Department of Agricultural and Food Engineering, Indian Institute of Technology Kharagpur, Kharagpur, West Bengal 721302, India.
Department of Agricultural and Food Engineering, Indian Institute of Technology Kharagpur, Kharagpur, West Bengal 721302, India.
Food Chem. 2024 Jul 30;447:138914. doi: 10.1016/j.foodchem.2024.138914. Epub 2024 Mar 6.
The modification in structural, rheological, and techno-functional characteristics of soy and pea protein isolates (SPI and PPI) due to dielectric barrier discharge cold plasma (DBD-CP) were assessed. The increased carbonyl groups in both samples with cold plasma (CP) treatment led to a reduction in free sulfhydryl groups. Moreover, protein solubility of treated proteins exhibited significant improvements, reaching up to 59.07 % and 41.4 % for SPI and PPI, respectively, at 30 kV for 8 min. Rheological analyses indicated that storage modulus (G') was greater than loss modulus (G″) for CP-treated protein gels. Furthermore, in vitro protein digestibility of SPI exhibited a remarkable improvement (4.78 %) at 30 kV for 6 min compared to PPI (3.23 %). Spectroscopic analyses, including circular dichroism and Fourier Transform-Raman, indicated partial breakdown and loss of α-helix structure in both samples, leading to the aggregation of proteins. Thus, DBD-CP induces reactive oxygen species-mediated oxidation, modifying the secondary and tertiary structures of samples.
评估了介电阻挡放电冷等离子体（DBD-CP）对大豆和豌豆分离蛋白（SPI 和 PPI）结构、流变和工艺功能特性的改性。与冷等离子体（CP）处理的两种样品中的羰基基团增加导致游离巯基基团减少。此外，处理后的蛋白质的蛋白质溶解度显著提高，在 30 kV 下处理 8 分钟后，SPI 和 PPI 的蛋白质溶解度分别达到 59.07%和 41.4%。流变分析表明，CP 处理的蛋白质凝胶的储能模量（G'）大于损耗模量（G"）。此外，与 PPI（3.23%）相比，SPI 的体外蛋白质消化率在 30 kV 下处理 6 分钟时显著提高（4.78%）。包括圆二色性和傅里叶变换拉曼在内的光谱分析表明，两种样品的α-螺旋结构都发生了部分断裂和损失，导致蛋白质聚集。因此，DBD-CP 诱导活性氧介导的氧化，从而改变样品的二级和三级结构。
