Key Laboratory of Agricultural Product Processing and Quality Control of Specialty(Co-construction by Ministry and Province), School of Food Science and Technology, Shihezi University, Shihezi, Xinjiang 832000, China; Key Laboratory for Food Nutrition and Safety Control of Xinjiang Production and Construction Corps, School of Food Science and Technology, Shihezi University, Shihezi, Xinjiang 832000, China; Engineering Research Center of Storage and Processing of Xinjiang Characteristic Fruits and Vegetables, Ministry of Education, School of Food Science and Technology, Shihezi University, Shihezi, Xinjiang 832000, China.
Key Laboratory of Agricultural Product Processing and Quality Control of Specialty(Co-construction by Ministry and Province), School of Food Science and Technology, Shihezi University, Shihezi, Xinjiang 832000, China; Key Laboratory for Food Nutrition and Safety Control of Xinjiang Production and Construction Corps, School of Food Science and Technology, Shihezi University, Shihezi, Xinjiang 832000, China; Engineering Research Center of Storage and Processing of Xinjiang Characteristic Fruits and Vegetables, Ministry of Education, School of Food Science and Technology, Shihezi University, Shihezi, Xinjiang 832000, China.
Int J Biol Macromol. 2024 Nov;281(Pt 3):136415. doi: 10.1016/j.ijbiomac.2024.136415. Epub 2024 Oct 10.
In this study, different ultrasound-assisted modes [ultrasonic simultaneous (US) and ultrasonic preconditioning (UP)] of synergistic enzymatic hydrolysis were used to prepare bioactive peptides of sheep hoof collagen. The 2, 2-diphenyl - 1-picrylhydrazyl (DPPH) radical scavenging activity, 2,2 '-Azino-bis (3-ethylbenzothiazoline-6-sulfonic acid) (ABTS) radical scavenging capacity and metal chelating capacity of sheep's hoof collagen antioxidant peptides (SCPs) (at 1 mg/mL) prepared at 20 min of treatment in US treatment mode (US-20) were 48.56 ± 0.68 %, 51.97 ± 1.15 % and 65.58 ± 1.36 %, respectively, which were higher compared with the control and UP groups. Using LC-MS/MS analysis, 9336, 11,527, and 11,909 peptide sequences were identified from collagen hydrolysate by C, UP-20, and US-20, respectively. The peptides ACEDAPPSAAHFR and FGFEVGPACFLG with high bioactivity were screened using computer analysis. Molecular docking results revealed that hydrogen bonding and hydrophobic interactions between the two peptide sequences with DPPH and ABTS radicals may be responsible for their antioxidant properties. Therefore, we have optimized the extraction of bioactive peptides from sheep hoof collagen using ultrasound-assisted enzymatic hydrolysis, which is helpful for the high-value utilisation of sheep hoof by-products and the extraction of foodborne antioxidant peptides.
在这项研究中，采用了不同的超声辅助模式（超声协同和超声预处理）协同酶解来制备羊蹄胶原蛋白的生物活性肽。在超声处理模式（US-20）下处理 20 分钟制备的羊蹄胶原蛋白抗氧化肽（SCPs）（1mg/mL）的 2,2-二苯基-1-苦基肼（DPPH）自由基清除活性、2,2'-联氮-双（3-乙基苯并噻唑啉-6-磺酸）（ABTS）自由基清除能力和金属螯合能力分别为 48.56±0.68%、51.97±1.15%和 65.58±1.36%，与对照组和 UP 组相比有所提高。通过 LC-MS/MS 分析，从胶原蛋白水解物中分别鉴定出 9336、11527 和 11909 条肽序列，来自 C、UP-20 和 US-20。使用计算机分析筛选出具有高生物活性的肽序列 ACEDAPPSAAHFR 和 FGFEVGPACFLG。分子对接结果表明，这两个与 DPPH 和 ABTS 自由基结合的肽序列之间的氢键和疏水相互作用可能是其抗氧化性质的原因。因此，我们已经优化了超声辅助酶解从羊蹄胶原蛋白中提取生物活性肽的方法，这有助于羊蹄副产品的高值利用和食源性抗氧化肽的提取。
