSER、YLGYLEQLLR的四种肽来自于Alpha+S1-casein,序列为NMAINPSK、NAVPITPTLNR、FALPQYLK的三种肽来自于Alpha+S2-casein,序列为VLPVPQK、AVPYPQR、GPFPIIV的三种肽来自于Beta+casein。本研究结果,为酪蛋白生物活性肽尤其是抗血栓活性肽的深度开发、酪蛋白活性肽在功能性食品领域的应用等奠定了一定的理论基础。
Thrombus is one of the most serious diseases which causes serious damage to human' s health and life,most of the common antithrombotic drugs have unpleasant side effects.Therefore,it is vital significant to develop some bioactive peptides with antithrombotic activity.Casein is the major protein in bovine milk,accounted for 80%of the total protein in milk.In this study,casein was chosen as raw material and hydrolyzed by trypsin.Maintained hydrolysis temperature(37℃),pH(8.0),substrate concentration(4%),changing enzyme concentration(1000 ~ 5000 u/g) and hydrolysis time(0.5 ~4h) to determine the optimalenzyme concentration and hydrolysis time with the antithrombotic activity in the hydrolysates as evaluation index.Meanwhile,the degree of hydrolysis(DH%) of the optimal conditions was determined,and then the peptides in hydrolysateswere analyzed and identified by Q- TOF.The results showed that when the enzyme concentration is 4000u/g,hydrolysis time is 3 h,the hydrolysate have the highest activity,the thrombin inhibitory rate is 76.25%,the degree of hydrolysis(DH%) is 12.34%;Meanwhile,the abundance higher top ten peptides was identified by the Q-TOF,including four peptideswith the sequences of HQGLPQEVLNENLLR,FFVAPFPEVFGK,EDVPSER and YLGYLEQLLRwere cleaved from alpha-Si-casein,three peptideswith the sequences of NMAINPSK,NAVPITPTLNR and FALPQYLKwere cleaved from alpha-S2-casein,and three peptides with the sequences of VLPVPQK,AVPYPQR and GPFPIIVwere from beta-casein.This study laid a theoretical foundation to the deep development of the casein active peptides,especially with antithrombotic activity,and the applicationsin functional food.
Thrombus is one of the most serious diseases which causes serious damage to human' s health and life,most of the common antithrombotic drugs have unpleasant side effects.Therefore,it is vital significant to develop some bioactive peptides with antithrombotic activity.Casein is the major protein in bovine milk,accounted for 80%of the total protein in milk.In this study,casein was chosen as raw material and hydrolyzed by trypsin.Maintained hydrolysis temperature(37℃),pH(8.0),substrate concentration(4%),changing enzyme concentration(1000 ~ 5000 u/g) and hydrolysis time(0.5 ~4h) to determine the optimalenzyme concentration and hydrolysis time with the antithrombotic activity in the hydrolysates as evaluation index.Meanwhile,the degree of hydrolysis(DH%) of the optimal conditions was determined,and then the peptides in hydrolysateswere analyzed and identified by Q- TOF.The results showed that when the enzyme concentration is 4000u/g,hydrolysis time is 3 h,the hydrolysate have the highest activity,the thrombin inhibitory rate is 76.25%,the degree of hydrolysis(DH%) is 12.34%;Meanwhile,the abundance higher top ten peptides was identified by the Q-TOF,including four peptideswith the sequences of HQGLPQEVLNENLLR,FFVAPFPEVFGK,EDVPSER and YLGYLEQLLRwere cleaved from alpha-Si-casein,three peptideswith the sequences of NMAINPSK,NAVPITPTLNR and FALPQYLKwere cleaved from alpha-S2-casein,and three peptides with the sequences of VLPVPQK,AVPYPQR and GPFPIIVwere from beta-casein.This study laid a theoretical foundation to the deep development of the casein active peptides,especially with antithrombotic activity,and the applicationsin functional food.
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