南方水产科学
南方水產科學
남방수산과학
SOUTH CHINA FISHERIES SCIENCE
2014年
4期
64-69
,共6页
潘创%SHOICHIRO Ishizaki%吉宏武
潘創%SHOICHIRO Ishizaki%吉宏武
반창%SHOICHIRO Ishizaki%길굉무
虾壳%凡纳滨对虾%β虾青蛋白%pH调节法%分离蛋白特性
蝦殼%凡納濱對蝦%β蝦青蛋白%pH調節法%分離蛋白特性
하각%범납빈대하%β하청단백%pH조절법%분리단백특성
shrimp shell%Litopenaeus vannamei%β crustacyanin%pH-shift processing%protein separation characteristics
采用 pH 调节法对凡纳滨对虾(Litopenaeus vannamei)虾壳中影响虾壳红变的β虾青蛋白进行分离回收,以蛋白质回收率、纯度和二级结构含量为分离特性参数,以1.0为 pH 变化梯度,研究 pH 调节法从虾壳中提取β虾青蛋白的规律。结果显示,pH 调节法的回收率为47.5%,所得蛋白质纯度为78.23%、分子量为45000 Da。该蛋白质在 pH 3.0和11.0时有最大溶解度,分别为60.5%和55.7%;在 pH 5.0时溶解度最低为15.4%;等电点为5.6。通过圆二色光谱图分析得知β虾青蛋白是一种以α螺旋为主要二级结构存在的物质,pH 调节法所得α螺旋含量为70.1%。
採用 pH 調節法對凡納濱對蝦(Litopenaeus vannamei)蝦殼中影響蝦殼紅變的β蝦青蛋白進行分離迴收,以蛋白質迴收率、純度和二級結構含量為分離特性參數,以1.0為 pH 變化梯度,研究 pH 調節法從蝦殼中提取β蝦青蛋白的規律。結果顯示,pH 調節法的迴收率為47.5%,所得蛋白質純度為78.23%、分子量為45000 Da。該蛋白質在 pH 3.0和11.0時有最大溶解度,分彆為60.5%和55.7%;在 pH 5.0時溶解度最低為15.4%;等電點為5.6。通過圓二色光譜圖分析得知β蝦青蛋白是一種以α螺鏇為主要二級結構存在的物質,pH 調節法所得α螺鏇含量為70.1%。
채용 pH 조절법대범납빈대하(Litopenaeus vannamei)하각중영향하각홍변적β하청단백진행분리회수,이단백질회수솔、순도화이급결구함량위분리특성삼수,이1.0위 pH 변화제도,연구 pH 조절법종하각중제취β하청단백적규률。결과현시,pH 조절법적회수솔위47.5%,소득단백질순도위78.23%、분자량위45000 Da。해단백질재 pH 3.0화11.0시유최대용해도,분별위60.5%화55.7%;재 pH 5.0시용해도최저위15.4%;등전점위5.6。통과원이색광보도분석득지β하청단백시일충이α라선위주요이급결구존재적물질,pH 조절법소득α라선함량위70.1%。
We analyzed the effect of pH-shift processing method on isolation of β crustacyanin from white leg shrimp(Litopenaeus van-namei)shell. The recovery rate,purity and secondary structure content of protein were selected as separation characteristics;the pro-tein was recovered by pH-shifting at a 1. 0 interval via acid and alkali. Under these conditions,the protein recovery rate reached 47. 5% with purity of 78. 23% ;the molecular weight was 45 000 Da analyzed by SDS-PAGE and Size Exclusion Chromatography;the maximum and minimum solubilities were obtained at pH 3. 0(60. 5% ),11. 0(55. 7% )and 5. 0(15. 4% ),respectively;the iso-electric point determined by Isoelectric Focusing Electrophoresis was about 5. 6. Secondary structure content obtained by circular di-chroism spectroscopy and spectrum revealed that β crustacyanin mainly existed in α helix form and contained nearly 70. 1% α helices via pH-shift processing.