Abstract
Abstract
Background: The research of high pressure (HP) processing of meat based foods needs to address how pressure affects protein interactions, aggregation and/or gelation. The understanding of the gel forming properties of myofibrillar components is fundamental for the development of muscle based products (Chapleau et al., 2004;Colmenero, 2002).
Object: The aim was to study the rheological properties of pork meat emulsion exposed to HP and the effect of HP on the aggregation state of myofibrillar proteins. To address the role of cathepsin in myofibrillar protein degradation the changes in the myofibrillar protein pattern and HP-induced change in activity of cathepsin B and L were investigated.
Results: In this study we showed that HP treatment of pork meat emulsion, ranging from 0.1 to 800 MPa, induced protein gel formation as shown by the increased Young’s modulus (Fig.1). Analysis of SDS–PAGE gels of myofibrillar protein extract from HP treated meat showed that myofibrillar proteins form high molecular weight aggregates after HP treatment. Myofibrillar protein aggregates were stable in a reducing environment, suggesting that disulfide bonds are not the main molecular interactions responsible for these aggregations (Fig.2). Furthermore HP treatment caused an increase in cathepsin activity (Fig.3), probably due to disruption of the lysosomal membrane and leakage of enzymes, which subsequently affected the myofibrillar protein degradation pattern (Fig.4).
Conclusion: HP treatment affects the rheological properties of pork meat batters by inducing formation of protein gels. HP induced protein gels are suggested to be formed by high molecular weight myofibrillar protein aggregates and by peptides formed by lysosomal enzyme-induced cleavage of myofibrillar proteins.
Perspectives: The data presented suggest that the lysosomal enzymes play a potential role in pressure assisted gelation.
Background: The research of high pressure (HP) processing of meat based foods needs to address how pressure affects protein interactions, aggregation and/or gelation. The understanding of the gel forming properties of myofibrillar components is fundamental for the development of muscle based products (Chapleau et al., 2004;Colmenero, 2002).
Object: The aim was to study the rheological properties of pork meat emulsion exposed to HP and the effect of HP on the aggregation state of myofibrillar proteins. To address the role of cathepsin in myofibrillar protein degradation the changes in the myofibrillar protein pattern and HP-induced change in activity of cathepsin B and L were investigated.
Results: In this study we showed that HP treatment of pork meat emulsion, ranging from 0.1 to 800 MPa, induced protein gel formation as shown by the increased Young’s modulus (Fig.1). Analysis of SDS–PAGE gels of myofibrillar protein extract from HP treated meat showed that myofibrillar proteins form high molecular weight aggregates after HP treatment. Myofibrillar protein aggregates were stable in a reducing environment, suggesting that disulfide bonds are not the main molecular interactions responsible for these aggregations (Fig.2). Furthermore HP treatment caused an increase in cathepsin activity (Fig.3), probably due to disruption of the lysosomal membrane and leakage of enzymes, which subsequently affected the myofibrillar protein degradation pattern (Fig.4).
Conclusion: HP treatment affects the rheological properties of pork meat batters by inducing formation of protein gels. HP induced protein gels are suggested to be formed by high molecular weight myofibrillar protein aggregates and by peptides formed by lysosomal enzyme-induced cleavage of myofibrillar proteins.
Perspectives: The data presented suggest that the lysosomal enzymes play a potential role in pressure assisted gelation.
| Original language | English |
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| Publication date | 2010 |
| Publication status | Published - 2010 |
| Event | HPBB - Duration: 20 Oct 2010 → … |
Conference
| Conference | HPBB |
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| Period | 20/10/2010 → … |