Application of preheating treatment in up- and down-regulating the glycation process of dietary proteins. (January 2020)

• Record Type: Journal Article
• Authors: Zhao, Di; Xu, Dan; Sheng, Bulei; Zhu, Zongshuai; Li, Hao; Nian, Yingqun; Wang, Cong; Li, Chunbao; Xu, Xinglian; Zhou, Guanghong
• Is Part Of: Food hydrocolloids. Volume 98(2020)
• Publication Date: 2020-01
• Subjects: Preheating treatment -- Glycation -- Bovine serum albumin -- β-Lactoglobulin -- β-Casein; Hydrocolloids -- Periodicals; Food additives -- Periodicals; Colloïdes -- Périodiques; Aliments -- Additifs -- Périodiques; Colloids; Food additives; Periodicals; Electronic journals; 664.06
• DOI: 10.1016/j.foodhyd.2019.105264
• Languages: English
• ISSNs: 0268-005X

Abstract

Abstract: Heating is the most commonly used treatment in food industry. This work reported the influence of preheating treatment (PT, 98 °C) on the following glycation behavior of bovine serum albumin (BSA), β-lactoglobulin (β-Lg) and β-casein (β-CN) at 90 °C. The PT was shown to induce both the unfolding and aggregation of proteins, which changed their subsequent glycation kinetics based on measurements of free amino group content and UV absorbance at 294 and 420 nm. Ten minutes of PT unfolded the globular structures of BSA and β-Lg and exposed more glycation sites, which largely up-regulated their glycation degrees. By contrast, 40 min of PT induced more severe aggregation in BSA and β-Lg during PT and the subsequent glycation process, which hid a portion of glycation sites and down-regulated their glycation degree. The glycation behavior of β-CN was almost not affected by PT, possibly due to its intrinsic disordered structure and high thermal stability. Proteomics analysis showed that PT resulted in changes in the number of glycated structures and preference of lysine residues to be glycated. These results suggested PT as an effective way in regulating the glycation behavior of dietary proteins, depending on PT duration and structure of treated protein. Graphical abstract: Image 1 Highlights: Glycation kinetics of BSA and β-Lg can be regulated by PT. PT can both up- and down-regulate the glycation of BSA and β-Lg depending on PT duration. Proteomics showed PT-induced change in the preference of glycation sites.