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Small-Angle X-ray Scattering Study of the Effect of pH and Salts on 11S Soy Glycinin in the Freeze-Dried Powder and Solution States

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Anna Sokolova*†‡, Catherine S. Kealley†‡^§, Tracey Hanley†, Agata Rekas

and Elliot P. Gilbert*†

^† Bragg Institute, Australian Nuclear Science and Technology Organisation, PMB 1, Menai, NSW 2234, Australia

^‡ Food Futures Flagship, P.O. Box 52, North Ryde, NSW 2113, Australia

National Deuteration Facility, Australian Nuclear Science and Technology Organisation, PMB 1, Menai, NSW 2234, Australia

J. Agric. Food Chem., 2010, 58 (2), pp 967–974

DOI: 10.1021/jf902349q

Publication Date (Web): December 21, 2009

*To whom correspondence should be addressed. A.S.: e-mail, anna.sokolova@ansto.gov.au; phone, (+61) 2 9717 7288; fax, (+61) 2 9717 3606. E.P.G.: e-mail, elliot.gilbert@ansto.gov.au; phone, (+61) 2 9717 9470; fax, (+61) 2 9717 3606., §

Current address: Institute for Nanoscale Technology, University of Technology, Sydney, P.O. Box 123, Broadway, NSW 2007, Australia.

Section:

Food and Feed Chemistry

Abstract

The nanostructures from powders of native protein, glycinin, and corresponding solutions from which the powders have been formed, have been studied as a function of pH and 1 M salts using small-angle X-ray scattering. All powders showed Porod scattering with the exception of that prepared from the solution close to pI which displayed fractal behavior. Well-defined Bragg peaks in the powder scattering at pH 5, pH 7, and 1 M NaCl indicate the presence of long-range order. The scattering from solutions at pH 7, pH 9, and 1 M NaCl can be described well on the basis of particles derived from the known atomic structures of homohexameric glycinin. Extreme acidic (pH 2) and basic (pH 11) environments lead to the partial denaturation of glycinin. Decreasing the pH to 2 initiates dissociation of the hexameric structure, while increasing the pH to 11, as well as the presence of 1 M NaSCN, results in the formation of large unimodal particles. This is reflected by “featureless” SAXS patterns for both powders and solutions.

Keywords (keywords):

11S; glycinin; SAXS; protein; freeze-dried; pH; Hofmeister; powder

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This article has been cited by 1 ACS Journal articles (1 most recent appear below).

Effects of Thermal Denaturation on the Solid-State Structure and Molecular Mobility of Glycinin
Mickey G. Huson, Ekaterina V. Strounina, Catherine S. Kealley, Manoj K. Rout, Jeffrey S. Church, Ingrid A. M. Appelqvist, Michael J. Gidley, and Elliot P. Gilbert
Biomacromolecules2011 12 (6), 2092-2102
- Effects of Thermal Denaturation on the Solid-State Structure and Molecular Mobility of Glycinin
  Mickey G. Huson, Ekaterina V. Strounina, Catherine S. Kealley, Manoj K. Rout, Jeffrey S. Church, Ingrid A. M. Appelqvist, Michael J. Gidley, and Elliot P. Gilbert
  Biomacromolecules2011 12 (6), 2092-2102
  The effects of moisture and thermal denaturation on the solid-state structure and molecular mobility of soy glycinin powder were investigated using multiple techniques that probe over a range of length and time scales. In native glycinin, increased ...
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History

Published In Issue January 27, 2010
Article ASAPDecember 21, 2009
Received: July 09, 2009
Revised: October 29, 2009
Accepted: November 17, 2009

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Article

Small-Angle X-ray Scattering Study of the Effect of pH and Salts on 11S Soy Glycinin in the Freeze-Dried Powder and Solution States