Jaziri Abdul Aziz, Shapawi Rossita, Mokhtar Ruzaidi Azli Mohd, Noordin Wan Norhana Md, Huda Nurul
Faculty of Food Science and Nutrition, Universiti Malaysia Sabah, Kota Kinabalu 88400, Malaysia.
Faculty of Fisheries and Marine Science, Universitas Brawijaya, Malang 65145, Indonesia.
Gels. 2022 Jul 27;8(8):471. doi: 10.3390/gels8080471.
Reducing food waste is critical for sustainability. In the case of fish processing, more than sixty percent of by-products are generated as waste. Lizardfish (Saurida tumbil Bloch, 1795) is an economically important species for surimi production. To address waste disposal and maximize income, an effective utilization of fish by-products is essential. This study aims to isolate and characterize pepsin-soluble collagens from the skin, bone and scales of lizardfish. Significant differences (p < 0.05) in the yields of collagen were noted with the highest yield recorded in pepsin-soluble skin collagen (PSSC) (3.50 ± 0.11%), followed by pepsin-soluble bone collagen (PSBC) (3.26 ± 0.10%) and pepsin-soluble scales collagen (PSCC) (0.60 ± 0.65%). Through SDS−polyacrylamide gel electrophoresis, the presence of two alpha chains were noted and classified as type I. From Fourier transform infrared spectroscopy (FTIR) analysis, the triple-helix structure of the collagen was maintained. The X-ray diffraction and UV visible spectra characteristics of the lizardfish collagens in this study are similar to the previously reported fish collagens. In terms of thermostability, PSSC (Tmax = 43.89 °C) had higher thermostability in comparison to PSBC (Tmax = 31.75 °C) and PSCC (Tmax = 30.54 °C). All pepsin-soluble collagens were highly soluble (>70%) in acidic conditions (particularly at pH 4.0) and at low sodium chloride concentrations (0−30 g/L). Microstructural analysis depicted that all extracted collagens were multi-layered, irregular, dense, sheet-like films linked by random coiled filaments. Overall, pepsin-soluble collagens from lizardfish skin, bone and scales could serve as potential alternative sources of collagens.
减少食物浪费对可持续发展至关重要。就鱼类加工而言，超过60%的副产物被作为废弃物产生。蜥鱼（Saurida tumbil Bloch，1795）是用于生产鱼糜的一种具有重要经济价值的物种。为了解决废物处理问题并使收入最大化，有效利用鱼类副产物至关重要。本研究旨在从蜥鱼的皮肤、骨骼和鳞片中分离并表征胃蛋白酶可溶性胶原蛋白。胶原蛋白产量存在显著差异（p < 0.05），胃蛋白酶可溶性皮肤胶原蛋白（PSSC）的产量最高（3.50 ± 0.11%），其次是胃蛋白酶可溶性骨胶原蛋白（PSBC）（3.26 ± 0.10%）和胃蛋白酶可溶性鳞片胶原蛋白（PSCC）（0.60 ± 0.65%）。通过SDS - 聚丙烯酰胺凝胶电泳，观察到两条α链的存在并归类为I型。从傅里叶变换红外光谱（FTIR）分析来看，胶原蛋白的三螺旋结构得以保持。本研究中蜥鱼胶原蛋白的X射线衍射和紫外可见光谱特征与先前报道的鱼类胶原蛋白相似。在热稳定性方面，与PSBC（Tmax = 31.75 °C）和PSCC（Tmax = 30.54 °C）相比，PSSC（Tmax = 43.89 °C）具有更高的热稳定性。所有胃蛋白酶可溶性胶原蛋白在酸性条件下（特别是在pH 4.0时）和低氯化钠浓度（0 - 30 g/L）下具有高溶解性（>70%）。微观结构分析表明，所有提取的胶原蛋白都是由无规卷曲细丝连接的多层、不规则、致密、片状薄膜。总体而言，来自蜥鱼皮肤、骨骼和鳞片的胃蛋白酶可溶性胶原蛋白可作为胶原蛋白的潜在替代来源。
