食品科学 ›› 2017, Vol. 38 ›› Issue (17): 36-41.doi: 10.7506/spkx1002-6630-201717007

• 基础研究 • 上一篇    下一篇

新疆莎车1号扁桃仁2S-清蛋白的纯化及特性研究

李述刚1,陆健康2,*,王 萍2,马美湖3,*   

  1. 1.湖北工业大学生物工程与食品学院,湖北工业发酵协同创新中心,菲利普斯亲水胶体研究中心,湖北 武汉 430068;2.塔里木大学生命科学学院,南疆特色农产品深加工兵团重点实验室,新疆 阿拉尔 843300;3.华中农业大学食品科学技术学院,湖北 武汉 430070
  • 出版日期:2017-09-15 发布日期:2017-09-12
  • 基金资助:
    国家自然科学基金青年科学基金项目(31401644);兵团中青年创新领军人才项目(2016BC001)

Purification and Characteristics of 2S-Albumin in Shache No. 1 Almond from Xinjiang

LI Shugang1, LU Jiankang2,*, WANG Ping2, MA Meihu3,*   

  1. 1. Glyn O. Phillips Hydrocolloid Research Center, Hubei Collaborative Innovation Center for Industrial Fermentation, School of Biological Engineering and Food, Hubei University of Technology, Wuhan 430068, China; 2. Production & Construction Group Key Laboratory of Special Agricultural Products Further Processing in Southern Xinjiang, College of Life Sciences, Tarim University, Alar 843300, China;3. College of Food Science and Technology, Huazhong Agricultural University, Wuhan 430070, China
  • Online:2017-09-15 Published:2017-09-12

摘要: 清蛋白是扁桃种仁中主要蛋白质,为揭示扁桃仁主要蛋白质组成及结构特性,以新疆莎车1号(SC-1)扁桃仁为研究对象,对其种仁中2S-清蛋白进行分离纯化和结构特性研究,即经有机溶剂多次沉淀提取,获得扁桃仁清蛋白的粗提物,再经Q Sepharose FF分离纯化,获得扁桃仁2S-清蛋白。经高效液相色谱-质谱联用分析表明,纯化后的扁桃仁2S-清蛋白准确分子质量为31.40 kD,其在十二烷基硫酸钠-聚丙烯酰胺凝胶电泳结果中显示为18.0 kD和19.5 kD 2 个条带,表明其由两个不同的亚基通过二硫键结合而成。扁桃仁2S-清蛋白中谷氨酸(Glu)、天冬氨酸(Asp)和精氨酸(Arg)的含量最高;其二级结构中主要为β-折叠,占65.9%;扁桃仁2S-清蛋白羰基含量为4.45 nmol/mg、活性巯基含量为39.95 μmol/g、总巯基含量为57.11 μmol/g、表面疏水性为23.45 μg;变性温度为43.3 ℃。研究结果可为新疆扁桃仁的开发利用提供理论依据。

关键词: 扁桃仁, 2S-清蛋白, 纯化, 结构特性

Abstract: Albumin is the major protein in almond. In this experiment, we purified and structurally characterized 2S-albumin from Shache No.1 almond (SC-1) from Xinjiang. Crude albumin extract was obtained from almond by repeated precipitation with organic solvents and then fractionated chromatographically on Q Sepharose FF to obtain 2S-albumin. By HPLC-MS analysis, the accurate molecular mass of 2S-albumin was determined to be 31.40 kD, which was separated into two bands (18.0 and 19.5 kD) in sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE), indicating that it was composed of two distinct subunits connected through disulfide bonds. In 2S-albumin, the contents of glutamic acid, aspartic acid and arginine residues were relatively high, and its dominant secondary structure was β-sheet (65.9%). The carbonyl group content of 2S-albumin was 4.45 nmol/mg, the active thiol group content was 39.95 μmol/g, the total thiol group content was 57.11 μmol/g, the surface hydrophobicity was 23.45 μg, and the denaturation temperature was 43.3 ℃. These results can provide a theoretical support for the development and utilization of Xinjiang grown almond.

Key words: almond, 2S-albumin, purification, structure characteristics

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