Mechanistic Insights into Synergistic Collagen Degradation by MMP-3 and MMP-16 in Post-Mortem Abalone Muscle

Tian-Bo Zhang1, Fu-Hao Zhang1, Ling-Jing Zhang1

  • 1College of Ocean Food and Biological Engineering, Jimei University, Xiamen 361021, China.

Insights

Matrix metalloproteinases (MMPs) cause abalone muscle softening. This study shows MMP-3 and MMP-16 synergistically degrade collagen, revealing a mechanism for seafood preservation.

Area of Science:

  • Biochemistry
  • Marine Biology
  • Food Science

Background:

  • Post-mortem muscle softening in abalone is linked to collagen breakdown by matrix metalloproteinases (MMPs).
  • The synergistic interactions between different MMPs in this process are not fully understood.

Purpose of the Study:

  • To investigate the combined effects of MMP-3 and MMP-16 on type I collagen and collagen fiber degradation.
  • To elucidate the mechanism of synergistic collagen degradation by MMPs.

Main Methods:

  • Heterologous expression of MMP-3 and MMP-16.
  • In vitro degradation assays of type I collagen and collagen fibers.
  • Mass spectrometry analysis of degradation products.

Main Results:

  • Both MMP-3 and MMP-16 degraded collagen individually.
  • Combined action of MMP-3 and MMP-16 significantly accelerated collagen fiber degradation.
  • MMP-3 cleaved telopeptides and disrupted the collagen triple helix, enabling MMP-16 to cause extensive proteolysis.

Conclusions:

  • A synergistic loosening-then-degradation mechanism for MMP-mediated collagen breakdown was elucidated.
  • This mechanism explains post-mortem muscle softening in abalone.
  • Findings provide a theoretical basis for developing seafood preservation strategies.

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