文献类型：期刊文献

中文题名：鸢乌贼和杜氏枪乌贼蛋白分离及其性质初探

英文题名：Proteins isolation from Symplectoteuthis oualaniensisand and Loligo duvauceli and their characteristics

作者：邱月[1];曾少葵[1];章超桦[1];郝记明[1];张静[1]

机构：[1]广东海洋大学食品科技学院广东省水产品加工与安全重点实验室广东普通高等学校水产品深加工重点实验室南海生物资源开发与利用协同创新中心

年份：2016

卷号：42

期号：9

起止页码：81

中文期刊名：食品与发酵工业

外文期刊名：Food and Fermentation Industries

收录：CSTPCD、、北大核心2014、CSCD2015_2016、北大核心、CSCD

基金：广东省教育厅创新强校工程项目(2014GKXM047)

语种：中文

中文关键词：鸢乌贼;杜氏枪乌贼;蛋白分离;SDS-PAGE;DSC;溶解度

外文关键词：Symplectoteuthis oualaniensis; Loligo duvauceli; protein separation; SDS-PAGE; DSC; solubility

中文摘要：以鸢乌贼(Symp lectoteuthis oualaniensis)和杜氏枪乌贼(Loligo duvauceli)头足、胴体为原料,分离各蛋白组分,并对其性质进行研究。结果表明:鸢乌贼头足水溶性蛋白(WSP)、盐溶性蛋白(SSP)和不溶性蛋白(ISP)分别占总蛋白的19.01%、52.21%和13.23%,胴体中的分别为10.83%、58.68%和10.03%;杜氏枪乌贼头足三者的比例分别为37.62%、31.79%和18.08%,胴体中的分别为24.30%、54.23%和7.65%。2种乌贼头足、胴体均是WSP和SSP必需氨基酸占氨基酸总量的40%左右。SDS-PAGE电泳分析显示,鸢乌贼头足和胴体中SSP的肌球蛋白重链(MHC)的分子质量大于200 k Da、副肌球蛋白(PM)的在100 k Da左右、肌动蛋白(Actin)接近44k Da;杜氏枪乌贼头足和胴体中SSP的MHC、PM、Actin蛋白条带颜色较浅,说明其蛋白含量较低。差示扫描量热法(DSC)结果表明,鸢乌贼头足WSP、SSP和ISP的变性温度分别为64.02℃、58.04℃和68.91℃;胴体中的分别为81.93℃、62.18℃和68.54℃;杜氏枪乌贼头足各蛋白组分的变性温度分别为81.36、83.24和78.18℃;胴体的分别为80.29、76.25和68.02℃,杜氏枪乌贼各蛋白组分的变性温度较鸢乌贼的高。鸢乌贼头足、胴体和杜氏枪乌贼头足WSP在p H 3溶解度最低,杜氏枪乌贼胴体的在p H 5最低,p H对SSP溶解度影响较大;在不同离子强度的溶液中,鸢乌贼头足SSP溶解性最好。

外文摘要：According to the solubility,water soluble protein（ WSP）,salt soluble protein（ SSP） and insoluble protein（ ISP） were isolated from the cephalopodium and mantles muscle of Symplectoteuthis oualaniensis and Loligo duvauceli. The results showed that in Symplectoteuthis oualaniensis,WSP,SSP and ISP component was 19. 01%,52. 21% and 13. 23% in cephalopodium and 10. 83%,58. 68% and 10. 03% in mantles muscle. In Loligo duvauceli,WSP,SSP and ISP percentage in cephalopodium and mantles muscle were 37. 62%,31. 79%,18. 08% and24. 30%,54. 23%,7. 65%,respectively. In cephalopodium and mantles muscle of Symplectoteuthis oualaniensis and Loligo duvauceli,the essential amino acids content in WSP and SSP was 40% of total amino acid. SDS-PAGE pattern showed that in cephalopodium and mantles muscle of Symplectoteuthis oualaniensis,the molecular weight of MHC was more than 200 k Da,PM was about 100 k Da and Actin was close to 44 k Da. In cephalopodium and mantles muscle of Loligo duvauceli,the MHC,PM and Actin protein bands of the SSP were lighter,indicating that the contents of the proteins were lower. As demonstrated by DSC,the denaturation temperature of WSP,SSP and ISP in cephalopodium of Symplectoteuthis oualaniensiswere 64. 02℃,58. 04℃ and 68. 91℃,and 81. 93℃,62. 18℃ and 68. 54℃ in mantles muscle; for Loligo duvauceli,the denaturation temperature of WSP,SSP and ISP was 81. 36℃,83. 24℃ and78. 18℃ in cephalopodium and 80. 29℃,76. 25℃ and 68. 02℃ in mantles muscle. The denaturation temperature of proteins from Loligo duvauceli were higher than that of Symplectoteuthis oualaniensis. The solubility of WSP in cephalopodium and mantles muscle of Symplectoteuthis oualaniensis and cephalopodium of Loligo duvauceli were at the minimum at p H 3; at p H 5,WSP solution in mantles muscle of Loligo duvauceli was the lowest. In different ionic strength solution,the solubility of SSP was better in cephalopodium of Symplectoteuthis oualaniensis.