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Calcium-binding peptide derived from pepsinolytic hydrolysates of hoki (Johnius belengerii) frame

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Abstract

In order to utilize fish byproducts in a calcium supplement with high solubility, hoki (Johnius belengerii) frames composed of flesh and skeleton discarded from industrial processing were degraded by pepsin in acetic acid solution (pH 2.2). After digestion, a calcium-binding peptide was isolated from the pepsinolytic hydrolysates using a hydroxyapatite affinity chromatography. Calcium-binding assay elucidated that J. belengerii frame peptide (JFP) can solubilize a similar amount of calcium with casein phosphopeptide (CPP). In ESI-QTOF tandem mass analysis for peptide identification, the amino acid sequence of JFP showed high similarity to those of actin (NCBInr database), was identified as Val-Leu-Ser-Gly-Gly-Thr-Thr-Met-Tyr-Ala-Ser-Leu-Tyr-Ala-Glu (MW: 1,561 Da).

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Acknowledgment

This research was supported by a grant (p-2004-01) from the Marine Bioprocess Research Center of the Marine Bio 21 Center funded by the Ministry of Maritime Affairs and Fisheries, Republic of Korea.

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Authors and Affiliations

  1. Department of Chemistry, Pukyong National University, Busan, 608-737, South Korea

    Won-Kyo Jung & Se-Kwon Kim

  2. Marine Bioprocess Research Center, Pukyong National University, Busan, 608-737, South Korea

    Won-Kyo Jung & Se-Kwon Kim

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  1. Won-Kyo Jung
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  2. Se-Kwon Kim
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Correspondence to Se-Kwon Kim.

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Jung, WK., Kim, SK. Calcium-binding peptide derived from pepsinolytic hydrolysates of hoki (Johnius belengerii) frame. Eur Food Res Technol 224, 763–767 (2007). https://doi.org/10.1007/s00217-006-0371-4

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  • DOI: https://doi.org/10.1007/s00217-006-0371-4

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