Effect of pH on the Structure, Functional Properties and Rheological Properties of Collagen from Greenfin Horse-Faced Filefish (<i>Thamnaconus septentrionalis</i>) Skin
Collagen is an important biopolymer widely used in food, cosmetics and biomedical applications. Understanding the effect of pH on the structure and properties of collagen is beneficial for its further processing and exploitation. In this study, greenfin horse-faced filefish skin collagen (GHSC) was...
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MDPI AG
2024-01-01
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| Series: | Marine Drugs |
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| Online Access: | https://www.mdpi.com/1660-3397/22/1/45 |
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| author | Kunyuan Wu Yushuang Li Junde Chen |
| author_facet | Kunyuan Wu Yushuang Li Junde Chen |
| author_sort | Kunyuan Wu |
| collection | DOAJ |
| description | Collagen is an important biopolymer widely used in food, cosmetics and biomedical applications. Understanding the effect of pH on the structure and properties of collagen is beneficial for its further processing and exploitation. In this study, greenfin horse-faced filefish skin collagen (GHSC) was prepared and identified as a type I collagen. We systematically investigated the effect of pH on the structural, functional and rheological properties of GHSC. Scanning electron microscopy showed that the collagen morphology changed from an ordered stacked sheet structure to a rough silk-like structure as pH increased. Gaussian-fitted Fourier infrared spectroscopy results of the collagen revealed that it unfolded with increasing pH. Moreover, the ordered structure was reduced, and random coils became the dominant conformation. Its β-sheet and random coil contents increased from 18.43 ± 0.08 and 33.62 ± 0.17 to 19.72 ± 0.02 and 39.53 ± 1.03%, respectively, with increasing pH. α-helices and β-turns decreased from 35.00 ± 0.26 and 12.95 ± 0.01 to 29.39 ± 0.92 and 11.36 ± 0.10%, respectively. The increase in β-sheets and random coils allowed the pI-treated collagen to exhibit maximum water contact angle. The emulsification and foaming properties decreased and then increased with increasing pH in a V-shape. The increased net surface charge and β-sheets in collagen benefited its emulsification and foaming properties. The rheological results showed that the protoprotein exhibited shear-thinning properties in all pH ranges. The collagen solutions showed liquid-like behaviour in low-pH (2, 4) solutions and solid-like behaviour in high-pH (6, 7.83 and 10) solutions. Moreover, the frequency-dependent properties of the storage modulus (G′) and loss modulus (G″) of the collagen solutions weakened with increasing pH. Collagen has considerable frequency-dependent properties of G′ and G″ at low pH (2, 4). Thus, the importance of collagen raw material preparation for subsequent processing was emphasised, which may provide new insights into applying collagen-based materials in food, biomaterials and tissue engineering. |
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| language | English |
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| publishDate | 2024-01-01 |
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| series | Marine Drugs |
| spelling | doaj.art-b9f2591e556544a88229b2c1ecb8212e2024-01-26T17:26:16ZengMDPI AGMarine Drugs1660-33972024-01-012214510.3390/md22010045Effect of pH on the Structure, Functional Properties and Rheological Properties of Collagen from Greenfin Horse-Faced Filefish (<i>Thamnaconus septentrionalis</i>) SkinKunyuan Wu0Yushuang Li1Junde Chen2Technical Innovation Center for Utilization of Marine Biological Resources, Third Institute of Oceanography, Ministry of Natural Resources, Xiamen 361005, ChinaTechnical Innovation Center for Utilization of Marine Biological Resources, Third Institute of Oceanography, Ministry of Natural Resources, Xiamen 361005, ChinaTechnical Innovation Center for Utilization of Marine Biological Resources, Third Institute of Oceanography, Ministry of Natural Resources, Xiamen 361005, ChinaCollagen is an important biopolymer widely used in food, cosmetics and biomedical applications. Understanding the effect of pH on the structure and properties of collagen is beneficial for its further processing and exploitation. In this study, greenfin horse-faced filefish skin collagen (GHSC) was prepared and identified as a type I collagen. We systematically investigated the effect of pH on the structural, functional and rheological properties of GHSC. Scanning electron microscopy showed that the collagen morphology changed from an ordered stacked sheet structure to a rough silk-like structure as pH increased. Gaussian-fitted Fourier infrared spectroscopy results of the collagen revealed that it unfolded with increasing pH. Moreover, the ordered structure was reduced, and random coils became the dominant conformation. Its β-sheet and random coil contents increased from 18.43 ± 0.08 and 33.62 ± 0.17 to 19.72 ± 0.02 and 39.53 ± 1.03%, respectively, with increasing pH. α-helices and β-turns decreased from 35.00 ± 0.26 and 12.95 ± 0.01 to 29.39 ± 0.92 and 11.36 ± 0.10%, respectively. The increase in β-sheets and random coils allowed the pI-treated collagen to exhibit maximum water contact angle. The emulsification and foaming properties decreased and then increased with increasing pH in a V-shape. The increased net surface charge and β-sheets in collagen benefited its emulsification and foaming properties. The rheological results showed that the protoprotein exhibited shear-thinning properties in all pH ranges. The collagen solutions showed liquid-like behaviour in low-pH (2, 4) solutions and solid-like behaviour in high-pH (6, 7.83 and 10) solutions. Moreover, the frequency-dependent properties of the storage modulus (G′) and loss modulus (G″) of the collagen solutions weakened with increasing pH. Collagen has considerable frequency-dependent properties of G′ and G″ at low pH (2, 4). Thus, the importance of collagen raw material preparation for subsequent processing was emphasised, which may provide new insights into applying collagen-based materials in food, biomaterials and tissue engineering.https://www.mdpi.com/1660-3397/22/1/45collagenpHsecondary structurefunctional propertiesrheological properties |
| spellingShingle | Kunyuan Wu Yushuang Li Junde Chen Effect of pH on the Structure, Functional Properties and Rheological Properties of Collagen from Greenfin Horse-Faced Filefish (<i>Thamnaconus septentrionalis</i>) Skin Marine Drugs collagen pH secondary structure functional properties rheological properties |
| title | Effect of pH on the Structure, Functional Properties and Rheological Properties of Collagen from Greenfin Horse-Faced Filefish (<i>Thamnaconus septentrionalis</i>) Skin |
| title_full | Effect of pH on the Structure, Functional Properties and Rheological Properties of Collagen from Greenfin Horse-Faced Filefish (<i>Thamnaconus septentrionalis</i>) Skin |
| title_fullStr | Effect of pH on the Structure, Functional Properties and Rheological Properties of Collagen from Greenfin Horse-Faced Filefish (<i>Thamnaconus septentrionalis</i>) Skin |
| title_full_unstemmed | Effect of pH on the Structure, Functional Properties and Rheological Properties of Collagen from Greenfin Horse-Faced Filefish (<i>Thamnaconus septentrionalis</i>) Skin |
| title_short | Effect of pH on the Structure, Functional Properties and Rheological Properties of Collagen from Greenfin Horse-Faced Filefish (<i>Thamnaconus septentrionalis</i>) Skin |
| title_sort | effect of ph on the structure functional properties and rheological properties of collagen from greenfin horse faced filefish i thamnaconus septentrionalis i skin |
| topic | collagen pH secondary structure functional properties rheological properties |
| url | https://www.mdpi.com/1660-3397/22/1/45 |
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