ISSN:
1750-3841
Source:
Blackwell Publishing Journal Backfiles 1879-2005
Topics:
Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition
,
Process Engineering, Biotechnology, Nutrition Technology
Notes:
αs-1Casein was polymerized in the presence of sodium hypochlorite (NaOCl). The polymerization was suppressed by succinylation of the protein. Dityrosine and α-aminoadipic acid were detected in the hydrolysate of the reacted proteins. A carbonyl group was detected in the reaction product of acetyl lysine methylester and NaOCl. The Schiff base formation between lysine and a-aminoadipic δ-semialdehyde residues, and dityrosine formation may clarify the mechanism of polymerization. The chemical modification of proteins by NaOCl is expected to be useful for improving the functional properties of food proteins, since polymerization by NaOCl could occur under mild conditions (NaOCl cone, 〈0.05%; time, 〈5 min; at 37°C and pH 7-9).
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1111/j.1365-2621.1985.tb10578.x
