College of Biological Sciences and Technology, Beijing Key Laboratory of Food Processing and Safety in Forestry, Beijing Forestry University, Beijing 100083, China.
Food Science and Engineering College, Beijing University of Agriculture, Beijing 102206, China.
Food Chem. 2022 Dec 1;396:133621. doi: 10.1016/j.foodchem.2022.133621. Epub 2022 Jul 2.
Studies on the control of lipid digestion by food-derived active substances have prioritized the direct inhibition of lipase, ignoring the influence of these substances on the stability of bile salt (BS)-stabilized oil emulsions, which are essential for the hydrolysis of triglycerides by lipase. This study aimed to demonstrate the inhibitory potential of oat peptides (OPs) on lipolysis due to lipase inhibition, in particular, the physicochemical destruction of BS-stabilized emulsions. OPs were characterized by an enterostatin-like X-Pro-Y-Pro-Arg terminal sequence, competitively and/or noncompetitively inhibited lipase, and even caused lipase conformational changes. Interestingly, OPs destabilized BS-stabilized emulsions by weakening the rheological cross-linking structure of the emulsions through competitive hydrophobic binding to BS. Further analysis revealed that the H-bond binding of OP to BS significantly destroyed the hydrophilic and lipophilic balance of BS by increasing the surface hydrophobicity. These findings provided novel insights into the action mechanism of bioactive peptides on lipid digestion.
研究食物来源的活性物质对脂质消化的控制作用时，优先考虑了对脂肪酶的直接抑制作用，而忽略了这些物质对胆汁盐（BS）稳定的油乳液稳定性的影响，因为脂肪酶的水解作用需要 BS 稳定的乳液。本研究旨在证明燕麦肽（OPs）通过抑制脂肪酶（特别是通过对 BS 稳定的乳液的物理化学破坏）来抑制脂肪分解的潜力。OPs 具有肠抑素样 X-Pro-Y-Pro-Arg 末端序列，对脂肪酶具有竞争性和/或非竞争性抑制作用，甚至导致脂肪酶构象发生变化。有趣的是，OPs 通过与 BS 竞争结合疏水性，削弱乳液的流变交联结构，从而使 BS 稳定的乳液不稳定。进一步的分析表明，OP 与 BS 之间的氢键结合通过增加表面疏水性，显著破坏了 BS 的亲水性和疏水性平衡。这些发现为生物活性肽对脂质消化的作用机制提供了新的见解。
