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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:利用碱性增溶和酸沉淀法从黄鳍金枪鱼籽中提取的蛋白质分离物的食品功能

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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 style="fixed-case">RPIs were significantly improved compared to those of controls. Foaming capacities of style="fixed-case">RPI‐1 and style="fixed-case">RPI‐3 were 141.9% and 128.1%, respectively, but those of style="fixed-case">RPI‐2 and style="fixed-case">RPI‐4 were not detected. The oil‐in‐water emulsifying activity index of style="fixed-case">RPI‐1 and style="fixed-case">RPI‐3 was 10.0 and 8.3 m2/g protein, which was not statistically different from casein (7.0 m2/g), but lower than that of hemoglobin (19.1 m2/g). Overall, style="fixed-case">RPIs, casein, and hemoglobin exhibited lower food functionality at style="fixed-case">pH 4–6 near isoelectric points. Through the style="fixed-case">pH‐shift treatment, the food functionalities of style="fixed-case">RPIs were improved over the controls, especially in the style="fixed-case">pH 2 and style="fixed-case">pH 8–12 ranges. style="fixed-case">RPI also showed in vitro antioxidant and antihypertensive activities. Therefore, it has been confirmed that style="fixed-case">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:通过碱溶化和酸沉淀(ASAP)工艺制备了四种鱼卵分离蛋白(RPI),并对其功能特性和体外生物活性进行了评估。在RPI-1(pH 11 / 4.5)中发现,在8-12的pH位移范围内具有更高的缓冲容量,与其他RPI相比,平均需要94.5 mM NaOH才能将pH改变1个单位。所有1%分散度(w / v)的样品在初始pH值附近显示出最低的缓冲能力。 RPI和酪蛋白作为无pH值变化的对照的持水量(WHC)在3.7–4.0 g / g蛋白质范围内,没有显着差异(p> 0.05)。在pH值为2和8-12且具有pH偏移的情况下,与对照组相比, style =“ fixed-case”> RPI s的WHC和蛋白质溶解度显着提高。 style =“ fixed-case”> RPI -1和 style =“ fixed-case”> RPI -3的发泡能力分别为141.9%和128.1%,但未检测到 style =“ fixed-case”> RPI ‐2和 style =“ fixed-case”> RPI ‐4。 style =“ fixed-case”> RPI -1和 style =“ fixed-case”> RPI -3的水包油乳化活性指数分别为10.0和8.3 m 2 / g蛋白,与酪蛋白无差异(7.0m 2 / g),但低于血红蛋白(19.1m 2 / g)。总体而言, style =“ fixed-case”> RPI s,酪蛋白和血红蛋白在等电点附近的 style =“ fixed-case”> pH 4–6处显示较低的食物功能。通过 style =“ fixed-case”> pH -shift处理,与对照相比, style =“ fixed-case”> RPI s的食品功能得到了改善,尤其是在 style =“ fixed-case”> pH 2和 style =“ fixed-case”> pH 8-12范围。 style =“ fixed-case”> RPI 还显示了体外抗氧化和降压活性。因此,已经证实,从黄鳍金枪鱼籽中提取的 style =“ fixed-case”> RPI 作为面条,糖食,烘焙和鱼糜类产品。

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