Document Detail

Effect of Disulfide Interactions and Hydrolysis on the Thermal Aggregation of β-Lactoglobulin.
MedLine Citation:
PMID:  20812724     Owner:  NLM     Status:  In-Data-Review    
The roles of sulfhydryl/disulfide interactions and acid/pepsin hydrolysis on β-lactoglobulin (β-lg) thermal aggregation at acidic pH 3.35 and 2 were studied using rheology, sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE), transmission electron microscopy (TEM), and Western blotting. Pepsin promoted additional hydrolysis compared to the acid-hydrolyzed control sample based on a 12% increase in free amino groups. Hydrolysis with pepsin also resulted in an increase in the apparent viscosity by 2 logs upon heating 8% β-lg solutions at pH 3.35. Seemingly, hydrolysis promoted thermal aggregation of β-lg, correlating well with viscosity increases. Large microgels were observed in heated pepsin hydrolysates using TEM, supporting the increased viscosities of these dispersions. During thermal aggregation (85 °C, 3 h) of β-lg at pH 3.35, beyond the existence of limited disulfide interactions, acid hydrolysis and noncovalent interactions more likely play a crucial role in defining the functionality of acidified powdered modified whey ingredients.
Prashant Mudgal; Christopher R Daubert; Debra A Clare; E Allen Foegeding
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Publication Detail:
Type:  Journal Article     Date:  2010-09-02
Journal Detail:
Title:  Journal of agricultural and food chemistry     Volume:  59     ISSN:  1520-5118     ISO Abbreviation:  J. Agric. Food Chem.     Publication Date:  2011 Mar 
Date Detail:
Created Date:  2011-03-02     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  0374755     Medline TA:  J Agric Food Chem     Country:  United States    
Other Details:
Languages:  eng     Pagination:  1491-7     Citation Subset:  IM    
Department of Food, Bioprocessing and Nutrition Sciences, Schaub Hall, Dan Allen Drive, North Carolina State University , Raleigh, North Carolina 27695-7624, United States.
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