Department of Food and Human Nutritional Sciences, University of Manitoba, Winnipeg, Manitoba, Canada.
Richardson Centre for Functional Foods and Nutraceuticals, University of Manitoba, Winnipeg, Manitoba, Canada.
J Food Biochem. 2022 Nov;46(11):e14289. doi: 10.1111/jfbc.14289. Epub 2022 Jun 27.
This study optimized the enzymatic hydrolysis of yellow field pea proteins using alcalase (ACH), chymotrypsin (CHH), flavourzyme (FZH), pancreatin (PCH), pepsin (PEH), and trypsin (TPH) to obtain hydrolysates and ultrafiltered fractions (<1, 1-3, 3-5 and 5-10 kDa) that possess antioxidant plus acetylcholinesterase (AChE) and butyrylcholinesterase (BuChE) inhibitory activities. The hydrolysates exhibited varying degrees of radical scavenging and inhibition of linoleic acid peroxidation, as well as cholinesterase inhibition activities but the potency generally improved by >10% after UF separation into peptide fractions. ACH, FZH, and PEH exhibited significantly (p < .05) higher (20%-30% increases) radical scavenging activities than the other hydrolysates. The 1 and 3 kDa UF fractions of ACH, FZH, and PEH inhibited ~20%-30% AChE activity, while ACH, PCH, TPH, and PEH inhibited ~20%-40% BuChE activity. We conclude that the pea protein hydrolysates and their peptide fractions possess multifunctional properties with potential use against neurodegenerative disorders. PRACTICAL APPLICATIONS: Alzheimer's disease (AD) has multiple pathological pathways in addition to the loss of acetylcholine (ACh) catalyzed by acetylcholinesterase (AChE) and butyrylcholinesterase (BuChE). The presence of severe oxidative stress triggered by lipid peroxidation and formation of free radicals is a common trait in AD patients. The concept of AChE and BuChE inhibition as an approach toward AD amelioration involves the use of compounds with a similar structure to ACh, the natural substrate. Peptides derived from food proteins consist of ester bonds with structural similarity to ACh and theoretically possess the ability to interact with AChE and BuChE. Results from the present study imply that pea protein-derived peptides are potential candidates for use as inhibitors of AChE and BuChE activities, with application in the prevention and management of AD.
本研究使用碱性蛋白酶 (ACH)、胰凝乳蛋白酶 (CHH)、风味蛋白酶 (FZH)、胰酶 (PCH)、胃蛋白酶 (PEH) 和胰蛋白酶 (TPH) 对黄田豌豆蛋白进行酶解优化，得到水解产物和超滤分级 (<1、1-3、3-5 和 5-10 kDa)，这些产物具有抗氧化和乙酰胆碱酯酶 (AChE) 和丁酰胆碱酯酶 (BuChE) 抑制活性。水解产物表现出不同程度的自由基清除和抑制亚油酸过氧化以及胆碱酯酶抑制活性，但通过超滤分离成肽级分后，效力通常提高了 10%以上。ACH、FZH 和 PEH 表现出显著 (p <.05) 更高的 (增加 20%-30%) 自由基清除活性，比其他水解产物。ACH、FZH 和 PEH 的 1 和 3 kDa UF 级分抑制 AChE 活性约 20%-30%，而 ACH、PCH、TPH 和 PEH 抑制 BuChE 活性约 20%-40%。我们得出结论，豌豆蛋白水解产物及其肽级分具有多功能特性，具有对抗神经退行性疾病的潜力。 实际应用：阿尔茨海默病 (AD) 除了乙酰胆碱 (ACh) 被乙酰胆碱酯酶 (AChE) 和丁酰胆碱酯酶 (BuChE) 催化失活之外，还有多种病理途径。由脂质过氧化和自由基形成引发的严重氧化应激的存在是 AD 患者的共同特征。作为改善 AD 的一种方法，AChE 和 BuChE 抑制的概念涉及使用与 ACh 结构相似的化合物，即天然底物。来源于食物蛋白的肽由与 ACh 结构相似的酯键组成，理论上具有与 AChE 和 BuChE 相互作用的能力。本研究结果表明，豌豆蛋白衍生肽是作为 AChE 和 BuChE 活性抑制剂的潜在候选物，可应用于 AD 的预防和治疗。
