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Food Chem. 2014 Feb 15;145:632-8. doi: 10.1016/j.foodchem.2013.08.055. Epub 2013 Aug 26.

Purification and characterization of a gelatinolytic matrix metalloproteinase from the skeletal muscle of grass carp (Ctenopharyngodon idellus).

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  • 1Institute of Biomedical and Pharmaceutical Technology, Fuzhou University, Fuzhou 350002, China. Electronic address:


A gelatinolytic matrix metalloproteinase (gMMP) from grass carp skeletal muscle was purified by 30-70% ammonium sulphate fractionation and a combination of chromatographic steps including ion exchange on DEAE-Sephacel, gel filtration on Sephacryl S-200, and affinity on gelatin-sepharose. The molecular weight of the proteinase as estimated by SDS-PAGE was 70 kDa under non-reducing conditions. The enzyme revealed high activity from 30 to 50 °C, and the gelatin hydrolysing activity was investigated at a slightly alkaline pH range using gelatin as substrate. Metalloproteinase inhibitor EDTA completely suppressed the gelatinolytic activity, while other proteinase inhibitors did not show any inhibitory effect. Divalent metal ion Ca(2+) was essential for the gelatinolytic activity. Further, peptide mass fingerprinting obtained four fragments with 45 amino acid residues, which were highly identical to MMP-2 from fish species. The gMMP could effectively hydrolyse type I collagen even at 4 °C, suggesting its involvement in the texture softening of fish muscle during the post-mortem stage.

Copyright © 2013 Elsevier Ltd. All rights reserved.


Gelatin zymography; Grass carp; Matrix metalloproteinase; Post-mortem tenderization; Purification

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