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Changes in proteins during Teruel dry-cured ham processing.

V Larrea¹, I Hernando, A Quiles

¹Universidad Politécnica de Valencia, Instituto de Ingeniería de Alimentos para el Desarrollo-Dpto. Tecnología de Alimentos. P.O. Box 22010, 46071 Valencia, Spain.

|November 9, 2011

Summary

This summary is machine-generated.

Protein degradation in "PDO Teruel" cured ham is linked to salting and ripening. Residual enzymatic activity from cathepsins B, L, and D significantly influences proteolysis, affecting the final product characteristics.

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Area of Science:

Food Science
Biochemistry
Meat Science

Background:

"PDO Teruel" ham is a protected designation of origin product.
Protein composition and degradation impact cured meat quality and sensory attributes.

Purpose of the Study:

Investigate water-soluble and myofibrillar protein degradation during "PDO Teruel" ham production.
Measure proteolytic activities (cathepsins B+L, L, D) as factors influencing sensory characteristics.
Contribute to the specific characterization of this EU-recognized quality product.

Main Methods:

Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) for protein analysis.
Enzymatic activity assays for cathepsins B+L, L, and D.
Analysis of protein changes throughout the ham production and ripening process.

Main Results:

Water-soluble proteins significantly decreased post-salting due to salting out and drainage.
Myofibrillar protein degradation intensified during ripening, especially in the final four months.
Significant residual activity of cathepsins B, L, and D was detected, indicating their role in proteolysis.

Conclusions:

Salting and ripening are key stages for protein degradation in "PDO Teruel" ham.
Cathepsin B, L, and D activities are crucial drivers of proteolysis during processing.
Understanding these processes is vital for controlling and enhancing the sensory quality of "PDO Teruel" ham.