School of Food and Biological Engineering, Jiangsu University, 301 Xuefu Road, Zhenjiang, Jiangsu 212013, China; Institute of Food Physical Processing , Jiangsu University, 301 Xuefu Road, Zhenjiang, Jiangsu 212013, China.
School of Food and Biological Engineering, Jiangsu University, 301 Xuefu Road, Zhenjiang, Jiangsu 212013, China; Institute of Applied Chemistry and Biological Engineering, Weifang Engineering Vocational College, 8979 Yunmenshan South Road, Qingzhou, Shandong 262500, China.
Ultrason Sonochem. 2020 May;63:104981. doi: 10.1016/j.ultsonch.2020.104981. Epub 2020 Jan 21.
The instability of allicin makes it easily decomposed into various organic sulfur compounds, resulting in significant decrease in biological activity. In this study, allicin was firstly extracted with water, then bound with whey protein isolates (WPI) which were pretreated by ultrasound to form conjugates, and the stability, water solubility and emulsibility of conjugates were as well investigated. The research results showed that there were no significant differences in the extraction yields of allicin from water, 40% and 80% ethanol. Appropriate frequency (20/40 kHz), power (50 W/L) and time (20 min) of ultrasonic pretreatments significantly increased (P < 0.05) the sulfhydryl groups content of WPI by 35.05% over control, causing improvement in binding ability of protein to allicin. The binding process of allicin-WPI displayed good fit with Elovich kinetic model (R = 0.9781). The mass retention rate of the conjugates (in 60% combination rate) with ultrasonic pretreating kept at 95.97% after 14 days of storage at 25 °C, whereas allicin's mass retention rate was only 61.79% at same storage condition. The water solubility of the prepared conjugates was significantly higher than allicin. And with optimal condition ultrasonic pretreatment of WPI, the conjugates showed the highest emulsifying capacity and emulsion stability (49.56 m/g, 10.06 min). In conclusion, the ultrasonically pretreated allicin-WPI conjugates exhibited better stability, water solubility and emulsifying properties compared to allicin, this expands the application field of allicin.
蒜素的不稳定性使其容易分解为各种有机硫化合物,导致生物活性显著降低。本研究首先用水提取蒜素,然后与乳清蛋白分离物(WPI)结合,WPI 经超声预处理形成结合物,并研究了结合物的稳定性、水溶性和乳化性。研究结果表明,水、40%和 80%乙醇从蒜素中的提取产率没有显著差异。适当的超声预处理频率(20/40 kHz)、功率(50 W/L)和时间(20 min)显著增加了 WPI 的巯基含量(P < 0.05),比对照提高了 35.05%,从而改善了蛋白质与蒜素的结合能力。蒜素-WPI 的结合过程与 Elovich 动力学模型拟合良好(R = 0.9781)。在 25°C 下储存 14 天后,以 60%结合率制备的结合物(经超声预处理)的质量保留率保持在 95.97%,而相同储存条件下蒜素的质量保留率仅为 61.79%。制备的结合物的水溶性明显高于蒜素。并且在 WPI 的最佳超声预处理条件下,结合物表现出最高的乳化能力和乳化稳定性(49.56 m/g,10.06 min)。总之,与蒜素相比,经超声预处理的 WPI-蒜素结合物具有更好的稳定性、水溶性和乳化性能,这扩大了蒜素的应用领域。