Publications by authors named "Songfan Tian"

In this study, from the perspective of simulating the milk fat globule (MFG) emulsion, the interaction between soybean lecithin (SL) and the main protein in milk, whey protein (WP), and its effect on physical characteristics and lipid digestion were investigated through multiple spectroscopic techniques and in vitro digestion. The mechanism of SL and WP was static quenching, indicating that a complex formed between WP and SL through hydrophobic interaction and hydrogen bonding. The addition of SL changed the secondary structure of WP.

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The formulation of probiotics-enriched products still remains a challenge for the food industry due to the loss of viability, mainly occurring upon consumption and during storage. To tackle this challenge, the current study investigated the potential of using sodium alginate and inulin (SIN) in combination with various encapsulating materials such as skim milk (SKIM), whey protein concentrate (WPC), soy protein concentrate (SPC), and flaxseed oil (FS) to increase the viability of Lactobacillus casei upon freeze-drying, under simulated gastrointestinal conditions, during 28 days of storage at 4°C, and in a formulation of millet yogurt. Microstructural properties of microcapsules and co-microcapsules by SEM, oxidative stability of flaxseed oil in co-microcapsules, and physicochemical and sensory analysis of the product were performed.

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This study aimed to identify differences of lipidome and fatty acid composition among human, bovine and caprine milk fat globule membrane (MFGM) using a lipidomics approach. In total, 11 lipid classes were determined, including PC, PE, SM, PG, PI, PS, Cer, PA, HexCer, HexCer and CL. Using positive and negative ionization modes, 73 and 156 common significantly differential lipid species were identified in three typical MFGM.

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The objective of this paper was to investigate the interactions between (-)-Epigallocatechin-3-gallate (EGCG) and whey protein isolate (WPI) by covalent and non-covalent combinations and the effects of the interactions on the conformational and functional changes of whey protein. Conformational changes in the secondary structure of whey protein with various concentrations of EGCG were studied using FTIR spectra. EGCG was more likely to form covalent bonds than non-covalent bonds when it interacted with whey proteins.

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