Document Detail

Consequential secondary structure alterations and aggregation during prolonged casein glycation.
MedLine Citation:
PMID:  23408088     Owner:  NLM     Status:  Publisher    
Non-enzymatic glycosylation (glycation) of casein is a process used not just to ameliorate the quality of dairy products but also to increase the shelf life of canned foods, including baby milk supplements. Incubation of κ-casein with reducing sugars for 15 days at physiological temperature showed the formation of a molten globule state at day 9 and 12 during fructation and glucation respectively. This state exhibits substantial secondary structure and maximum ANS binding. Later on, glycation resulted in the formation of aggregates at day 12 in presence of fructose and day 15 in presence of glucose. Aggregates possess extensive β-sheet structure as revealed by far-UV CD and FTIR. These aggregates showed altered tryptophan environment, decrease ANS binding relative to molten globule state and increase in Thioflavin T fluorescence. Aggregates were also accompanied by the accumulation of AGEs, indicative of structural damage to the protein and formation of potentially harmful species at the physiological level. Fructose was more reactive than glucose and thus caused early and significant changes in the protein. From our studies, we conclude that controlling the extent of the Maillard reaction in the food industry is essential to counter its negative effects and expand its safety spectrum.
Supriya Jindal; Aabgeena Naeem
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Publication Detail:
Type:  JOURNAL ARTICLE     Date:  2013-2-14
Journal Detail:
Title:  Journal of fluorescence     Volume:  -     ISSN:  1573-4994     ISO Abbreviation:  J Fluoresc     Publication Date:  2013 Feb 
Date Detail:
Created Date:  2013-2-14     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  9201341     Medline TA:  J Fluoresc     Country:  -    
Other Details:
Languages:  ENG     Pagination:  -     Citation Subset:  -    
Department of Biochemistry, Faculty of Life Science, AMU, Aligarh, 202002, India.
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