High pressure treatment of brine enhanced pork affects endopeptidase activity, protein solubility, and peptide formation

TY - JOUR

T1 - High pressure treatment of brine enhanced pork affects endopeptidase activity, protein solubility, and peptide formation

AU - Grossi, Alberto Blak

AU - Gkarane, Vasiliki

AU - Otte, Jeanette Anita Held

AU - Ertbjerg, Per

AU - Orlien, Vibeke

PY - 2012/10/1

Y1 - 2012/10/1

N2 - In order to study the effect of high-pressure (HP) treatment and two different methods of brine addition (important for lysosomal membrane destabilisation) on lysosomal enzymes activity and protein degradation, pork semitendinosus muscle was brine enhanced by injection or tumbling, and HP treated at 600 MPa following storage at 2 °C for up to 8 weeks. In this report a novel protocol for SDS gelatin zymography was established, and an increase of cathepsin B and L activity after HP treatment was shown followed by a decrease during storage. No calpain activity was detected following HP treatment. HP treatment was shown to induce a decrease in protein solubility in both myofibrillar and sarcoplasmic fractions. LC–MS analysis of these fractions showed changes in the peptide pattern during storage. Western blot analysis showed that troponin-T was indeed degraded during storage after HP treatment. The results therefore suggest that HP treatment induced an increase in cathepsin activity, which subsequently affected the myofibrillar protein degradation pattern in pork meat.

AB - In order to study the effect of high-pressure (HP) treatment and two different methods of brine addition (important for lysosomal membrane destabilisation) on lysosomal enzymes activity and protein degradation, pork semitendinosus muscle was brine enhanced by injection or tumbling, and HP treated at 600 MPa following storage at 2 °C for up to 8 weeks. In this report a novel protocol for SDS gelatin zymography was established, and an increase of cathepsin B and L activity after HP treatment was shown followed by a decrease during storage. No calpain activity was detected following HP treatment. HP treatment was shown to induce a decrease in protein solubility in both myofibrillar and sarcoplasmic fractions. LC–MS analysis of these fractions showed changes in the peptide pattern during storage. Western blot analysis showed that troponin-T was indeed degraded during storage after HP treatment. The results therefore suggest that HP treatment induced an increase in cathepsin activity, which subsequently affected the myofibrillar protein degradation pattern in pork meat.

U2 - 10.1016/j.foodchem.2012.03.089

DO - 10.1016/j.foodchem.2012.03.089

M3 - Journal article

C2 - 25005980

SN - 0308-8146

VL - 134

SP - 1556

EP - 1563

JO - Food Chemistry

JF - Food Chemistry

IS - 3

ER -