In this study, we investigated the effects of solid lipid nanoparticle (SLN) nanocrystallization on the stability of two fractions of oat globulin-derived peptides. i.e., OGL, with molecular weight (MW) < 3 kDa, and OGH, with MW 3–10 kDa, in simulated gastrointestinal fluids (SGF). Both fractions were effectively encapsulated in SLNs with similar encapsulation efficiencies, zeta potentials and storage stability, but the particle sizes of each fraction, their polydispersity indices and thermogravimetric properties differed. The encapsulated peptide fractions had different rates of release and degradation in SGF, but both fractions could be protected from secondary hydrolysis, and both maintained high bioactivity rates when they encountered the SGF. Results from infrared spectroscopy and X-ray diffraction revealed that OGL had high binding affinity for the SLN–OH group and a high degree of crystallinity, which ensured its stability in SGF. These findings contribute to the delivery-system design for the encapsulated peptides with improved functional attributes.

在这项研究中，我们调查了固态脂质纳米颗粒（SLN）纳米结晶对燕麦球蛋白衍生肽的两个部分的稳定性的影响。例如，在模拟胃肠液（SGF）中，分子量（MW）<3 kDa的OGL和MW 3-10 kDa的OGH。两种级分均有效地包封在SLN中，具有相似的包封效率，ζ电位和储存稳定性，但每个级分的粒径，其多分散性指数和热重性质均不同。包封的肽级分在SGF中具有不同的释放和降解速率，但是两个级分都可以避免二次水解，并且在遇到SGF时都保持较高的生物活性。红外光谱和X射线衍射的结果表明，OGL对SLN-OH基团具有很高的结合亲和力，并且具有很高的结晶度，从而确保了其在SGF中的稳定性。这些发现有助于具有改善的功能属性的包封的肽的递送系统设计。