期刊
FOOD HYDROCOLLOIDS
卷 106, 期 -, 页码 -出版社
ELSEVIER SCI LTD
DOI: 10.1016/j.foodhyd.2020.105892
关键词
Glycation; Maillard reaction; Bovine serum albumin; Aggregation; Mass spectrometry
资金
- National Key R&D Program of China [2018YFD0400300]
- National Natural Science Foundation of China [31771985]
- Jilin Province and School Co-construction [SF2017-6-4]
- Fundamental Research Funds for the Central Universities
- Program for JLU Science and Technology Innovative Research Team [2017TD-29]
- China Scholarship Council
We report the wet-state glycation of Bovine Serum Albumin (BSA) with xylose through the Maillard reaction and its effect on protein aggregations during heat treatment. Using low doses of xylose, glycation stabilized the conformations of BSA and reduced the formation of large aggregates during heat treatment. However, using high doses of xylose, glycation promoted the conversion of alpha-helices to unfolded structures and beta-sheets, and induced the formation of short amyloid-like aggregates after heat treatment. Using high-resolution mass spectrometry, three possible glycation sites were determined on BSA treated with low dose of xylose, while six glycations sites were detected when high doses of xylose were used instead. Considering the importance of glycation to the food industry, this work not only provides new insights into the nonlinear effects of glycation on protein stability, but also provides a strategy to tune the nutritional value and functionality of proteins during food processing.
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