title: The aggregation behavior and interactions of yak milk protein under thermal treatment.
abstract: The aggregation behavior and interactions of yak milk protein were investigated after heat treatments. Skim yak milk was heated at temperatures in the range of 65 to 95°C for 10 min. The results showed that the whey proteins in yak milk were denatured after heat treatment, especially at temperatures higher than 85°C. Sodium dodecyl sulfate-PAGE analysis indicated that heat treatment induced milk protein denaturation accompanied with aggregation to a certain extent. When the heating temperature was 75 and 85°C, the aggregation behavior of yak milk proteins was almost completely due to the formation of disulfide bonds, whereas denatured α-lactalbumin and β-lactoglobulin interacted with κ-casein. When yak milk was heated at 85 and 95°C, other noncovalent interactions were found between proteins including hydrophobic interactions. The particle size distributions and microstructures demonstrated that the heat stability of yak milk proteins was significantly lowered by heat treatment. When yak milk was heated at 65 and 75°C, no obvious changes were found in the particle size distribution and microstructures in yak milk. When the temperature was 85 and 95°C, the particle size distribution shifted to larger size trend and aggregates were visible in the heated yak milk.
authors.affiliation: Beijing Advanced Innovation Center for Food Nutrition and Human Health, China Agricultural University, Beijing 100083, China; Key Laboratory of Functional Dairy, Ministry of Education, College of Food Science and Nutritional Engineering, China Agricultural University, Beijing 100083, China.
authors.forename: T T
authors.initials: TT
authors.lastname: Wang
authors.affiliation: Key Laboratory of Functional Dairy, Ministry of Education, College of Food Science and Nutritional Engineering, China Agricultural University, Beijing 100083, China.
authors.forename: Z W
authors.initials: ZW
authors.lastname: Guo
authors.affiliation: Key Laboratory of Functional Dairy, Ministry of Education, College of Food Science and Nutritional Engineering, China Agricultural University, Beijing 100083, China.
authors.forename: Z P
authors.initials: ZP
authors.lastname: Liu
authors.affiliation: Key Laboratory of Functional Dairy, Ministry of Education, College of Food Science and Nutritional Engineering, China Agricultural University, Beijing 100083, China.
authors.forename: Q Y
authors.initials: QY
authors.lastname: Feng
authors.affiliation: Key Laboratory of Functional Dairy, Ministry of Education, College of Food Science and Nutritional Engineering, China Agricultural University, Beijing 100083, China.
authors.forename: X L
authors.initials: XL
authors.lastname: Wang
authors.affiliation: Beijing Advanced Innovation Center for Food Nutrition and Human Health, China Agricultural University, Beijing 100083, China; Key Laboratory of Functional Dairy, Ministry of Education, College of Food Science and Nutritional Engineering, China Agricultural University, Beijing 100083, China.
authors.forename: Q
authors.initials: Q
authors.lastname: Tian
authors.affiliation: Beijing Advanced Innovation Center for Food Nutrition and Human Health, China Agricultural University, Beijing 100083, China; Key Laboratory of Functional Dairy, Ministry of Education, College of Food Science and Nutritional Engineering, China Agricultural University, Beijing 100083, China.
authors.forename: F Z
authors.initials: FZ
authors.lastname: Ren
authors.affiliation: Beijing Advanced Innovation Center for Food Nutrition and Human Health, China Agricultural University, Beijing 100083, China; Key Laboratory of Functional Dairy, Ministry of Education, College of Food Science and Nutritional Engineering, China Agricultural University, Beijing 100083, China. Electronic address: maoxueying@cau.edu.cn.
authors.forename: X Y
authors.initials: XY
authors.lastname: Mao
mesh_terms: D000818:Animals; D002364:Caseins / Q000032:analysis; D002417:Cattle; D004220:Disulfides / Q000737:chemistry; D004355:Drug Stability; D004591:Electrophoresis, Polyacrylamide Gel; D005260:Female; D006358:Hot Temperature; D007768:Lactalbumin / Q000737:chemistry; D007782:Lactoglobulins / Q000737:chemistry; D008892:Milk / Q000737:chemistry; D008894:Milk Proteins / Q000737:chemistry*; D010316:Particle Size; D066329:Protein Aggregates; D011489:Protein Denaturation; D000067816:Whey Proteins / Q000737:chemistry
chemical_list: D002364:Caseins; D004220:Disulfides; D007782:Lactoglobulins; D008894:Milk Proteins; D066329:Protein Aggregates; D000067816:Whey Proteins; D007768:Lactalbumin
keywords: SDS-PAGE; disulfide bonds; hydrophobicity; thermal aggregation; yak milk protein