Document Detail


Deglycosylation of ovalbumin prohibits formation of a heat-stable conformer.
MedLine Citation:
PMID:  17154314     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
To study the influence of the carbohydrate-moiety of ovalbumin on the formation of the heat-stable conformer S-ovalbumin, ovalbumin is deglycosylated with PNGase-F under native conditions. Although the enzymatic deglycosylation procedure resulted in a complete loss of the ability to bind to Concavalin A column-material, only in about 50% the proteins lost their complete carbohydrate moiety, as demonstrated by mass spectrometry and size exclusion chromatography. Thermal stability and conformational changes were determined using circular dichroism and differential scanning calorimetry and demonstrated at ambient temperature no conformational changes due to the deglycosylation. Also the denaturation temperature of the processed proteins remained the same (77.4 +/- 0.4 degrees C). After heat treatment of the processed protein at 55 degrees C and pH 9.9 for 72 h, the condition that converts native ovalbumin into the heat-stable conformer (S-ovalbumin), only the material with the intact carbohydrate moiety forms this heat-stable conformer. The material that effectively lost its carbohydrate moiety appeared fully denatured and aggregated due to these processing conditions. These results indicate that the PNGase-F treatment of ovalbumin prohibits the formation and stabilization of the heat-stable conformer S-ovalbumin. Since S-ovalbumin in egg protein samples is known to affect functional properties, this work illustrates a potential route to control the quality of egg protein ingredients.
Authors:
Jolan de Groot; Hans A Kosters; Harmen H J de Jongh
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Publication Detail:
Type:  Journal Article    
Journal Detail:
Title:  Biotechnology and bioengineering     Volume:  97     ISSN:  0006-3592     ISO Abbreviation:  Biotechnol. Bioeng.     Publication Date:  2007 Jul 
Date Detail:
Created Date:  2007-05-30     Completed Date:  2007-07-17     Revised Date:  2008-11-21    
Medline Journal Info:
Nlm Unique ID:  7502021     Medline TA:  Biotechnol Bioeng     Country:  United States    
Other Details:
Languages:  eng     Pagination:  735-41     Citation Subset:  IM    
Copyright Information:
(c) 2006 Wiley Periodicals, Inc.
Affiliation:
Wageningen Centre for Food Sciences, P.O. Box 557, 6700 AN Wageningen, The Netherlands.
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MeSH Terms
Descriptor/Qualifier:
Animals
Chickens
Chromatography, Gel
Circular Dichroism
Enzyme Stability
Glycosylation
Hot Temperature
Isoelectric Focusing
Mass Spectrometry
Molecular Weight
Ovalbumin / chemistry*,  metabolism
Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase / metabolism
Protein Conformation*
Spectrometry, Fluorescence
Chemical
Reg. No./Substance:
9006-59-1/Ovalbumin; EC 3.5.1.52/Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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