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THE EFFECT OF WATER CONTENT UPON THE RATE OF HEAT DENATURATION OF CRYSTALLIZABLE EGG ALBUMIN

1. The denaturation rate of partially dried crystallizable egg albumin is greatly decreased by decreasing its water content. 2. The temperature of denaturation, defined as the temperature at which half of the protein becomes insoluble in distilled water after a definite time of heating, is a linear...

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Detalles Bibliográficos
Autor principal: Barker, H. Albert
Formato: Texto
Lenguaje:English
Publicado: The Rockefeller University Press 1933
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2141266/
https://www.ncbi.nlm.nih.gov/pubmed/19872759
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author Barker, H. Albert
author_facet Barker, H. Albert
author_sort Barker, H. Albert
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description 1. The denaturation rate of partially dried crystallizable egg albumin is greatly decreased by decreasing its water content. 2. The temperature of denaturation, defined as the temperature at which half of the protein becomes insoluble in distilled water after a definite time of heating, is a linear function of the relative humidity with which the protein is in equilibrium. 3. By applying the Arrhenius equation it is shown that the rate of heat denaturation at a given temperature is an exponential function of the relative humidity. 4. The application of the observed relations to the analysis of the mechanism of thermal death of microorganisms is suggested. 5. The water content of native and heat-denatured egg albumin is determined as a function of the relative humidity of water vapor. It is shown that the heat-denatured modification takes up approximately 80 per cent as much water at all relative humidities as does native egg albumin.
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spelling pubmed-21412662008-04-23 THE EFFECT OF WATER CONTENT UPON THE RATE OF HEAT DENATURATION OF CRYSTALLIZABLE EGG ALBUMIN Barker, H. Albert J Gen Physiol Article 1. The denaturation rate of partially dried crystallizable egg albumin is greatly decreased by decreasing its water content. 2. The temperature of denaturation, defined as the temperature at which half of the protein becomes insoluble in distilled water after a definite time of heating, is a linear function of the relative humidity with which the protein is in equilibrium. 3. By applying the Arrhenius equation it is shown that the rate of heat denaturation at a given temperature is an exponential function of the relative humidity. 4. The application of the observed relations to the analysis of the mechanism of thermal death of microorganisms is suggested. 5. The water content of native and heat-denatured egg albumin is determined as a function of the relative humidity of water vapor. It is shown that the heat-denatured modification takes up approximately 80 per cent as much water at all relative humidities as does native egg albumin. The Rockefeller University Press 1933-09-20 /pmc/articles/PMC2141266/ /pubmed/19872759 Text en Copyright © Copyright, 1933, by The Rockefeller Institute for Medical Research This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/4.0/).
spellingShingle Article
Barker, H. Albert
THE EFFECT OF WATER CONTENT UPON THE RATE OF HEAT DENATURATION OF CRYSTALLIZABLE EGG ALBUMIN
title THE EFFECT OF WATER CONTENT UPON THE RATE OF HEAT DENATURATION OF CRYSTALLIZABLE EGG ALBUMIN
title_full THE EFFECT OF WATER CONTENT UPON THE RATE OF HEAT DENATURATION OF CRYSTALLIZABLE EGG ALBUMIN
title_fullStr THE EFFECT OF WATER CONTENT UPON THE RATE OF HEAT DENATURATION OF CRYSTALLIZABLE EGG ALBUMIN
title_full_unstemmed THE EFFECT OF WATER CONTENT UPON THE RATE OF HEAT DENATURATION OF CRYSTALLIZABLE EGG ALBUMIN
title_short THE EFFECT OF WATER CONTENT UPON THE RATE OF HEAT DENATURATION OF CRYSTALLIZABLE EGG ALBUMIN
title_sort effect of water content upon the rate of heat denaturation of crystallizable egg albumin
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2141266/
https://www.ncbi.nlm.nih.gov/pubmed/19872759
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