High pressure processing of meat: possible role of myofibrillar protein interactions and cathepsin activity

Research output: Contribution to conferencePosterResearch

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High pressure processing of meat : possible role of myofibrillar protein interactions and cathepsin activity. / Grossi, Alberto; Christensen, Mette; Ertbjerg, Per; Olsen, Karsten; Orlien, Vibeke.

2010. Poster session presented at HPBB , .

Research output: Contribution to conferencePosterResearch

Harvard

Grossi, A, Christensen, M, Ertbjerg, P, Olsen, K & Orlien, V 2010, 'High pressure processing of meat: possible role of myofibrillar protein interactions and cathepsin activity' HPBB , 20/10/2010, .

APA

Grossi, A., Christensen, M., Ertbjerg, P., Olsen, K., & Orlien, V. (2010). High pressure processing of meat: possible role of myofibrillar protein interactions and cathepsin activity. Poster session presented at HPBB , .

Vancouver

Grossi A, Christensen M, Ertbjerg P, Olsen K, Orlien V. High pressure processing of meat: possible role of myofibrillar protein interactions and cathepsin activity. 2010. Poster session presented at HPBB , .

Author

Grossi, Alberto ; Christensen, Mette ; Ertbjerg, Per ; Olsen, Karsten ; Orlien, Vibeke. / High pressure processing of meat : possible role of myofibrillar protein interactions and cathepsin activity. Poster session presented at HPBB , .

Bibtex

@conference{8a4b86b27d154e8ca453032025a59bb1,
title = "High pressure processing of meat: possible role of myofibrillar protein interactions and cathepsin activity",
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.",
author = "Alberto Grossi and Mette Christensen and Per Ertbjerg and Karsten Olsen and Vibeke Orlien",
year = "2010",
language = "English",
note = "HPBB ; Conference date: 20-10-2010",

}

RIS

TY - CONF

T1 - High pressure processing of meat

T2 - possible role of myofibrillar protein interactions and cathepsin activity

AU - Grossi, Alberto

AU - Christensen, Mette

AU - Ertbjerg, Per

AU - Olsen, Karsten

AU - Orlien, Vibeke

PY - 2010

Y1 - 2010

N2 - 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.

AB - 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.

M3 - Poster

ER -

ID: 32108686