Distinction of different heat-treated bovine milks by native-PAGE fingerprinting of their whey proteins

作者：Lin Suju; Sun Jing; Cao Dongdong; Cao Jiankang; Jiang Weibo^*

来源：Food Chemistry, 2010, 121(3): 803-808.

DOI：10.1016/j.foodchem.2009.12.088

• Heat treatment
• Milk
• Native-PAGE
• Whey proteins

Native-PAGE (polyacrylamide gel electrophoresis) was used for the simultaneous qualitative and quantitative analysis of whey proteins of raw, commercial and laboratory heat-treated bovine milks. Four whey protein bands, including beta-lactoglobulin variants (beta-LG A and B), could be distinctively separated in the gel. The results showed that levels of the major whey proteins were reduced by less than 23% in the pasteurized milks and by more than 85% in the UHT milks as compared with raw milk. The alpha-lactalbumin (alpha-LA) exhibited the strongest heat-tolerance: about 32% of it remained in its native state after the milk was heated at 100 degrees C for 10 min. About 42% of beta-LG A and 53% of beta-LG B were lost after the milk was heated at 75 degrees C for 30 min. Blood serum albumin (BSA) was lost almost completely when the milk at pH 5.0 was heated at a temperature of 75 degrees C or higher. The beta-LcA and beta-LGB were much more stable at low pH than in neutral conditions.

• 出版日期2010-8-1
• 单位中国农业大学