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中国精品科技期刊2020

低pH条件下大豆蛋白7S和11S组分的表面特性

徐红华, 董世荣, 何雪飞

徐红华, 董世荣, 何雪飞. 低pH条件下大豆蛋白7S和11S组分的表面特性[J]. 食品工业科技, 2015, (15): 92-95. DOI: 10.13386/j.issn1002-0306.2015.15.011
引用本文: 徐红华, 董世荣, 何雪飞. 低pH条件下大豆蛋白7S和11S组分的表面特性[J]. 食品工业科技, 2015, (15): 92-95. DOI: 10.13386/j.issn1002-0306.2015.15.011
XU Hong-hua, DONG Shi-rong, HE Xue-fei. Superficial properties of soy protein 7S and 11S at low pH[J]. Science and Technology of Food Industry, 2015, (15): 92-95. DOI: 10.13386/j.issn1002-0306.2015.15.011
Citation: XU Hong-hua, DONG Shi-rong, HE Xue-fei. Superficial properties of soy protein 7S and 11S at low pH[J]. Science and Technology of Food Industry, 2015, (15): 92-95. DOI: 10.13386/j.issn1002-0306.2015.15.011

低pH条件下大豆蛋白7S和11S组分的表面特性

基金项目: 

国家自然基金项目(31471682); 黑龙江省教育厅青年学术骨干项目(1155G10);

详细信息
    作者简介:

    徐红华(1969-),女,博士,教授,从事食品蛋白质及营养的教学和研究,E-mail:dongshirong118@126.com。;

  • 中图分类号: TS201.2

Superficial properties of soy protein 7S and 11S at low pH

  • 摘要: 本文采用7S形成纤维聚合结构的制备条件,研究低p H条件下长时间热处理对大豆蛋白7S和11S(包括酸性亚基和碱性亚基)乳化性和起泡性的影响。结果发现,低p H条件下长时间热处理的聚合手段,可以显著(p<0.05)改善不同大豆蛋白组分的起泡性,但对乳化性没有明显的改善作用,甚至对乳化稳定性有降低作用,这种改善程度与是否形成纤维聚合结构无关。与p H7.0条件下的热处理手段相比,低p H条件下长时间热处理的聚合手段能够使大豆蛋白7S和11S表面疏水性显著增加,这种特殊的结构变化更有力于提高起泡性能。因此,在低p H条件下长时间热处理后,7S和11S具有较高的表面疏水性和较好的起泡性能。 
    Abstract: Based on the conditions of 7S forming fibril,the emulsifying and foaming properties of soy protein 7S and11S( including acidic and basic subunits) was investigated under prolonged heat treatment at low p H. The results showed that the foaming properties of different soy protein components were significantly improved( p < 0.05),while the emulsification was not sigificantly regular changed even the emulsion stability was reduced by heating treatment at low p H. There were no relationships between the fibrillar aggregates and modified properties.Compared with the heating treatment at p H7.0,the surface hydrophobicities of soy protein 7S and 11 S were significantly increased under heating treatment at low p H,and the special structure with high surface hydrophobicities was benefit for improving foaming properties of soy protein. Then,the surface hydrophobicities and foaming properties of 7S and 11 S were improved significantly after prolonged heat treatment at low p H.
  • [1] 赵新淮,徐红华,姜毓君.食品蛋白质结构、性质与功能[M].北京:科学出版社,2009:1-485.
    [2]

    Wang J M,Yang X Q,Yin S W,et al.Growth Kinetics of Amyloid-like Fibrils Derived from Individual Subunits of Soyβ-Conglycinin[J].Journal of Agriculture and Food Chemistry,2011,59:11270-11277.

    [3]

    Tang C H,Wang C S.Formation and Characterization of Amyloid-like Fibrils from Soyβ-Conglycinin and Glycinin[J].Journal of Agricultural and Food Chemistry,2010,58:11058-11066.

    [4]

    Tang C H,Wang S S,Huang Q R.Improvement of heatinduced fibril assembly of soyβ-conglycinin(7S Globulins)at p H2.0 through electrostatic screening[J].Food Research International,2012,l46:229-236.

    [5]

    Nagano T,Hirotsuka M,Mori H,et al.Dynamic viscoelastic study on the gelation of 7S globulin from soybeans[J].Journal of Agricultural and Food Chemistry,1992,40(6):941-944.

    [6]

    Mo X Q,Zhong Z K,Wang D H,et al.Soybean Glycinin Subnits Charaterizztion of Physicochemical and Adhesion Properties[J].Journal of Agriculture and Food Chemistry,2006,54:7589-7593.

    [7]

    Hayakawa S,Nakai S.Relationships of hydrophobicity and net charge to the solubility of milk and soy proteins[J].Journal of Food Science,1985,50:486-491.

    [8]

    Stieger M,Richering W,Pedersen J S,et al.Small-angle neutron scattering study of structural changes in temperature sensitive microgel colloids[J].The Journal of Chemical Physics,2004,120:6197-6206.

    [9]

    Pearce K N,Kinsella J E.Emulsifying properties of proteins:evaluation of a turbidimetric technique[J].Journal of Agricultural and Food Chemistry,1978,6:716-723.

    [10]

    Agyare K K,Kwaku A,Xiong Y L.Emulsifying and foaming properties of transglutaminase-treated wheat gluten hydrolysate as influenced by p H,temperature and salt[J].Food Hydrocolloids,2009,23:72-81.

    [11]

    Akkermans C,Vader Goot A J,Venema P,et al.Micrometer-Sized Fibrillar Protein Aggregates from Soy Glycinin and Soy Protein Isolate[J].Journal of Agricultural and Food Chemistry,2007,55:9877-9882.

    [12]

    María J Martinez,Víctor M.Pizones Ruiz-Henestrosa,Cecilio Carrera Sánchez,et al.Foaming and surface prope rties of casein glycomacrope ptideegelatin mixtures as affected by their interactions in the aqueous phase[J].Food Hydrocolloids,2013,33:48-57.

    [13] 王金梅.大豆蛋白热聚集行为及界面、乳化性质研究[D].广州:华南理工大学,2012,1-24.
    [14]

    Zhang T,Jiang B,Mu W.M.,et al.Emulsifying properties of chickpea protein isolates:Influence of p H and Na Cl[J].Food Hydrocolloids,2009,23:146-152.

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出版历程
  • 收稿日期:  2014-10-20

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