Laboratoire de Valorisation, Analyses et Sécurité des Aliments, Université de Sfax, École Nationale d'Ingénieurs de Sfax, Route de Soukra, 3038 Sfax, Tunisia.
Laboratoire de Biochimie et de Génie Enzymatique des Lipases, Université de Sfax, École Nationale d'Ingénieurs de Sfax, Route de Soukra, 3038 Sfax, Tunisia.
Int J Biol Macromol. 2019 Apr 1;126:454-465. doi: 10.1016/j.ijbiomac.2018.12.198. Epub 2018 Dec 23.
The main purpose of this work was to investigate some physiochemical and antioxidant properties of purified proteins of 18 kDa from black cumin seeds. The structural properties of purified proteins were characterized using Fourier Transform-Infrared spectroscopy (FT-IR) and Circular dichroism (CD) spectroscopy analysis. The Tunisian purified protein exhibited a α-helix structure and the Turkish purified protein adopted a β-sheet conformation. The thermal properties were also evaluated by differential scanning calorimetry (DSC). The Tunisian purified protein presented two endothermic peaks, the first one was at 76.71 °C and the second one was at 131.32 °C. However, only one endothermic peak was found for the Turkish purified protein at 157.63 °C. Both Tunisian and Turkish purified proteins were very stable towards heat-induced denaturation. In addition, the effect of pH, salt (NaCl and NaSO) and temperature on functional properties was investigated. The Tunisian black cumin seeds pure protein exhibited better antioxidant activity than that of the Turkish one at all tested concentrations (0.2 to 1 mg/mL) and temperatures (50 °C, 75 °C and 100 °C), as well as after gastrointestinal digestion simulation.
本工作的主要目的是研究黑孜然种子中 18 kDa 纯化蛋白的一些理化和抗氧化性质。采用傅里叶变换红外光谱(FT-IR)和圆二色性(CD)光谱分析对纯化蛋白的结构特性进行了表征。突尼斯纯化蛋白表现出α-螺旋结构,而土耳其纯化蛋白则采用β-折叠构象。通过差示扫描量热法(DSC)还评估了热性质。突尼斯纯化蛋白呈现出两个吸热峰,第一个峰在 76.71°C,第二个峰在 131.32°C。然而,土耳其纯化蛋白仅在 157.63°C 处发现一个吸热峰。突尼斯和土耳其纯化蛋白均对热诱导变性非常稳定。此外,还研究了 pH 值、盐(NaCl 和 NaSO)和温度对功能性质的影响。在所有测试浓度(0.2 至 1mg/mL)和温度(50°C、75°C 和 100°C)下,以及经过胃肠道消化模拟后,突尼斯黑孜然种子纯蛋白表现出比土耳其黑孜然种子纯蛋白更好的抗氧化活性。