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

doi:10.1021/jf100554d

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 journal › Article › peer-review

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. © 2010 American Chemical Society.

Original language	English
Pages (from-to)	6490-6497
Number of pages	7
Journal	Journal of agricultural and food chemistry
Volume	58
Issue number	10
DOIs	https://doi.org/10.1021/jf100554d
Publication status	Published - 26 May 2010

Keywords

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

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@article{71e6ab63fbfb4b588f3e1ba0b20269e1,

title = "Structural stability and surface activity of sunflower 2S albumins and nonspecific lipid transfer protein",

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. {\textcopyright} 2010 American Chemical Society.",

keywords = "2S albumin, Alb1, Alb2, Circular dichroism spectroscopy, Emulsion, Heating, Helianthus annuus L., Interfacial rheology, NsLTP, SFA8, Sunflower",

author = "Bernadett Berecz and Mills, {E. N Clare} and L{\'a}szl{\'o} Tam{\'a}s and Ferenc L{\'a}ng and Shewry, {Peter R.} and MacKie, {Alan R.}",

year = "2010",

month = may,

day = "26",

doi = "10.1021/jf100554d",

language = "English",

volume = "58",

pages = "6490--6497",

journal = "Journal of agricultural and food chemistry",

issn = "0021-8561",

publisher = "American Chemical Society",

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TY - JOUR

T1 - Structural stability and surface activity of sunflower 2S albumins and nonspecific lipid transfer protein

AU - Berecz, Bernadett

AU - Mills, E. N Clare

AU - Tamás, László

AU - Láng, Ferenc

AU - Shewry, Peter R.

AU - MacKie, Alan R.

PY - 2010/5/26

Y1 - 2010/5/26

N2 - 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. © 2010 American Chemical Society.

AB - 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. © 2010 American Chemical Society.

KW - 2S albumin

KW - Alb1

KW - Alb2

KW - Circular dichroism spectroscopy

KW - Emulsion

KW - Heating

KW - Helianthus annuus L.

KW - Interfacial rheology

KW - NsLTP

KW - SFA8

KW - Sunflower

U2 - 10.1021/jf100554d

DO - 10.1021/jf100554d

M3 - Article

C2 - 20429585

SN - 0021-8561

VL - 58

SP - 6490

EP - 6497

JO - Journal of agricultural and food chemistry

JF - Journal of agricultural and food chemistry

IS - 10

ER -

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

Abstract

Keywords

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