Abadía-García Lucía, Castaño-Tostado Eduardo, Cardador-Martínez Anaberta, Martín-Del-Campo Sandra Teresita, Amaya-Llano Silvia L
Facultad de Química, Universidad Autónoma de Querétaro, Querétaro 76010, Mexico.
Tecnologico de Monterrey, Escuela de Ingeniería y Ciencias, Querétaro 76130, Mexico.
Foods. 2021 Sep 5;10(9):2099. doi: 10.3390/foods10092099.
High Intensity Ultrasound (HIUS) can induce modification of the protein structure. The combination of enzymatic hydrolysis and ultrasound is an interesting strategy to improve the release of the Angiotensin-Converting Enzyme (ACE) inhibitory peptides. In this study, whey proteins were pretreated with HIUS at two levels of amplitude (30 and 50%) for 10 min, followed by hydrolysis using the vegetable protease bromelain. The hydrolysates obtained were ultrafiltrated and their fractions were submitted to a simulated gastrointestinal digestion. The conformational changes induced by HIUS on whey proteins were analyzed using Fourier-transform infrared spectroscopy by attenuated total reflectance (FTIR-ATR) and intrinsic spectroscopy. It was found that both levels of ultrasound pretreatment significantly decreased the IC value (50% Inhibitory Concentration) of the hydrolysates in comparison with the control (α 0.05). After this treatment, HIUS-treated fractions were shown as smaller in size and fractions between 1 and 3 kDa displayed the highest ACE inhibition activity. HIUS promoted significant changes in whey protein structure, inducing, unfolding, and aggregation, decreasing the content of α-helix, and increasing β-sheets structures. These findings prove that ultrasound treatment before enzymatic hydrolysis is an innovative and useful strategy that modifies the peptide profile of whey protein hydrolysates and enhances the production of ACE inhibitory peptides.
高强度超声(HIUS)可诱导蛋白质结构的改变。酶水解与超声相结合是一种提高血管紧张素转换酶(ACE)抑制肽释放量的有趣策略。在本研究中,乳清蛋白在两个振幅水平(30%和50%)下用HIUS预处理10分钟,然后用植物蛋白酶菠萝蛋白酶进行水解。将得到的水解产物进行超滤,并将其组分进行模拟胃肠道消化。使用衰减全反射傅里叶变换红外光谱(FTIR-ATR)和固有光谱分析HIUS对乳清蛋白诱导的构象变化。结果发现,与对照相比,两个超声预处理水平均显著降低了水解产物的IC值(50%抑制浓度)(α<0.05)。经过这种处理后,HIUS处理的组分显示尺寸更小,1至3 kDa之间的组分表现出最高的ACE抑制活性。HIUS促进了乳清蛋白结构的显著变化,诱导了展开和聚集,降低了α-螺旋含量,并增加了β-折叠结构。这些发现证明,酶水解前的超声处理是一种创新且有用的策略,可改变乳清蛋白水解产物的肽谱并提高ACE抑制肽的产量。