Changes in Structures and Properties of Collagen Fibers during Collagen Casing Film Manufacturing
Collagen casing is an edible film, which is widely used in the industrial production of sausages. However, the detailed changes in the collagen fibers, from the raw material to the final collagen film, have rarely been reported. In this research, the changes in the collagen fibers during the manufac...
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| Format: | Article |
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MDPI AG
2023-04-01
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| Series: | Foods |
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| Online Access: | https://www.mdpi.com/2304-8158/12/9/1847 |
| _version_ | 1797602612429717504 |
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| author | Fei Liu Zhe Yu Beibei Wang Bor-Sen Chiou |
| author_facet | Fei Liu Zhe Yu Beibei Wang Bor-Sen Chiou |
| author_sort | Fei Liu |
| collection | DOAJ |
| description | Collagen casing is an edible film, which is widely used in the industrial production of sausages. However, the detailed changes in the collagen fibers, from the raw material to the final collagen film, have rarely been reported. In this research, the changes in the collagen fibers during the manufacturing process, including the fiber arrangement, the triple-helix structure and the thermal stability, were investigated using scanning electron microscopy (SEM), thermogravimetric analysis (TGA), X-ray diffraction (XRD), differential scanning calorimetry (DSC) and Fourier-transform infrared (FTIR) spectroscopy. The relationship between the structure stability and the arrangement of the collagen fibers was also discussed. According to the SEM, XRD, TGA, DSC and FTIR results, the collagen fibers were depolymerized during the acid swelling and became uniformly aligned after the homogenization process. Degassing had no obvious effect on the triple-helix structure. Alkaline neutralization with ammonia destroyed the triple-helix structure, which could be partly reversed through the washing and soaking processes. During the final drying step, the depolymerized triple helix of the collagen fibers recombined to form new structures that showed decreased thermal stability. This study expands our knowledge about the behavior of collagen fibers during the industrial process of producing collagen biobased casings. |
| first_indexed | 2024-03-11T04:19:04Z |
| format | Article |
| id | doaj.art-42ef8018167f40c5a57144b9952f85e9 |
| institution | Directory Open Access Journal |
| issn | 2304-8158 |
| language | English |
| last_indexed | 2024-03-11T04:19:04Z |
| publishDate | 2023-04-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Foods |
| spelling | doaj.art-42ef8018167f40c5a57144b9952f85e92023-11-17T22:55:40ZengMDPI AGFoods2304-81582023-04-01129184710.3390/foods12091847Changes in Structures and Properties of Collagen Fibers during Collagen Casing Film ManufacturingFei Liu0Zhe Yu1Beibei Wang2Bor-Sen Chiou3Key Laboratory of Synthetic and Biological Colloids, Ministry of Education, Jiangnan University, Wuxi 214122, ChinaKey Laboratory of Synthetic and Biological Colloids, Ministry of Education, Jiangnan University, Wuxi 214122, ChinaKey Laboratory of Synthetic and Biological Colloids, Ministry of Education, Jiangnan University, Wuxi 214122, ChinaWestern Regional Research Center, ARS, U.S. Department of Agriculture, Albany, CA 94710, USACollagen casing is an edible film, which is widely used in the industrial production of sausages. However, the detailed changes in the collagen fibers, from the raw material to the final collagen film, have rarely been reported. In this research, the changes in the collagen fibers during the manufacturing process, including the fiber arrangement, the triple-helix structure and the thermal stability, were investigated using scanning electron microscopy (SEM), thermogravimetric analysis (TGA), X-ray diffraction (XRD), differential scanning calorimetry (DSC) and Fourier-transform infrared (FTIR) spectroscopy. The relationship between the structure stability and the arrangement of the collagen fibers was also discussed. According to the SEM, XRD, TGA, DSC and FTIR results, the collagen fibers were depolymerized during the acid swelling and became uniformly aligned after the homogenization process. Degassing had no obvious effect on the triple-helix structure. Alkaline neutralization with ammonia destroyed the triple-helix structure, which could be partly reversed through the washing and soaking processes. During the final drying step, the depolymerized triple helix of the collagen fibers recombined to form new structures that showed decreased thermal stability. This study expands our knowledge about the behavior of collagen fibers during the industrial process of producing collagen biobased casings.https://www.mdpi.com/2304-8158/12/9/1847collagen casingscollagen fibermanufacturing processtriple-helix structure |
| spellingShingle | Fei Liu Zhe Yu Beibei Wang Bor-Sen Chiou Changes in Structures and Properties of Collagen Fibers during Collagen Casing Film Manufacturing Foods collagen casings collagen fiber manufacturing process triple-helix structure |
| title | Changes in Structures and Properties of Collagen Fibers during Collagen Casing Film Manufacturing |
| title_full | Changes in Structures and Properties of Collagen Fibers during Collagen Casing Film Manufacturing |
| title_fullStr | Changes in Structures and Properties of Collagen Fibers during Collagen Casing Film Manufacturing |
| title_full_unstemmed | Changes in Structures and Properties of Collagen Fibers during Collagen Casing Film Manufacturing |
| title_short | Changes in Structures and Properties of Collagen Fibers during Collagen Casing Film Manufacturing |
| title_sort | changes in structures and properties of collagen fibers during collagen casing film manufacturing |
| topic | collagen casings collagen fiber manufacturing process triple-helix structure |
| url | https://www.mdpi.com/2304-8158/12/9/1847 |
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