Biochemical and Utralmicroscopic Evaluation of Myofibril Proteins and Collagen during Ageing in Broiler Chicken PSE (Pale, Sof, Exudative) Meat
Abstract The aim of this work was to study the myofibril proteins and collagen fraction changes in broiler chickens PSE (pale, soft, exudative) meat during ageing and their relationship to meat quality. The results presented an increase of myofibril proteins and collagen solubility promoted by the e...
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| Format: | Article |
| Language: | English |
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Instituto de Tecnologia do Paraná (Tecpar)
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| Series: | Brazilian Archives of Biology and Technology |
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| Online Access: | http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1516-89132019000100503&lng=en&tlng=en |
| _version_ | 1819110999212425216 |
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| author | Denis Fabrício Marchi Flávia Maria Beteto Gleice Rocha dos Santos Almeida Adriana Lourenço Soares Francisco Javier Hernandez-Blazquez Elza Iouko Ida Massami Shimokomaki |
| author_facet | Denis Fabrício Marchi Flávia Maria Beteto Gleice Rocha dos Santos Almeida Adriana Lourenço Soares Francisco Javier Hernandez-Blazquez Elza Iouko Ida Massami Shimokomaki |
| author_sort | Denis Fabrício Marchi |
| collection | DOAJ |
| description | Abstract The aim of this work was to study the myofibril proteins and collagen fraction changes in broiler chickens PSE (pale, soft, exudative) meat during ageing and their relationship to meat quality. The results presented an increase of myofibril proteins and collagen solubility promoted by the enhanced proteases activities during storage. Ultramicroscopically, the PSE meat samples revealed intracellularly a sarcomere super contraction and lacunas within the A and I bands while Z-lines appeared very dense and fragmented in comparison to normal samples. This observation was noticed already at 4h storage while extracellularly collagen fibrils decreased visually within the endomysium only after 24h of conditioning. These results influenced the quality as the PSE meat presented better functional properties at the first hours of conditioning before further proteins degradation by proteases. Thereafter, at the later ageing stage a further disintegration of the abnormal meat structure would affect the meat functional properties. |
| first_indexed | 2024-12-22T03:50:38Z |
| format | Article |
| id | doaj.art-35d2402f6e2d4ee4845e0a9d3b7e5c7b |
| institution | Directory Open Access Journal |
| issn | 1678-4324 |
| language | English |
| last_indexed | 2024-12-22T03:50:38Z |
| publisher | Instituto de Tecnologia do Paraná (Tecpar) |
| record_format | Article |
| series | Brazilian Archives of Biology and Technology |
| spelling | doaj.art-35d2402f6e2d4ee4845e0a9d3b7e5c7b2022-12-21T18:40:01ZengInstituto de Tecnologia do Paraná (Tecpar)Brazilian Archives of Biology and Technology1678-43246210.1590/1678-4324-2019180119S1516-89132019000100503Biochemical and Utralmicroscopic Evaluation of Myofibril Proteins and Collagen during Ageing in Broiler Chicken PSE (Pale, Sof, Exudative) MeatDenis Fabrício MarchiFlávia Maria BetetoGleice Rocha dos Santos AlmeidaAdriana Lourenço SoaresFrancisco Javier Hernandez-BlazquezElza Iouko IdaMassami ShimokomakiAbstract The aim of this work was to study the myofibril proteins and collagen fraction changes in broiler chickens PSE (pale, soft, exudative) meat during ageing and their relationship to meat quality. The results presented an increase of myofibril proteins and collagen solubility promoted by the enhanced proteases activities during storage. Ultramicroscopically, the PSE meat samples revealed intracellularly a sarcomere super contraction and lacunas within the A and I bands while Z-lines appeared very dense and fragmented in comparison to normal samples. This observation was noticed already at 4h storage while extracellularly collagen fibrils decreased visually within the endomysium only after 24h of conditioning. These results influenced the quality as the PSE meat presented better functional properties at the first hours of conditioning before further proteins degradation by proteases. Thereafter, at the later ageing stage a further disintegration of the abnormal meat structure would affect the meat functional properties.http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1516-89132019000100503&lng=en&tlng=enCooking lossTendernessCollagen contentMyofibrillar Fragmentation Index |
| spellingShingle | Denis Fabrício Marchi Flávia Maria Beteto Gleice Rocha dos Santos Almeida Adriana Lourenço Soares Francisco Javier Hernandez-Blazquez Elza Iouko Ida Massami Shimokomaki Biochemical and Utralmicroscopic Evaluation of Myofibril Proteins and Collagen during Ageing in Broiler Chicken PSE (Pale, Sof, Exudative) Meat Brazilian Archives of Biology and Technology Cooking loss Tenderness Collagen content Myofibrillar Fragmentation Index |
| title | Biochemical and Utralmicroscopic Evaluation of Myofibril Proteins and Collagen during Ageing in Broiler Chicken PSE (Pale, Sof, Exudative) Meat |
| title_full | Biochemical and Utralmicroscopic Evaluation of Myofibril Proteins and Collagen during Ageing in Broiler Chicken PSE (Pale, Sof, Exudative) Meat |
| title_fullStr | Biochemical and Utralmicroscopic Evaluation of Myofibril Proteins and Collagen during Ageing in Broiler Chicken PSE (Pale, Sof, Exudative) Meat |
| title_full_unstemmed | Biochemical and Utralmicroscopic Evaluation of Myofibril Proteins and Collagen during Ageing in Broiler Chicken PSE (Pale, Sof, Exudative) Meat |
| title_short | Biochemical and Utralmicroscopic Evaluation of Myofibril Proteins and Collagen during Ageing in Broiler Chicken PSE (Pale, Sof, Exudative) Meat |
| title_sort | biochemical and utralmicroscopic evaluation of myofibril proteins and collagen during ageing in broiler chicken pse pale sof exudative meat |
| topic | Cooking loss Tenderness Collagen content Myofibrillar Fragmentation Index |
| url | http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1516-89132019000100503&lng=en&tlng=en |
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