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

被引：29

作者：

Berecz, Bernadett ^{[1
]}

Mills, E. N. Clare ^{[2
]}

Tamas, Laszlo ^{[1
]}

Lang, Ferenc ^{[1
]}

Shewry, Peter R. ^{[3
]}

Mackie, Alan R. ^{[2
]}

机构：

[1] Eotvos Lorand Univ, Dept Plant Physiol & Mol Plant Biol, H-1117 Budapest, Hungary

[2] Inst Food Res, Colney NR4 7UA, Norfolk, England

[3] Rothamsted Res, Crop Performance & Improvement, Harpenden AL5 2JQ, Herts, England

来源：

JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY | 2010年 / 58卷 / 10期

基金：

英国生物技术与生命科学研究理事会;

关键词：

Helianthus annuus L; sunflower; 2S albumin; nsLTP; SFA8; Alb1; Alb2; interfacial rheology; emulsion; circular dichroism spectroscopy; heating; SEED STORAGE PROTEINS; METHIONINE-RICH; BARLEY; SECONDARY; SEQUENCE; BINDING;

D O I：

10.1021/jf100554d

中图分类号：

S [农业科学];

学科分类号：

09 ;

摘要：

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 A1b2 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.

引用

页码：6490 / 6497

页数：8

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