Uchida Denise Tiemi, Volnistem Adriane do Nascimento, Cook Michael Thomas, Bruschi Marcos Luciano
Laboratory of Research and Development of Drug Delivery Systems, Postgraduate Program in Pharmaceutical Sciences, Department of Pharmacy, State University of Maringa, Colombo Avenue, 5790, K68, Rooms 210-214, Maringa, Paraná 87020-900, Brazil.
Department of Physics, State University of Maringa, Colombo Avenue, 5790, Maringa, Paraná 87020-900, Brazil.
ACS Omega. 2025 Aug 7;10(32):35809-35826. doi: 10.1021/acsomega.5c02637. eCollection 2025 Aug 19.
Collagen from the skin of (Tilapia; TS) has gained visibility due to its extraction from waste materials from slaughterhouses, reducing environmental impacts, and because it is biodegradable, biocompatible, and nontoxic. The aim of this work was to evaluate the impact of two extraction methods on the physicochemical characteristics of collagen from TS for pharmaceutical and biomedical applications. The obtained TS was analyzed for its proximate composition. Two types of extractions were conducted using a 2 factorial design: acidic extraction (COL) and acidic extraction using pepsin (pCOL). The characterization of collagen was performed using rheological analyses, Raman spectroscopy, differential scanning calorimetry (DSC), thermogravimetric analysis (TGA), X-ray diffraction (XRD), circular dichroism, and scanning electron microscopy (SEM). The acid extraction method was effective in obtaining collagen both with and without pepsin. The proximate composition of the raw material showed results consistent with those of previous studies, highlighting the quality of collagen for use in pharmaceutical formulations. The extraction COL yielded more than pCOL, with both yields being close to 10%. The denaturation temperature of the collagen was above 32 °C, confirmed by DSC, TGA, and circular dichroism analyses, which is favorable for the intended applications. XRD revealed that the supramolecular structure of the type I collagen was preserved. Raman spectroscopy confirmed the presence of hydroxyproline and characteristic collagen amides, with the pCOL6 extraction showing greater stability. Structural differences between COL5 and pCOL6 were observed in the SEM micrographs, suggesting the potential for future applications in the pharmaceutical and biomedical areas.
罗非鱼皮胶原蛋白（TS）因其从屠宰场废料中提取，减少了环境影响，且具有生物可降解性、生物相容性和无毒特性而受到关注。本研究旨在评估两种提取方法对TS胶原蛋白用于制药和生物医学应用时物理化学特性的影响。对所得TS进行了近似成分分析。采用二因素设计进行了两种类型的提取：酸性提取（COL）和使用胃蛋白酶的酸性提取（pCOL）。通过流变学分析、拉曼光谱、差示扫描量热法（DSC）、热重分析（TGA）、X射线衍射（XRD）、圆二色性和扫描电子显微镜（SEM）对胶原蛋白进行了表征。酸性提取方法无论有无胃蛋白酶都能有效获得胶原蛋白。原料的近似成分结果与先前研究一致，突出了用于药物制剂的胶原蛋白质量。COL提取的产量高于pCOL，两者产量均接近10%。通过DSC、TGA和圆二色性分析证实，胶原蛋白的变性温度高于32°C，这有利于预期应用。XRD显示I型胶原蛋白的超分子结构得以保留。拉曼光谱证实了羟脯氨酸和特征性胶原蛋白酰胺的存在，pCOL6提取显示出更高的稳定性。在SEM显微照片中观察到COL5和pCOL6之间的结构差异，表明其在制药和生物医学领域未来应用的潜力。
