Characterization of Collagen Structure in Normal, Wooden Breast and Spaghetti Meat Chicken Fillets by FTIR Microspectroscopy and Histology
Recently, two chicken breast fillet abnormalities, termed Wooden Breast (WB) and Spaghetti Meat (SM), have become a challenge for the chicken meat industry. The two abnormalities share some overlapping morphological features, including myofiber necrosis, intramuscular fat deposition, and collagen fi...
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doaj-345cb1c54ca843d686be18e1496c06392021-03-07T00:02:39ZengMDPI AGFoods2304-81582021-03-011054854810.3390/foods10030548Characterization of Collagen Structure in Normal, Wooden Breast and Spaghetti Meat Chicken Fillets by FTIR Microspectroscopy and HistologyKaren Wahlstrøm Sanden0Ulrike Böcker1Ragni Ofstad2Mona Elisabeth Pedersen3Vibeke Høst4Nils Kristian Afseth5Sissel Beate Rønning6Nancy Pleshko7Nofima AS, Muninbakken 9-13, Breivika, 9019 Tromsø, NorwayNofima AS, Muninbakken 9-13, Breivika, 9019 Tromsø, NorwayNofima AS, Muninbakken 9-13, Breivika, 9019 Tromsø, NorwayNofima AS, Muninbakken 9-13, Breivika, 9019 Tromsø, NorwayNofima AS, Muninbakken 9-13, Breivika, 9019 Tromsø, NorwayNofima AS, Muninbakken 9-13, Breivika, 9019 Tromsø, NorwayNofima AS, Muninbakken 9-13, Breivika, 9019 Tromsø, NorwayDepartment of Bioengineering, Temple University, Philadelphia, PA 19122, USARecently, two chicken breast fillet abnormalities, termed Wooden Breast (WB) and Spaghetti Meat (SM), have become a challenge for the chicken meat industry. The two abnormalities share some overlapping morphological features, including myofiber necrosis, intramuscular fat deposition, and collagen fibrosis, but display very different textural properties. WB has a hard, rigid surface, while the SM has a soft and stringy surface. Connective tissue is affected in both WB and SM, and accordingly, this study’s objective was to investigate the major component of connective tissue, collagen. The collagen structure was compared with normal (NO) fillets using histological methods and Fourier transform infrared (FTIR) microspectroscopy and imaging. The histology analysis demonstrated an increase in the amount of connective tissue in the chicken abnormalities, particularly in the perimysium. The WB displayed a mixture of thin and thick collagen fibers, whereas the collagen fibers in SM were thinner, fewer, and shorter. For both, the collagen fibers were oriented in multiple directions. The FTIR data showed that WB contained more β-sheets than the NO and the SM fillets, whereas SM fillets expressed the lowest mature collagen fibers. This insight into the molecular changes can help to explain the underlying causes of the abnormalities.https://www.mdpi.com/2304-8158/10/3/548chicken meat qualitymuscle abnormalitiesconnective tissuehistologyFTIR microspectroscopy |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
Karen Wahlstrøm Sanden Ulrike Böcker Ragni Ofstad Mona Elisabeth Pedersen Vibeke Høst Nils Kristian Afseth Sissel Beate Rønning Nancy Pleshko |
spellingShingle |
Karen Wahlstrøm Sanden Ulrike Böcker Ragni Ofstad Mona Elisabeth Pedersen Vibeke Høst Nils Kristian Afseth Sissel Beate Rønning Nancy Pleshko Characterization of Collagen Structure in Normal, Wooden Breast and Spaghetti Meat Chicken Fillets by FTIR Microspectroscopy and Histology Foods chicken meat quality muscle abnormalities connective tissue histology FTIR microspectroscopy |
author_facet |
Karen Wahlstrøm Sanden Ulrike Böcker Ragni Ofstad Mona Elisabeth Pedersen Vibeke Høst Nils Kristian Afseth Sissel Beate Rønning Nancy Pleshko |
author_sort |
Karen Wahlstrøm Sanden |
title |
Characterization of Collagen Structure in Normal, Wooden Breast and Spaghetti Meat Chicken Fillets by FTIR Microspectroscopy and Histology |
title_short |
Characterization of Collagen Structure in Normal, Wooden Breast and Spaghetti Meat Chicken Fillets by FTIR Microspectroscopy and Histology |
title_full |
Characterization of Collagen Structure in Normal, Wooden Breast and Spaghetti Meat Chicken Fillets by FTIR Microspectroscopy and Histology |
title_fullStr |
Characterization of Collagen Structure in Normal, Wooden Breast and Spaghetti Meat Chicken Fillets by FTIR Microspectroscopy and Histology |
title_full_unstemmed |
Characterization of Collagen Structure in Normal, Wooden Breast and Spaghetti Meat Chicken Fillets by FTIR Microspectroscopy and Histology |
title_sort |
characterization of collagen structure in normal, wooden breast and spaghetti meat chicken fillets by ftir microspectroscopy and histology |
publisher |
MDPI AG |
series |
Foods |
issn |
2304-8158 |
publishDate |
2021-03-01 |
description |
Recently, two chicken breast fillet abnormalities, termed Wooden Breast (WB) and Spaghetti Meat (SM), have become a challenge for the chicken meat industry. The two abnormalities share some overlapping morphological features, including myofiber necrosis, intramuscular fat deposition, and collagen fibrosis, but display very different textural properties. WB has a hard, rigid surface, while the SM has a soft and stringy surface. Connective tissue is affected in both WB and SM, and accordingly, this study’s objective was to investigate the major component of connective tissue, collagen. The collagen structure was compared with normal (NO) fillets using histological methods and Fourier transform infrared (FTIR) microspectroscopy and imaging. The histology analysis demonstrated an increase in the amount of connective tissue in the chicken abnormalities, particularly in the perimysium. The WB displayed a mixture of thin and thick collagen fibers, whereas the collagen fibers in SM were thinner, fewer, and shorter. For both, the collagen fibers were oriented in multiple directions. The FTIR data showed that WB contained more β-sheets than the NO and the SM fillets, whereas SM fillets expressed the lowest mature collagen fibers. This insight into the molecular changes can help to explain the underlying causes of the abnormalities. |
topic |
chicken meat quality muscle abnormalities connective tissue histology FTIR microspectroscopy |
url |
https://www.mdpi.com/2304-8158/10/3/548 |
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