Abstract
Calcium-binding peptide was derived from protein hydrolysates. In this study, tilapia protein at a concentration of 2 % (w/v) was hydrolyzed using various proteases including Alcalase 2.4 L, Flavourzyme 1,000L, Protease GN, and papain at 50 °C, pH 8 for 6 h. It was found that the degree of hydrolysis increased with the time of the incubation in all cases. The highest calcium-binding capacity of the hydrolysate was 65 mg/g protein at 27.7 % degree of hydrolysis by Alcalase 2.4 L. The molecular weight of the calcium-binding peptides characterized by gel-filtration chromatography on a Sephadex G-25 was 1.2 kDa. The calcium-binding motif of the hydrolyzed peptides identified by the automated Edman degradation was a short peptide (Trp-Glu-Trp-Leu-His-Tyr-Trp). The results of this study suggested that tilapia protein is a good source for calcium-binding peptides.
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This work was financially supported by Office of the Higher Education Commission to Narin Charoenphun under the CHE PhD. Scholarship Program. There was also supported from the Graduate School, Prince of Songkla University.
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Charoenphun, N., Cheirsilp, B., Sirinupong, N. et al. Calcium-binding peptides derived from tilapia (Oreochromis niloticus) protein hydrolysate. Eur Food Res Technol 236, 57–63 (2013). https://doi.org/10.1007/s00217-012-1860-2
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DOI: https://doi.org/10.1007/s00217-012-1860-2