欢迎来到天天文库
浏览记录
ID:34339742
大小:74.75 KB
页数:11页
时间:2019-03-05
《不同离子强度下罗非鱼肌球蛋白热变性聚集研究》由会员上传分享,免费在线阅读,更多相关内容在工程资料-天天文库。
1、不同离子强度下罗非鱼肌球蛋白热变性聚集研究李婷朱潘红齐慧红周春霞洪鹏志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水产品深加工广东普通高等学校重点实验室摘要:以罗非鱼肉为原料,提取肌球蛋白,分析不同离子强度(1、50、150、300、600mmol/KCl)下热处理(40〜80°C,l°C/min)对其浊度、溶解度、表面疏水性、Q-螺旋含量及聚集体粒径的影响。结果显示,离子强度及热处理温度明显影响肌球蛋白的热变性聚集。在低离子强度(P150mmol/LKC1)下,肌球蛋白聚集成纤丝,溶解性差,热处理后分子聚集沉淀,溶解度和a-螺旋含量减小(P2、),体系热稳定性差;在高离子强度(300^600mmol/LKC1)下,肌球蛋白分子解离成单体,溶液澄清,当热处理温度高于50°C时,肌球蛋白溶解度下降,表而疏水性增加,a-螺旋含量显著减小(p<0.05),但分子聚集不明显。总体分析,高盐离子的静电屏蔽作用导致肌球蛋白纤丝解离,由此也会对肌球蛋白分子结构有一定的保护作用,热稳定性相对较好。关键词:罗非鱼;肌球蛋口;离子强度;热变性聚集;结构变化;作者简介:李婷(1994-),女,在读硕士,研究方向:罗非鱼肌球蛋白增溶和稳态化研究。E-mail:LTZzang@163.com.作者简介:周春霞(1979-)女,博士3、,副教授,研究方向:水产品加工与贮藏。E-mail:chunxia.zhou@163・com・基金:国家自然科学棊金项Fl(31201389)StudyonthethermaldenaturationandaggregationoftilapiamyosinunderdifferentionicstrengthconditionsLiTingZhuPan-hongQ[Hui-hongZHOUChun-xiaHONGPeng-zhiCollegeofFoodScienceandTechnology,GuangdongOceanUniversity;Abstract:4、Tilapiawasusedasmaterialtoextractmyosin.Theeffectsofheattreatment(40-80°C,loC/min)ontheturbidity,solubility,surfacehydrophobicity,a-helixcontentandaggregatedparticlesofmyosinwereinvestigatedunderdifferentionicstrength(1,50,150,300,600mmol/KCl).Theresultsshowedthattheionicstrengthandhe5、attreatmentsignificantlyaffectedthethermaldenaturationandaggregationofmyosin.Myosinhaspoorsolubilitybecauseofitassemblesandformsafilamentouspolymerunderlowionicstrength(1-150mmol/LKC1),afterheattreatment,themolecularaggregationprecipitales,thesolubilityanda-helixcontentdecreased(p<0.06、5),thethermalstcibilityofthemyosininthissystemwasundesirable-Whilcundcrthehighionicstrength(300-600mmol/LKC1),myosindissociatedintomonomer,thesolutionisclear.Whenthetemperatureishigherthan50°C,aincreaseinturbidityanddecreaseinsolubilityofti1apiamyosinwasdetected,accompaniedbyincreasin7、ginsurfacehydrophobicityandasignificantlossofa-helix(p<0.05),butthemolecularaggregationisnotobvious.TheresuItsindicatedthattheelectrostaticshieldingofhighsaltionsinhibitedformationofmyosinfilament,whichalsoprotectsthemolecularstruetureofmyosin.Sothatthemyosinthatunderthehighionicstren8、gthha
2、),体系热稳定性差;在高离子强度(300^600mmol/LKC1)下,肌球蛋白分子解离成单体,溶液澄清,当热处理温度高于50°C时,肌球蛋白溶解度下降,表而疏水性增加,a-螺旋含量显著减小(p<0.05),但分子聚集不明显。总体分析,高盐离子的静电屏蔽作用导致肌球蛋白纤丝解离,由此也会对肌球蛋白分子结构有一定的保护作用,热稳定性相对较好。关键词:罗非鱼;肌球蛋口;离子强度;热变性聚集;结构变化;作者简介:李婷(1994-),女,在读硕士,研究方向:罗非鱼肌球蛋白增溶和稳态化研究。E-mail:LTZzang@163.com.作者简介:周春霞(1979-)女,博士
3、,副教授,研究方向:水产品加工与贮藏。E-mail:chunxia.zhou@163・com・基金:国家自然科学棊金项Fl(31201389)StudyonthethermaldenaturationandaggregationoftilapiamyosinunderdifferentionicstrengthconditionsLiTingZhuPan-hongQ[Hui-hongZHOUChun-xiaHONGPeng-zhiCollegeofFoodScienceandTechnology,GuangdongOceanUniversity;Abstract:
4、Tilapiawasusedasmaterialtoextractmyosin.Theeffectsofheattreatment(40-80°C,loC/min)ontheturbidity,solubility,surfacehydrophobicity,a-helixcontentandaggregatedparticlesofmyosinwereinvestigatedunderdifferentionicstrength(1,50,150,300,600mmol/KCl).Theresultsshowedthattheionicstrengthandhe
5、attreatmentsignificantlyaffectedthethermaldenaturationandaggregationofmyosin.Myosinhaspoorsolubilitybecauseofitassemblesandformsafilamentouspolymerunderlowionicstrength(1-150mmol/LKC1),afterheattreatment,themolecularaggregationprecipitales,thesolubilityanda-helixcontentdecreased(p<0.0
6、5),thethermalstcibilityofthemyosininthissystemwasundesirable-Whilcundcrthehighionicstrength(300-600mmol/LKC1),myosindissociatedintomonomer,thesolutionisclear.Whenthetemperatureishigherthan50°C,aincreaseinturbidityanddecreaseinsolubilityofti1apiamyosinwasdetected,accompaniedbyincreasin
7、ginsurfacehydrophobicityandasignificantlossofa-helix(p<0.05),butthemolecularaggregationisnotobvious.TheresuItsindicatedthattheelectrostaticshieldingofhighsaltionsinhibitedformationofmyosinfilament,whichalsoprotectsthemolecularstruetureofmyosin.Sothatthemyosinthatunderthehighionicstren
8、gthha
此文档下载收益归作者所有