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| Differentiation of fish gelatin from bovine/porcine gelatin by tandem mass spectrometry |
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Abstract Sequence alignment analysis indicated that bovine, porcine and fish collagen type I contain differential sequences, which might be used as marker peptides for gelatin differentiation. In this research, bovine, porcine and fish gelatin were digested by trypsin. The peptides in the digest mixtures were identified by high performance liquid chromatography/mass spectrometry (HPLC/MS). Marker peptides specific for fish collagen type I were found in the digested fish gelatin. Actual sample analysis indicated that fish gelatin might be identified according to the marker peptides detected. The effect of hydroxylation of proline and the molecular weight range of gelatin on the relative abundance of marker peptides were also investigated. This research demonstrated that fish gelatin can be differentiated by detection of marker peptides in the tryptic digest of sample gelatin.
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Received: 25 July 2008
Published: 02 July 2009
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