Structural stability and surface activity of sunflower 2S albumins and nonspecific lipid transfer protein

Bernadett Berecz, E. N.Clare Mills, László Tamás, Ferenc Láng, Peter R. Shewry, Alan R. MacKie

Research output: Contribution to journalArticle

19 Citations (Scopus)

Abstract

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.

Original languageEnglish
Pages (from-to)6490-6497
Number of pages8
JournalJournal of Agricultural and Food Chemistry
Volume58
Issue number10
DOIs
Publication statusPublished - May 26 2010

Keywords

  • 2S albumin
  • Alb1
  • Alb2
  • Circular dichroism spectroscopy
  • Emulsion
  • Heating
  • Helianthus annuus L.
  • Interfacial rheology
  • NsLTP
  • SFA8
  • Sunflower

ASJC Scopus subject areas

  • Chemistry(all)
  • Agricultural and Biological Sciences(all)

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