Study on internal structure of casein micelles in reconstituted skim milk powder

Structural Properties of Casein Micelles with Adjusted Micellar Calcium Phosphate Content

“…The methyl signal that appears at ~0.5 ppm was most intense in MCP 7 and the least in MCP 129 (Figure 6). This resonance arises from the methyl protons of alanine, leucine, isoleucine and threonine and their intensity could be related to their greater presence in the soluble phase [26]. Similarly, the aromatic region of the spectrum (6-9 ppm) [27], depicting ring protons of phenylalanine, tyrosine, tryptophan and histidine, resonated greatly at lower MCP content (Figure 6A-E), which again was attributed to a greater proportion of soluble proteins in the past [28].…”

The aggregation of casein micelles induced by Ca2+ during in vitro digestion: effects on the release of loaded anthocyanins

“…36 According to previous studies, the bands at around 50-60 kDa could be crosslinkers between the homologous MC subunits, namely, the α S -casein dimer and β-casein dimer. [37][38][39][40] Due to the higher involvement of Ca 2+ for crosslinking reactions within the SFD-S sample, its clusters showed a stronger resistance to hydrolysis. Nevertheless, electrophoresis tests could not accu-…”

Novel Applications of Silk Proteins Based on Their Interactions with Metal Ions

“…Characterization results indicated that LM/NaAlg perfectly combined with the silk fibers spun by these silkworms and LM/NaAlg hindered the conformation transition of SF from the random coil and α-helix structure to the β-sheet structure by forming hydrogen bonds between LM/NaAlg and SF. Moreover, silk fibers spun by silkworms that were fed or injected with ethylenediaminetetraacetic acid (EDTA), a strong metal chelating agent [157,158], in their fifth instar larvae exhibited a significant conformational transition from β-sheet structure to β-turn structure and their strength, toughness, and Young's modulus decreased greatly [11].…”