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首页> 外文期刊>Food Science & Nutrition >Food functionality of protein isolates extracted from Yellowfin Tuna ( Thunnus albacares ) roe using alkaline solubilization and acid precipitation process
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Food functionality of protein isolates extracted from Yellowfin Tuna ( Thunnus albacares ) roe using alkaline solubilization and acid precipitation process

机译:用碱性溶解和酸沉淀工艺从黄鳍金枪鱼(Thunnus Albacares)Roe中提取的蛋白质分离物的食物功能

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摘要

Four types of roe protein isolates (RPIs) were prepared through the alkaline solubilization and acid precipitation (ASAP) process, and their functional properties and in vitro bioactivities were evaluated. Higher buffer capacity in pH‐shift range of 8–12 was found in RPI‐1 (pH 11/4.5), required average 94.5 mM NaOH than that of other RPIs to change the pH by 1 unit. All the samples of 1% dispersion (w/v) showed the lowest buffering capacity near the initial pH. The water‐holding capacities (WHC) of RPIs and casein as controls without pH‐shift were in range of 3.7–4.0 g/g protein, and there were no significant differences ( p? ? 0.05). At pH 2 and 8–12 with pH‐shift, WHC and protein solubility of RPIs were significantly improved compared to those of controls. Foaming capacities of RPI‐1 and RPI‐3 were 141.9% and 128.1%, respectively, but those of RPI‐2 and RPI‐4 were not detected. The oil‐in‐water emulsifying activity index of RPI‐1 and RPI‐3 was 10.0 and 8.3?m 2 /g protein, which was not statistically different from casein (7.0?m 2 /g), but lower than that of hemoglobin (19.1?m 2 /g). Overall, RPIs, casein, and hemoglobin exhibited lower food functionality at pH 4–6 near isoelectric points. Through the pH‐shift treatment, the food functionalities of RPIs were improved over the controls, especially in the pH 2 and pH 8–12 ranges. RPI also showed in vitro antioxidant and antihypertensive activities. Therefore, it has been confirmed that RPI extracted from yellowfin tuna roe has high utility as a protein‐ or food‐functional‐enhancing material or protein substitute resource for noodles, confectionery, baking, and surimi‐based products.
机译:通过碱性溶解和酸沉淀(ASAP)方法制备四种类型的ROE蛋白分离株(RPI),并评估其功能性和体外生物活性。在RPI-1(pH11 / 4.5)中发现了8-12的pH转移范围的更高的缓冲能力,需要平均94.5mm NaOH,而不是其他RPI将pH改变1单位。 1%分散体(W / V)的所有样品显示出初始pH附近的最低缓冲能力。 RPI和酪蛋白的水保持容量(WHC)作为没有pH型移位的对照为3.7-4.0g / g蛋白,没有显着差异(p?> 0.05)。在pH 2和8-12具有pH型偏移,与对照相比,RPI的WHC和蛋白质溶解度显着改善。 RPI-1和RPI-3的发泡能力分别为141.9%和128.1%,但没有检测到RPI-2和RPI-4的那些。 RPI-1和RPI-3的水包油乳化活性指数为10.0和8.3?m 2 / g蛋白,其与酪蛋白(7.0×m 2 / g)无统计学不同,但低于血红蛋白的蛋白质(19.1?m 2 / g)。总体而言,RPI,酪蛋白和血红蛋白在等电点附近的pH 4-6下表现出较低的食物功能。通过pH转移处理,RPI的食物功能在对照上得到改善,特别是在pH 2和pH8-12范围内。 RPI还显示出体外抗氧化和抗高血压活动。因此,已经证实,从黄鳍金枪鱼ROE提取的RPI具有高效用作为面条,糖果,烘焙和基于SURIMI的产品的蛋白质或食物功能增强材料或蛋白质替代资源。

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