Characterization of sea cucumber (stichopus japonicus) ovum hydrolysates: calcium chelation, solubility and absorption into intestinal epithelial cells
Tóm tắt
Sea cucumber (
The results of the present study show that the calcium‐binding capacity of SCOHs depended greatly on the type of proteases. The maximum level of Ca binding (0.38 mmol L–1) occurred when trypsin was used, with a peptide yield of 85.7%. Investigation of the possible chelating modes between SCOHs and calcium ions indicated that calcium ions bound to SCOHs primarily via interactions with carboxyl oxygen and amino nitrogen atoms of Glu and Asp and also that the phosphoserine residues might be also responsible for SCOH–calcium chelation. Moreover, SCOH–calcium complexes maintained the solubility of calcium under simulated gastrointestinal digestion, regardless of the presence of dietary components such as oxalate. Furthermore, SCOH–Ca led to higher peak intracellular [Ca2+]i in both Caco‐2 cells (338.3 nmol L–1
Carboxyl oxygen and amino nitrogen atoms in the SCOHs could bind calcium ions, forming SCOH–calcium complexes. These complexes improved calcium solubility under simulated gastrointestinal digestion and also promoted calcium absorption in Caco‐2 and HT‐29 cells. © 2017 Society of Chemical Industry
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Tài liệu tham khảo
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