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Related Experiment Videos

Plasmin activity in pressurized milk.

M R García-Risco1, I Recio, E Molina

  • 1Instituto de Fermentaciones Industriales (CSIC), Juan de la Cierva, 3, 28008 Madrid, Spain.

Journal of Dairy Science
|April 22, 2003
PubMed
Summary
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High pressure processing disrupts milk micelle structure, releasing caseins and enzymes. While caseins become more susceptible to proteolysis, overall milk proteolysis does not increase during storage due to enzyme inactivation.

Area of Science:

  • Food Science
  • Biochemistry
  • Dairy Technology

Background:

  • Milk proteinase activity, particularly plasmin, affects milk quality and shelf-life.
  • Understanding the impact of high pressure processing (HPP) on milk's native proteinase system is crucial for dairy innovation.
  • Casein micelle structure and beta-lactoglobulin (beta-LG) are key components affected by processing.

Purpose of the Study:

  • To investigate the effects of room temperature HPP (up to 400 MPa) on native proteinase activity in milk.
  • To assess the influence of pressure on plasmin activity, plasminogen activation, and enzyme distribution within milk fractions.
  • To determine the impact of HPP on micelle microstructure, beta-LG denaturation, and casein susceptibility to proteolysis.

Main Methods:

  • Application of high pressure (up to 400 MPa) at room temperature to raw milk.

Related Experiment Videos

  • Assay of plasmin activity and plasmin-derived activity post-plasminogen activation.
  • Analysis of milk fractions via ultracentrifugation to determine protein distribution.
  • Evaluation of beta-LG denaturation and casein susceptibility to exogenous plasmin.

    • Main Results:

    • HPP did not inactivate plasmin but reduced total activity by 20-30% after plasminogen activation.
    • Severe disruption of micellar structure occurred, releasing caseins, plasmin, and plasminogen into the soluble fraction.
    • Significant denaturation of beta-LG was observed, particularly at 400 MPa.
    • Caseins became more susceptible to proteolysis due to micellar disintegration, but overall proteolytic degradation did not increase during refrigerated storage.

    Conclusions:

    • HPP significantly alters milk's colloidal and soluble phases, impacting protein distribution and structure.
    • Despite increased casein susceptibility, reduced overall proteolysis during storage suggests protective mechanisms for liberated enzymes.
    • Further research is needed to fully elucidate the interplay between pressure-induced structural changes and enzyme activity in milk systems.