Hydrophobic probe binding of β-lactoglobulin in the native and molten globule state induced by high pressure as affected by pH, KIO3 and N-ethylmaleimide

Jian Yang, Joseph R. Powers, Stephanie Clark, A. Dunker, Barry G. Swanson

Research output: Contribution to journalArticle

27 Citations (Scopus)

Abstract

High hydrostatic pressure (HHP) at 500 MPa and 50°C induces β-LG into the molten globule state. Retinol, cis-parinaric acid (CPA), and 1-anilino-naphthalene-8-sulfonate (ANS) fluorescence from pH 2.5 to 10.5 in the presence of the native and molten globule states of β-LG indicate that retinol binds to β-LG in the calyx, CPA at the surface hydrophobic site, and ANS in multiple hydrophobic sites. HHP treatment results in a decrease of β-LG affinity for retinol and CPA, suggesting conformational changes in the calyx and surface hydrophobic site of β-LG during HHP treatment. β-LG treated by HHP in the presence of N-ethylmaleimide (NEM) retains retinol affinity, suggesting that NEM protects the calyx conformation of β-LG during HHP treatment. HHP treatment of β-LG in the presence of KIO3 exhibits a great decrease of CPA affinity compared to HHP-treated β-LG in the absence of KIO3, suggesting the formation of non-native disulfide bonding at the CPA binding site.

Original languageEnglish (US)
Pages (from-to)5207-5214
Number of pages8
JournalJournal of Agricultural and Food Chemistry
Volume50
Issue number18
DOIs
StatePublished - Aug 28 2002
Externally publishedYes

Fingerprint

lactoglobulins
Lactoglobulins
Hydrostatic Pressure
Ethylmaleimide
Hydrostatic pressure
probes (equipment)
high pressure treatment
Molten materials
vitamin A
Pressure
calyx
Vitamin A
acids
naphthalene
sulfonates
sulfides
binding sites
fluorescence
Disulfides
Conformations

Keywords

  • β-Lactoglobulin
  • 1-anilinonaphthalene-8-sulfonate
  • cis-parinaric acid
  • High pressure
  • KIO
  • Molten globule
  • N-ethylmaleimide
  • Retinol

ASJC Scopus subject areas

  • Agricultural and Biological Sciences (miscellaneous)
  • Food Science
  • Chemistry (miscellaneous)

Cite this

Hydrophobic probe binding of β-lactoglobulin in the native and molten globule state induced by high pressure as affected by pH, KIO3 and N-ethylmaleimide. / Yang, Jian; Powers, Joseph R.; Clark, Stephanie; Dunker, A.; Swanson, Barry G.

In: Journal of Agricultural and Food Chemistry, Vol. 50, No. 18, 28.08.2002, p. 5207-5214.

Research output: Contribution to journalArticle

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abstract = "High hydrostatic pressure (HHP) at 500 MPa and 50°C induces β-LG into the molten globule state. Retinol, cis-parinaric acid (CPA), and 1-anilino-naphthalene-8-sulfonate (ANS) fluorescence from pH 2.5 to 10.5 in the presence of the native and molten globule states of β-LG indicate that retinol binds to β-LG in the calyx, CPA at the surface hydrophobic site, and ANS in multiple hydrophobic sites. HHP treatment results in a decrease of β-LG affinity for retinol and CPA, suggesting conformational changes in the calyx and surface hydrophobic site of β-LG during HHP treatment. β-LG treated by HHP in the presence of N-ethylmaleimide (NEM) retains retinol affinity, suggesting that NEM protects the calyx conformation of β-LG during HHP treatment. HHP treatment of β-LG in the presence of KIO3 exhibits a great decrease of CPA affinity compared to HHP-treated β-LG in the absence of KIO3, suggesting the formation of non-native disulfide bonding at the CPA binding site.",
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