作者
Asghar Taheri-Kafrani, Jean-Charles Gaudin, Hanitra Rabesona, Claudia Nioi, Deepesh Agarwal, Martine Drouet, Jean-Marc Chobert, Abdol-Khalegh Bordbar, Thomas Haertle
发表日期
2009/6/10
期刊
Journal of Agricultural and Food chemistry
卷号
57
期号
11
页码范围
4974-4982
出版商
American Chemical Society
简介
β-Lactoglobulin (β-LG) is one of the cow's major milk proteins and the most abundant whey protein. This globular protein of about 18 kDa is folded, forming a β-barrel (or calyx) structure. This structure is stabilized by two disulfide bonds and can be altered by heating above 65 °C. β-LG is also one of the major allergens in milk. Heating is one of the most common technologic treatments applied during many milk transformations. During heating in the presence of reducing sugars, β-LG is also submitted to the Maillard reaction, which at the first stage consists of the covalent fixation of sugars on the ε-amino groups of lysyl residues. The following steps are condensation and polymerization reactions leading to the formation of melanoidins (brown pigments). Despite the frequency of use of heating during milk transformation, the effects of heat-induced denaturation and of glycation of β-LG on its recognition by IgE from cow …
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