Facultad de Ingenieria, Universidad Nacional de Jujuy, Centro Interdisciplinario de Investigaciones en Tecnologías y Desarrollo Social para el NOA (CIITED-CONICET-Universidad Nacional de Jujuy), San Salvador de Jujuy, Argentina.
J Sci Food Agric. 2023 Aug 30;103(11):5242-5252. doi: 10.1002/jsfa.12612. Epub 2023 Apr 19.
Protein-pectin conjugates, obtained through a controlled Maillard reaction in blends of precursors, are studied for their contribution to improving the emulsifying and thermal properties of proteins. The objective was to obtain a conjugate between whey protein concentrate (WPC) and non-conventional pectins extracted in acid (acid tomato pectin, ATP) and aqueous medium (water tomato pectin, WTP) from industrialized tomato residues (tomato waste, TW), characterize the conjugates and study their emulsion properties. The Maillard reaction was carried out at 60 °C and 75% relative humidity in blends with 2:1 proportions; 1:1 and 1:2 (m :m ) for 3, 6 and 12 days. Conjugates were compared concerning treated and untreated WPC.
The WPC-ATP conjugate showed significant increases in color difference (ΔE). The electrophoresis profile of the conjugates showed diffuse bands of molecular weight between 37 and 250 kDa and a reduction in the intensity of bands characteristic of WPC (α-lactalbumin and β-lactoglobulin). Thermal analysis showed an increase in the peak temperature and a reduction in the enthalpy change in protein denaturation, associated with the formation of conjugates. The infrared spectroscopy of the conjugates, in the amide III zone (1300-1100 cm ), indicated an increase in the relative peak area associated with the unfolding and exhibition of the hydrophobic zones of the WPC fraction. The emulsions formulated with the conjugates showed a significant increase in the emulsifying stability index (ESI) (P < 0.05) concerning the treated and untreated WPC emulsions.
The formation of conjugates increased the emulsifying properties and improved the thermal stability of WPC, showing an innovative and alternative food ingredient too. © 2023 Society of Chemical Industry.
通过在预混物的受控美拉德反应中获得的蛋白质-果胶缀合物，因其对改善蛋白质的乳化和热性质的贡献而受到研究。目的是获得乳清蛋白浓缩物（WPC）与从工业化番茄废物（番茄废物，TW）中提取的非传统果胶（酸性番茄果胶，ATP 和水相番茄果胶，WTP）之间的缀合物，对其进行表征并研究其乳液特性。美拉德反应在 60°C 和 75%相对湿度下进行，在 2:1 比例的混合物中进行；对于 3、6 和 12 天，比例为 1:1 和 1:2（m：m）。比较了缀合物与未处理的 WPC。
WPC-ATP 缀合物的色差（ΔE）显著增加。缀合物的电泳图谱显示分子量在 37 至 250 kDa 之间的弥散带，并且 WPC 的特征带的强度降低（α-乳白蛋白和β-乳球蛋白）。热分析表明，峰温度升高，蛋白质变性焓变降低，与缀合物的形成有关。在酰胺 III 区（1300-1100 cm）的缀合物的红外光谱中，与 WPC 部分展开和暴露的疏水区相关的相对峰面积增加。与处理过和未处理过的 WPC 乳液相比，用缀合物配制的乳液的乳化稳定性指数（ESI）显著增加（P<0.05）。
缀合物的形成增加了 WPC 的乳化性能并提高了其热稳定性，同时也展示了一种创新的替代食品成分。© 2023 化学工业协会。
