College of Life Science, Linyi University, Linyi 276005, China.
College of Life Science, Linyi University, Linyi 276005, China.
Int J Biol Macromol. 2023 Dec 31;253(Pt 7):127500. doi: 10.1016/j.ijbiomac.2023.127500. Epub 2023 Oct 17.
To improve the hydration properties of high-temperature pressed peanut protein isolate (HPPI), we investigated the effect of cold plasma (CP) oxidation on functional and structural properties. Compared to HPPI, the hydrated molecules number and the surface contact angle were significantly decreased at 70 W, from 77.2 × 10 to 17.7 × 10 and from 85.74° to 57.81°, respectively. The reduction of the sulfhydryl content and the increase of the disulfide bond and di-tyrosine content indicated that the structural transformation was affected by the oxidation effect. In terms of structural changes, a stretched tertiary structure, ordered secondary structure, and rough apparent structure were observed after CP treatment. Additionally, the enhancement of surface free energy and group content such as -COOH, -CO and -OH on the surface of HPPI contributed to the formation of hydrated crystal structures. In general, the oxidation effect of CP effectively improved the hydration properties of HPPI and broaden its application field.
为改善高温压榨花生分离蛋白（HPPI）的水合性质，研究了冷等离子体（CP）氧化对其功能和结构性质的影响。与 HPPI 相比，70 W 时水合分子数量和表面接触角分别显著降低，从 77.2×10 降至 17.7×10，从 85.74°降至 57.81°。巯基含量减少，二硫键和二酪氨酸含量增加，表明结构转化受氧化作用影响。就结构变化而言，CP 处理后观察到三级结构拉伸、二级结构有序和表观结构粗糙。此外，HPPI 表面表面自由能和 -COOH、-CO 和 -OH 等基团含量的增加有助于形成水合晶体结构。总的来说，CP 的氧化作用有效改善了 HPPI 的水合性质，拓宽了其应用领域。
