Structural Stability and Surface Activity of Sunflower 2S Albumins and Nonspecific Lipid Transfer Protein

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• 作者：Bernadett Berecz ; E. N. Clare Mills ; Lszl Tams ; Ferenc Lng ; Peter R. Shewry ; Alan R. Mackie
• 刊名：Journal of Agricultural and Food Chemistry
• 出版年：2010
• 出版时间：May 26, 2010
• 年：2010
• 卷：58
• 期：10
• 页码：6490-6497
• 全文大小：868K
• 年卷期：v.58,no.10(May 26, 2010)
• ISSN：1520-5118

文摘

The structural and interfacial properties of five different fractions of sunflower (Helianthus annuus L.) seed storage proteins were studied. The fractions comprised lipid transfer protein (LTP), the methionine-rich 2S albumin SFA8 (sunflower albumin 8), and three mixtures of non-methionine-rich 2S albumins called Alb1 and Alb2 proteins (sunflower albumins 1 and 2). Heating affected all of the proteins studied, with SFA8 and LTP becoming more surface active than the native proteins after heating and cooling. LTP appeared to be less thermostable than homologous LTPs from other plant species. SFA8 generated the greatest elastic modulus and formed the most stable emulsions, whereas LTP showed poorer emulsification properties. The mixed 2S albumin fractions showed moderate levels of surface activity but had the poorest emulsification properties among the proteins studied.