Kluyveromyces marxianus protein hydrolysates were prepared by two different sonicated-enzymatic (trypsin and chymotrypsin) hydrolysis treatments to obtain antioxidant and ACE-inhibitory peptides. Trypsin and chymotrypsin hydrolysates obtained by 5 h, exhibited the highest antioxidant and ACE-inhibitory activities. After fractionation using ultrafiltration and reverse phase high performance liquid chromatography (RP-HPLC) techniques, two new peptides were identified. One fragment (LL-9, MW = 1180 Da) with the amino acid sequence of Leu-Pro-Glu-Ser-Val-His-Leu-Asp-Lys showed significant ACE inhibitory activity (IC50 = 22.88 μM) while another peptide fragment (VL-9, MW = 1118 Da) with the amino acid sequence of Val-Leu-Ser-Thr-Ser-Phe-Pro-Pro-Lys showed the highest antioxidant and ACE inhibitory properties (IC50 = 15.20 μM, 5568 μM TE/mg protein). The molecular docking studies revealed that the ACE inhibitory activities of VL-9 is due to interaction with the S2 (His513, His353, Glu281) and S'1 (Glu162) pockets of ACE and LL-9 can fit perfectly into the S1 (Thr345) and S2 (Tyr520, Lys511, Gln281) pockets of ACE.

中文翻译：

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从马克斯克鲁维酵母蛋白水解物中生产抗氧化和 ACE 抑制肽：纯化和分子对接

马克斯克鲁维酵母蛋白水解物是通过两种不同的超声酶促（胰蛋白酶和糜蛋白酶）水解处理制备的，以获得抗氧化和 ACE 抑制肽。5 h 获得的胰蛋白酶和糜蛋白酶水解物表现出最高的抗氧化和 ACE 抑制活性。使用超滤和反相高效液相色谱 (RP-HPLC) 技术进行分级分离后，鉴定出两种新肽。一个具有 Leu-Pro-Glu-Ser-Val-His-Leu-Asp-Lys 氨基酸序列的片段 (LL-9, MW = 1180 Da) 显示出显着的 ACE 抑制活性 (IC50 = 22.88 μM) 而另一个肽片段(VL-9, MW = 1118 Da) 氨基酸序列为 Val-Leu-Ser-Thr-Ser-Phe-Pro-Pro-Lys 显示出最高的抗氧化和 ACE 抑制性能 (IC50 = 15.20 μM, 5568 μM TE /mg蛋白质）。