Kamal Hina, Jafar Sabika, Mudgil Priti, Hamdi Marwa, Ayoub Mohammed Akli, Maqsood Sajid
Department of Food Science, College of Agriculture and Veterinary Medicine, United Arab Emirates University, Al-Ain, 15551, United Arab Emirates.
Department of Biology, College of Science, United Arab Emirates University, Al-Ain, 15551, United Arab Emirates.
Nutr Health. 2024 Jun;30(2):371-379. doi: 10.1177/02601060221122213. Epub 2022 Sep 6.
Whey proteins and their peptide derivatives have attracted a great attention of researchers in the pharmaceutical and nutritional fields, due to their numerous bio-functionalities. In the present research study, enzymatic protein hydrolysates (CWPHs) from camel whey proteins (CWPs) were produced and investigated for their antioxidant and antimicrobial potentials. Herein, Pepsin (gastric), and Trypsin and Chymotrypsin (pancreatic) enzymes were used to produce CWPHs. The obtained hydrolysates were characterize to ascertain the level of protein degradation and studies on their antimicrobial and antioxidant potential were conducted. Among all CWPHs, a complete degradation of all different protein bands was perceived with Chymotrypsin-derived CWPHs, whereas, light bands of serum albumin and α-lactalbumin were observed with Trypsin and Pepsin-derived CWPHs. After enzymatic degradation, both CWPHs antioxidant and antimicrobial activities were improved. Chymotrypsin-derived CWPHs demonstrated higher DPPH and ABTS radical scavenging activities, anent the increase in proteolysis time. Compared to unhydrolyzed CWPs, higher metal chelating activities were displayed by Trypsin-derived CWPHs. No significant increase in the FRAP activities was noticed after CWPs hydrolysis using Trypsin and Chymotrypsin, while Pepsin-derived CWPHs showed higher reducing power. In terms of antimicrobial activity, significantly higher bacterial growth inhibition rates were exhibited by CWPHs compared to the unhydrolyzed CWP. Overall, CWPHs displayed enhanced antioxidative and antimicrobial properties.
乳清蛋白及其肽衍生物因其众多的生物功能而引起了制药和营养领域研究人员的极大关注。在本研究中，制备了骆驼乳清蛋白（CWP）的酶促蛋白水解物（CWPH），并研究了其抗氧化和抗菌潜力。在此，使用胃蛋白酶（胃液）、胰蛋白酶和胰凝乳蛋白酶（胰液）来制备CWPH。对获得的水解产物进行表征以确定蛋白质降解水平，并对其抗菌和抗氧化潜力进行研究。在所有CWPH中，胰凝乳蛋白酶衍生的CWPH可观察到所有不同蛋白条带的完全降解，而胰蛋白酶和胃蛋白酶衍生的CWPH则观察到血清白蛋白和α-乳白蛋白的浅条带。酶促降解后，CWPH的抗氧化和抗菌活性均有所提高。随着蛋白水解时间的增加，胰凝乳蛋白酶衍生的CWPH表现出更高的DPPH和ABTS自由基清除活性。与未水解的CWP相比，胰蛋白酶衍生的CWPH表现出更高的金属螯合活性。使用胰蛋白酶和胰凝乳蛋白酶水解CWP后，未观察到FRAP活性有显著增加，而胃蛋白酶衍生的CWPH表现出更高的还原能力。在抗菌活性方面，与未水解的CWP相比，CWPH表现出显著更高的细菌生长抑制率。总体而言，CWPH表现出增强的抗氧化和抗菌性能。
