The Structural Characteristics of Collagen in Swim Bladders with 25-Year Sequence Aging: The Impact of Age

Aged swim bladders from the yellow drum (<i>Protonibea diacanthus</i>) are considered collagen-based functional food with extremely high market value. The structural integrity of collagen may be crucial for its biological functions. In the current study, swim bladders with 25-year-old se...

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Main Authors: Xiaofeng He, Liling Xie, Xiaoshan Zhang, Fan Lin, Xiaobo Wen, Bo Teng
Format: Article
Language:English
Published: MDPI AG 2021-05-01
Series:Applied Sciences
Subjects:
Online Access:https://www.mdpi.com/2076-3417/11/10/4578
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author Xiaofeng He
Liling Xie
Xiaoshan Zhang
Fan Lin
Xiaobo Wen
Bo Teng
author_facet Xiaofeng He
Liling Xie
Xiaoshan Zhang
Fan Lin
Xiaobo Wen
Bo Teng
author_sort Xiaofeng He
collection DOAJ
description Aged swim bladders from the yellow drum (<i>Protonibea diacanthus</i>) are considered collagen-based functional food with extremely high market value. The structural integrity of collagen may be crucial for its biological functions. In the current study, swim bladders with 25-year-old sequences were collected and found to be basically composed of collagen. Then, thermogravimetry (TG), differential scanning calorimetry (DSC), X-ray diffraction (XRD), and attenuated total reflectance–Fourier transform infrared spectroscopy (ATR–FTIR) were conducted to evaluate the integrity of the peptide chain and triple helix in the collagen. The structures of microfibers and fiber bundles were revealed with atomic force microscopy (AFM), scanning electrical microscopy (SEM), and optical spectroscopy. The collagens in the aged swim bladders were found to have similar thermal properties to those of fresh ones, but the relative content of the triple helixes was found to be negatively correlated with aging. The secondary structure of the remaining triple helix showed highly retained characteristics as in fresh swim bladders, and the microfibrils also showed a similar D-period to that of the fresh one. However, the fiber bundles displayed more compact and thick characteristics after years of storage. These results indicate that despite 25 years of aging, the collagen in the swim bladders was still partially retained with structures.
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spelling doaj.art-9934b44ddc8648baa715435bf90a25bc2023-11-21T20:06:46ZengMDPI AGApplied Sciences2076-34172021-05-011110457810.3390/app11104578The Structural Characteristics of Collagen in Swim Bladders with 25-Year Sequence Aging: The Impact of AgeXiaofeng He0Liling Xie1Xiaoshan Zhang2Fan Lin3Xiaobo Wen4Bo Teng5College of Science, Shantou University, Shantou 515063, ChinaCollege of Science, Shantou University, Shantou 515063, ChinaAnalysis and Testing Center, Shantou University, Shantou 515063, ChinaGuangdong Provincial Key Laboratory of Marine Biotechnology, Shantou University, Shantou 515063, ChinaCollege of Marine Sciences, South China Agricultural University, Guangzhou 510642, ChinaGuangdong Provincial Key Laboratory of Marine Biotechnology, Shantou University, Shantou 515063, ChinaAged swim bladders from the yellow drum (<i>Protonibea diacanthus</i>) are considered collagen-based functional food with extremely high market value. The structural integrity of collagen may be crucial for its biological functions. In the current study, swim bladders with 25-year-old sequences were collected and found to be basically composed of collagen. Then, thermogravimetry (TG), differential scanning calorimetry (DSC), X-ray diffraction (XRD), and attenuated total reflectance–Fourier transform infrared spectroscopy (ATR–FTIR) were conducted to evaluate the integrity of the peptide chain and triple helix in the collagen. The structures of microfibers and fiber bundles were revealed with atomic force microscopy (AFM), scanning electrical microscopy (SEM), and optical spectroscopy. The collagens in the aged swim bladders were found to have similar thermal properties to those of fresh ones, but the relative content of the triple helixes was found to be negatively correlated with aging. The secondary structure of the remaining triple helix showed highly retained characteristics as in fresh swim bladders, and the microfibrils also showed a similar D-period to that of the fresh one. However, the fiber bundles displayed more compact and thick characteristics after years of storage. These results indicate that despite 25 years of aging, the collagen in the swim bladders was still partially retained with structures.https://www.mdpi.com/2076-3417/11/10/4578collagentriple helix structureswim bladderaging
spellingShingle Xiaofeng He
Liling Xie
Xiaoshan Zhang
Fan Lin
Xiaobo Wen
Bo Teng
The Structural Characteristics of Collagen in Swim Bladders with 25-Year Sequence Aging: The Impact of Age
Applied Sciences
collagen
triple helix structure
swim bladder
aging
title The Structural Characteristics of Collagen in Swim Bladders with 25-Year Sequence Aging: The Impact of Age
title_full The Structural Characteristics of Collagen in Swim Bladders with 25-Year Sequence Aging: The Impact of Age
title_fullStr The Structural Characteristics of Collagen in Swim Bladders with 25-Year Sequence Aging: The Impact of Age
title_full_unstemmed The Structural Characteristics of Collagen in Swim Bladders with 25-Year Sequence Aging: The Impact of Age
title_short The Structural Characteristics of Collagen in Swim Bladders with 25-Year Sequence Aging: The Impact of Age
title_sort structural characteristics of collagen in swim bladders with 25 year sequence aging the impact of age
topic collagen
triple helix structure
swim bladder
aging
url https://www.mdpi.com/2076-3417/11/10/4578
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