CHEMICAL AND CONFORMATIONAL CHANGES OF OVALBUMIN DUE TO THE MAILLARD REACTION

CHEMICAL AND CONFORMATIONAL CHANGES OF OVALBUMIN DUE TO THE MAILLARD REACTION ABSTRACT Ovalbumin freeze‐dried with or without the addition of glucose was stored at 50°C and 65% relative humidity to study the effect of the Maillard reaction on the chemical properties and conformational composition of ovalbumin. About 70% of available lysine in ovalbumin reacted with glucose before denaturation. The solubility and heat stability of the protein‐glucose complex increased with the addition of the hydrophilic group and the repulsion force due to changes of such charged groups. During prolonged storage the changes of charge balance promoted the unfolding of ovalbumin at the expense of α‐helix without the loss of β‐structure. Insolubilization of the complex was accompanied by the high loss of lysine and arginine residues, brown color development and the formation of aggregates which were not cleaved by SDS plus 2‐mercaptoethanol. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Journal of Food Processing and Preservation Wiley

CHEMICAL AND CONFORMATIONAL CHANGES OF OVALBUMIN DUE TO THE MAILLARD REACTION

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Publisher
Wiley
Copyright
Copyright © 1980 Wiley Subscription Services, Inc., A Wiley Company
ISSN
0145-8892
eISSN
1745-4549
D.O.I.
10.1111/j.1745-4549.1980.tb00587.x
Publisher site
See Article on Publisher Site

Abstract

ABSTRACT Ovalbumin freeze‐dried with or without the addition of glucose was stored at 50°C and 65% relative humidity to study the effect of the Maillard reaction on the chemical properties and conformational composition of ovalbumin. About 70% of available lysine in ovalbumin reacted with glucose before denaturation. The solubility and heat stability of the protein‐glucose complex increased with the addition of the hydrophilic group and the repulsion force due to changes of such charged groups. During prolonged storage the changes of charge balance promoted the unfolding of ovalbumin at the expense of α‐helix without the loss of β‐structure. Insolubilization of the complex was accompanied by the high loss of lysine and arginine residues, brown color development and the formation of aggregates which were not cleaved by SDS plus 2‐mercaptoethanol.

Journal

Journal of Food Processing and PreservationWiley

Published: Jan 1, 1980

References

  • Effect of Maillard condensation with D‐glucose on the heat stability of bovine serum albumin
    MORALES, MORALES; DILL, DILL; LANDMANN, LANDMANN
  • Conformation of proteins
    TIMASHEFF, TIMASHEFF; GORBUNOFF, GORBUNOFF
  • Optical rotatory dispersion of egg proteins. I. Ovalbumin, conalbumin, ovomucoid and lysozyme
    TOMIMATSU, TOMIMATSU; GAFFIELD, GAFFIELD

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