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食品研究与开发:2024,45(2):87-95
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吊干杏杏仁蛋白功能特性和结构特性
(1.塔里木大学食品科学与工程学院,新疆阿拉尔 843300;2.南疆特色农产品深加工兵团重点实验室,新疆阿拉尔 843300;3.塔里木大学分析测试中心,新疆阿拉尔 843300;4.武汉市农业科学院,湖北武汉 430207)
Functional and Structural Characteristics of Proteins in Almond Kernel of Hanging Dried Apricot
(1.College of Food Science and Engineering,Tarim University,Alar 843300,Xinjiang,China;2.Production&Construction Group Key Laboratory of Special Agricultural Products Further Processing in Southern Xinjiang,Alar 843300,Xinjiang,China;3.Analysis and Testing Center,Tarim University,Alar 843300,Xinjiang,China;4.Wuhan Academy of Agricultural Sciences,Wuhan 430207,Hubei,China)
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投稿时间:2022-10-30    
中文摘要: 为提高吊干杏加工副产物的利用率,以吊干杏杏仁为原料,通过Osborne 分级分离法和传统碱溶酸沉法分别提取清蛋白、球蛋白和分离蛋白,分析比较3 种蛋白的氨基酸组成及功能和结构特性。结果表明,吊干杏杏仁中3 种蛋白质的含量丰富,氨基酸配比合理,其中谷氨酸含量最高;在pH 值为7 的条件下,清蛋白溶解性[(50.00±0.87)%]、持油性[(16.06±0.22)g/g]均较好;pH 值由3 增加至9,3 种蛋白的起泡能力呈现先降低后升高趋势。清蛋白和球蛋白泡沫稳定性变化趋势相似,与起泡性变化趋势相反。球蛋白的表面疏水性和游离巯基含量均显著高于清蛋白和分离蛋白(P<0.05);3 种蛋白的二级结构均以β-转角和β-折叠为主。十二烷基硫酸钠-聚丙烯酰胺凝胶电泳分析表明,3 种蛋白亚基含量分布均较广,分子量在11~63 kDa,其中在21、22 kDa 处的谱带最为强烈。
Abstract:To improve the utilization of by-products of hanging dried apricot in processing,this paper,with almond kernel of hanging dried apricot as raw material,extracted albumin,globulin and protein isolate by Osborne fractionation and traditional alkali-soluble acid precipitation,and compared the amino acid composition,function and structural characteristics of the three proteins.The results showed that hanging dried apricot was rich in the three proteins.The ratio of amino acids was reasonable,and the content of glutamate was the highest.Under pH7,the solubility[(50.00±0.87)%]and oil holding capacity[(16.06±0.22)g/g]of albumin were desirable.With the increase of pH value from 3 to 9,the foaming properties of the three proteins decreased first and then increased.Albumin and globulin had similar change trend of foam stability,which was opposite to that of foaming properties.The surface hydrophobicity and free sulfhydryl groups of globulin were higher than those of albumin and protein isolate(P<0.05).The secondary structures of the three proteins were mainly βcorner and β-folding.Sodium dodecyl sulfate polyacrylamide gel electrophoresis(SDS-PAGE)found that the subunits of the three proteins were widely distributed,with molecular weight ranging from 11 to 63 kDa,and the bands at 21 kDa and 22 kDa were the most intense.
文章编号:202402013     中图分类号:    文献标志码:
基金项目:塔里木大学南疆特色农产品深加工兵团重点实验室项目(AP1903)
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