Biochemical and structural characterisation of thermostable acid- and pepsin-soluble collagens from South African Geelbek (Atractoscion aequidens) scales and its potential application in film formation

IF 2.2 4区化学 Q2 Engineering

Chemical Papers Pub Date : 2024-11-22 DOI:10.1007/s11696-024-03806-7

Hlalanathi Sibiya, Prashant Bhagwat, Kugenthiren Permaul, Santhosh Pillai

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引用次数: 0

Abstract

Fish processing typically generates large amounts of non-edible by-products, which contain collagen protein as one of the principal constituents. In this study, the biochemical properties, in vitro fibril-forming potential and film-forming potential of acid (ASC)- and pepsin (PSC)-soluble collagens extracted from the scales of geelbek (Atractoscion aequidens) were evaluated. Based on ultraviolet absorption spectroscopy, electrophoretic pattern, Fourier transform infrared (FTIR) spectroscopy, and scanning electron microscopy (SEM) analysis, both ASC and PSC were classified as type I collagen. Further, amino acid composition analyses confirmed the presence of 326 and 319 glycine residues/1000 residues in ASC and PSC, respectively, which is characteristic of collagen. The collagens were thermally stable, with a maximum transition temperature of 112.27 °C for ASC and 113.41 °C for PSC. The collagens also demonstrated excellent fibril-forming potential, as indicated by SEM analysis. Being a bioactive material, the extracted collagen was further utilised to prepare collagen–chitosan films. The presence of collagen–chitosan interaction was revealed by FTIR spectra examination of the films, confirming a favourable modification of collagen’s secondary structure. Colour, differential scanning calorimetry and dynamic mechanical analysis demonstrated that the collagen–chitosan films had moderate colour indices and enhanced thermal properties. Overall, this study offers insights into biomaterial fabrication using geelbek collagen that could potentially be useful in the biomedical and food industries.

Graphical abstract

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南非 Geelbek（白术）鳞片中可溶于热稳定酸和胃蛋白酶的胶原的生物化学和结构特征及其在薄膜形成中的潜在应用

鱼类加工通常会产生大量不可食用的副产品，其中的主要成分之一就是胶原蛋白。本研究评估了从白术（Atractoscion aequidens）鳞片中提取的酸（ASC）和胃蛋白酶（PSC）可溶性胶原蛋白的生化特性、体外成纤潜力和成膜潜力。根据紫外线吸收光谱、电泳图谱、傅立叶变换红外光谱（FTIR）和扫描电子显微镜（SEM）分析，ASC 和 PSC 均被归类为 I 型胶原蛋白。此外，氨基酸组成分析证实，ASC 和 PSC 中分别含有 326 和 319 个甘氨酸残基/1000 个残基，这是胶原蛋白的特征。这些胶原具有热稳定性，ASC 和 PSC 的最高转变温度分别为 112.27 ℃ 和 113.41 ℃。扫描电镜分析表明，这些胶原还具有良好的纤维形成潜力。作为一种生物活性材料，提取的胶原蛋白被进一步用于制备胶原蛋白-壳聚糖薄膜。薄膜的傅立叶变换红外光谱分析显示了胶原蛋白与壳聚糖之间的相互作用，证实了胶原蛋白二级结构的良好改性。颜色、差示扫描量热和动态机械分析表明，胶原蛋白-壳聚糖薄膜具有适度的颜色指数和更强的热性能。总之，这项研究为使用吉尔贝克胶原蛋白制造生物材料提供了见解，这种生物材料有可能在生物医学和食品工业中发挥作用。

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来源期刊

Chemical Papers Chemical Engineering-General Chemical Engineering

CiteScore

3.30

自引率

4.50%

发文量

590

期刊介绍： Chemical Papers is a peer-reviewed, international journal devoted to basic and applied chemical research. It has a broad scope covering the chemical sciences, but favors interdisciplinary research and studies that bring chemistry together with other disciplines.