Dustin Pomary, Belinda Selase Korkor, B. Asimeng, Solomon Kingsley Katu, Lily Paemka, V. Apalangya, Bismark Mensah, E. J. Foster, E. Tiburu
{"title":"Collagen derived from a giant African snail (Achatina achatina) for biomedical applications","authors":"Dustin Pomary, Belinda Selase Korkor, B. Asimeng, Solomon Kingsley Katu, Lily Paemka, V. Apalangya, Bismark Mensah, E. J. Foster, E. Tiburu","doi":"10.24294/jpse.v7i1.4471","DOIUrl":null,"url":null,"abstract":"Achatina achatina (AA) is a rich source of collagen due to its large size, but it is underutilized. Type I collagen was extracted from AA to serve as an alternative to existing collagen sources. The collagen was extracted at varying alkaline and temperature conditions to determine the optimal parameters that would give a high yield of acid-soluble collagen. The extracted collagen was characterised using X-ray diffraction, Fourier transform infrared (FTIR) spectrometry, thermogravimetric analysis (TGA), and differential scanning calorimetry (DSC) to confirm the integrity and purity of the extracted collagen. The type of collagen was determined using sodium dodecyl sulphate-polyacrylamide gel electrophoresis. The α-1, α-2, and dimer electrophoresis bands confirmed that the collagen is type I, and the XRD data supported the findings. The highest collagen yield was obtained at 4 ℃ for 48 h, which decreased with increasing temperature due to the instability of the protein in acid at high temperatures. A cytotoxicity test was conducted using an Alamar blue assay. The AA collagen-treated normal prostate cell line (PNT2) showed no significant difference from the untreated control cells. The high-quality type I collagen extracted from AA has the potential for biomedical and other industrial applications.","PeriodicalId":503084,"journal":{"name":"Journal of Polymer Science and Engineering","volume":"348 8","pages":""},"PeriodicalIF":0.0000,"publicationDate":"2024-04-15","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Journal of Polymer Science and Engineering","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.24294/jpse.v7i1.4471","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
引用次数: 0
Abstract
Achatina achatina (AA) is a rich source of collagen due to its large size, but it is underutilized. Type I collagen was extracted from AA to serve as an alternative to existing collagen sources. The collagen was extracted at varying alkaline and temperature conditions to determine the optimal parameters that would give a high yield of acid-soluble collagen. The extracted collagen was characterised using X-ray diffraction, Fourier transform infrared (FTIR) spectrometry, thermogravimetric analysis (TGA), and differential scanning calorimetry (DSC) to confirm the integrity and purity of the extracted collagen. The type of collagen was determined using sodium dodecyl sulphate-polyacrylamide gel electrophoresis. The α-1, α-2, and dimer electrophoresis bands confirmed that the collagen is type I, and the XRD data supported the findings. The highest collagen yield was obtained at 4 ℃ for 48 h, which decreased with increasing temperature due to the instability of the protein in acid at high temperatures. A cytotoxicity test was conducted using an Alamar blue assay. The AA collagen-treated normal prostate cell line (PNT2) showed no significant difference from the untreated control cells. The high-quality type I collagen extracted from AA has the potential for biomedical and other industrial applications.
Achatina achatina(AA)因其体积大而成为胶原蛋白的丰富来源,但却未得到充分利用。从 AA 中提取 I 型胶原蛋白可作为现有胶原蛋白来源的替代品。在不同的碱性和温度条件下提取胶原蛋白,以确定获得高产率酸溶性胶原蛋白的最佳参数。使用 X 射线衍射、傅立叶变换红外光谱、热重分析和差示扫描量热法对提取的胶原蛋白进行表征,以确认提取胶原蛋白的完整性和纯度。使用十二烷基硫酸钠-聚丙烯酰胺凝胶电泳法测定胶原蛋白的类型。α-1、α-2 和二聚体电泳条带证实胶原蛋白为 I 型,XRD 数据也支持这一结论。在 4 ℃ 下培养 48 小时后,胶原蛋白的产量最高,但随着温度的升高,产量有所下降,这是因为蛋白质在高温下的酸性不稳定。使用阿拉玛蓝检测法进行了细胞毒性试验。经 AA 胶原处理的正常前列腺细胞系(PNT2)与未经处理的对照细胞无明显差异。从 AA 中提取的高质量 I 型胶原蛋白具有生物医学和其他工业应用的潜力。