Recovery of a novel Ca-binding peptide from Alaska Pollack (Theragra chalcogramma) backbone by pepsinolytic hydrolysis

Purification of a Novel Oligophosphopeptide with High Calcium Binding Activity from Carp Egg Hydrolysate

“…Casein phosphopeptides (CPPs) were well known for their metal binding abilities because the CPPs contained electronegative phosphoserines (West et al, 1986;Meisel et al, 1990;Yuan et al, 1991;Gerber et al, 1986;Sato et al, 1986). The phosphopeptides obtained from the enzymolysis of fish bone (Jung et al, 2007(Jung et al, , 2006(Jung et al, , 2005 can also chelate Ca, whose performance is similar to CPPs. Many studies indicated that fish eggs also contain high phosphoprotein and can obtain phosphopeptides by hydrolysis (Catherine et al, 2002;Inoue et al, 1971).…”

“…The yield and calcium binding ability of U1 are far greater than that of U2 (Table 2), which shows that after hydrolysis, the carp eggs protein has decomposed into small molecule peptides with high calcium binding ability. Many studies have shown that biologically active peptides usually contain 3 _ 20 amino acid residues and the molecular weight of discovered peptides with calcium binding capacity are mostly from 1 kDa to 3.5 kDa (Jiang et al, 2000;Jung et al, 2005Jung et al, , 2006Jung et al, , 2007Lee et al, 2009 ).…”

“…By HA chromatography, the peptides and proteins with calcium binding activity have been successfully separated and obtained from fish bones and bullfrogs (Jung, et al, 2005(Jung, et al, , 2006(Jung, et al, , 2007Dohi et al, 1987). Amino acid content analysis showed that the serine content of H3 is 2.5 times more than that of U1, but the threonine and tyrosine contents is almost identical, which proved that the serine in the peptide played a vital role in ability to bind calcium.…”

Effectiveness of Carp Egg Phosphopeptide on Inhibiting the Formation of Insoluble Ca Salts in vitro and Enhancing Ca Bioavailability in vivo

“…By hydroxyapatite chromatography, the peptides and proteins with calcium binding activity have been successfully separated and obtained from fish bones and bullfrog bone (Jung et al, 2005(Jung et al, , 2006(Jung et al, , 2007Dohi, 1987). The results showed that after hydroxyapatite chromatography, the calcium binding activity of EPP was significantly increased and slightly lower than CPP ( p < There was a positive correlation between the phosphorus content of peptide and its Ca binding activity.…”

“…Studies have shown that CPP can maintain a higher concentration of soluble Ca in small intestine so as to promote Ca's absorption in the small intestine through passive diffusion absorption (Sato et al, 1986). Since phosphate groups endow CPP with high ability to promote Ca absorption, researchers devote themselves to develop other proteins or peptides rich in phosphate groups, such as phosvitin and its tryptic peptide, osteocalcin and fish bone peptides for Ca nutraceutical additive usage (Jiang and Ming, 2000;Jung et al, 2006;Jung and Kim, 2007;Nishmoto et al, 2003). However, some scholars have pointed out that the phosphorus-rich macromolecules such as phosvitin would resist the hydrolysis of protease (Mecham and Olcott, 1949;Goulas et al, 1996) and reduce Ca absorption (Ishikawa et al, 2007;Mineo et al, 2009), and we should obtain small molecules phosphorylated peptides through exogenous hydrolysis.…”