References
- Admassu, H., Gasmalla, M. A. A., Yang, R., & Zhao, W. (2018). Bioactive peptides derived from seaweed protein and their health benefits: Anti-hypertensive, antioxidant, and antidiabetic properties. Journal of Food Science, 83(1), 6–16. https://doi.org/https://doi.org/10.1111/1750-3841.14011
- Alashi, A. M., Blanchard, C. L., Mailer, R. J., Agboola, S. O., Mawson, A. J., He, R., Malomo, S. A., Girgih, A. T., & Aluko, R. E. (2014). Blood pressure lowering effects of Australian canola protein hydrolysates in spontaneously hypertensive rats. Food Research International, 55, 281–287. https://doi.org/https://doi.org/10.1016/j.foodres.2013.11.015
- Amorim, M., Pinheiro, H., & Pintado, M. (2019). Valorization of spent brewer’s yeast: Optimization of hydrolysis process towards the generation of stable ACE-inhibitory peptides. Lwt-Food Science and Technology, 111, 77–84. https://doi.org/https://doi.org/10.1016/j.lwt.2019.05.011
- Cao, S., Wang, Y., Hao, Y., Zhang, W., & Zhou, G. (2020). Anti-hypertensive effects in vitro and in vivo of novel angiotensin-converting enzyme inhibitory peptides from bovine bone gelatin hydrolysate. Journal of Agricultural and Food Chemistry, 68(3), 759–768. https://doi.org/https://doi.org/10.1021/acs.jafc.9b05618
- Carboni, S., Clegg, S. H., & Hughes, A. D. (2016). The use of biorefinery by-products and natural detritus as feed sources for oysters (Crassostrea gigas) juveniles. Aquaculture, 464, 392–398. https://doi.org/https://doi.org/10.1016/j.aquaculture.2016.07.021
- Chaudhary, S., Vats, I. D., Chopra, M., Biswas, P., & Pasha, S. (2009). Effect of varying chain length between P-1 and P-1 ‘ position of tripeptidomimics on activity of angiotensin-converting enzyme inhibitors. Bioorganic & Medicinal Chemistry Letters, 19(15), 4364–4366. https://doi.org/https://doi.org/10.1016/j.bmcl.2009.05.079
- Chen, J.-C., Wang, J., Zheng, B.-D., Pang, J., Chen, L.-J., Lin, H.-T., & Guo, X. (2016). Simultaneous determination of 8 small antihypertensive peptides with tyrosine at the C-terminal in L aminaria japonica hydrolysates by RP-HPLC method. Journal of Food Processing and Preservation, 40(3), 492–501. https://doi.org/https://doi.org/10.1111/jfpp.12628
- Cushman, D. W., & Cheung, H. S. (1971). Spectrophotometric assay and properties of the angiotensin-converting enzyme of rabbit lung. Biochemical Pharmacology. 20(7), 1637. https://doi.org/https://doi.org/10.1016/0006-2952(71)90292-9
- Cushman, D. W., Pluscec, J., Williams, N. J., Weaver, E. R., Sabo, E. F., Kocy, O., Cheung, H. S., & Ondetti, M. A. (1973). Inhibition of angiotensin-converting enzyme by analogs of peptides from bothrops-jararaca venom. Experientia, 29(8), 1032–1035. https://doi.org/https://doi.org/10.1007/bf01930447
- Daliri, E. B.-M., Ofosu, F. K., Chelliah, R., Park, M. H., Kim, J. H., & Oh, D. H. (2019). Development of a Soy Protein Hydrolysate with an Anti-hypertensive Effect. International Journal of Molecular Sciences, 20 (6), 1496. https://doi.org/https://doi.org/10.3390/ijms20061496
- Derrien, M., Badr, A., Gosselin, A., Desjardins, Y., & Angers, P. (2017). Optimization of a green process for the extraction of lutein and chlorophyll from spinach by-products using response surface methodology (RSM). Lwt-Food Science and Technology, 79, 170–177. https://doi.org/https://doi.org/10.1016/j.lwt.2017.01.010
- Elavarasan, K., Shamasundar, B. A., Badii, F., & Howell, N. (2016). Angiotensin I-converting enzyme (ACE) inhibitory activity and structural properties of oven- and freeze-dried protein hydrolysate from fresh water fish (Cirrhinus mrigala). Food Chemistry, 206, 210–216. https://doi.org/https://doi.org/10.1016/j.foodchem.2016.03.047
- Fishery Bureau, of Ministry of agriculture and Rural Affairs of China. (2019). The China Fishery Yearbook. China Agriculture Press.
- Fu, W., Chen, C., Zeng, H., Lin, J., Zhang, Y., Hu, J., & Zheng, B. (2019). Novel angiotensin-converting enzyme inhibitory peptides derived from Trichiurus lepturus myosin: Molecular docking and surface plasmon resonance study. Lwt-Food Science and Technology, 110, 54–63. https://doi.org/https://doi.org/10.1016/j.lwt.2019.04.053
- García-Mora, P., Martín-Martínez, M., Ma, B., González-Múniz, R., Peñas, E., Frias, J., & Martinez-Villaluenga, C. (2017). Identification, functional gastrointestinal stability and molecular docking studies of lentil peptides with dual antioxidant and angiotensin I converting enzyme inhibitory activities. Food Chemistry, 221, 464–472. https://doi.org/https://doi.org/10.1016/j.foodchem.2016.10.087
- Garcia-Vaquero, M., Mora, L., & Hayes, M. (2019). In vitro and in silico approaches to generating and identifying angiotensin-converting enzyme I inhibitory peptides from green Macroalga Ulva lactuca. Marine Drugs, 17(4), 204. https://doi.org/https://doi.org/10.3390/md17040204
- Gu, R.-Z., Li, C.-Y., Liu, W.-Y., Yi, W.-X., & Cai, M.-Y. (2011). Angiotensin I-converting enzyme inhibitory activity of low-molecular-weight peptides from Atlantic salmon (Salmo salar L.) skin. Food Research International, 44(5), 1536–1540. https://doi.org/https://doi.org/10.1016/j.foodres.2011.04.006
- Ko, S.-C., Kang, N., Kim, E.-A., Kang, M. C., Lee, S.-H., Kang, S.-M., Lee, J.-B., Jeon, B.-T., Kim, S.-K., Park, S.-J., Park, P.-J., Jung, W.-K., Kim, D., & Jeon, Y.-J. (2012). A novel angiotensin I-converting enzyme (ACE) inhibitory peptide from a marine Chlorella ellipsoidea and its antihypertensive effect in spontaneously hypertensive rats. Process Biochemistry, 47(12), 2005–2011. https://doi.org/https://doi.org/10.1016/j.procbio.2012.07.015
- Kocak, A., Sanli, T., Anli, E. A., & Hayaloglu, A. A. (2020). Role of using adjunct cultures in release of bioactive peptides in white-brined goat-milk cheese. Lwt-Food Science and Technology, 123, 109127. https://doi.org/https://doi.org/10.1016/j.lwt.2020.109127
- Krichen, F., Sila, A., Caron, J., Kobbi, S., Nedjar, N., Miled, N., Blecker, C., Besbes, S., & Bougatef, A. (2018). Identification and molecular docking of novel ACE inhibitory peptides from protein hydrolysates of shrimp waste. Engineering in Life Sciences, 18(9), 682–691. https://doi.org/https://doi.org/10.1002/elsc.201800045
- Kristinsson, H. G., & Rasco, B. A. (2000). Fish protein hydrolysates: Production, biochemical, and functional properties. Critical Reviews in Food Science and Nutrition, 40(1), 43–81. https://doi.org/https://doi.org/10.1080/10408690091189266
- Lee, J. K., Jeon, J.-K., & Byun, H.-G. (2014). Anti-hypertensive effect of novel angiotensin converting enzyme inhibitory peptide from chum salmon (Oncorhynchus keta) skin in spontaneously hypertensive rats. Journal of Functional Foods, 7, 381–389. https://doi.org/https://doi.org/10.1016/j.jff.2014.01.021
- Majumder, K., & Wu, J. (2015). Molecular targets of anti-hypertensive peptides: Understanding the mechanisms of action based on the pathophysiology of hypertension. International Journal of Molecular Sciences, 16(1), 256–283. https://doi.org/https://doi.org/10.3390/ijms16010256
- Matsui, T., & Matsumoto, K. (2006). Lead molecules from natural products: Discovery and new trends: Antihypertensive peptides from natural resource, Elsevier North Holland. (Vol. 2, pp. 255–271).
- Meisel, H., & FitzGerald, R. J. (2003). Biofunctional peptides from milk proteins: Mineral binding and cytomodulatory effects. Current Pharmaceutical Design, 9(16), 1289–1295. https://doi.org/https://doi.org/10.2174/1381612033454847
- Memarpoor-Yazdi, M., Zare-Zardini, H., Mogharrab, N., & Navapour, L. (2020). Purification, characterization and mechanistic evaluation of angiotensin converting enzyme inhibitory peptides derived from Zizyphus Jujuba fruit. Scientific Reports, 10(1), 3976. https://doi.org/https://doi.org/10.1038/s41598-020-60972-w
- Ngo, D.-H., Kang, K.-H., Ryu, B., Vo, T.-S., Jung, W.-K., Byun, H.-G., & Kim, S.-K. (2015). Angiotensin-I converting enzyme inhibitory peptides from anti-hypertensive skate (Okamejei kenojei) skin gelatin hydrolysate in spontaneously hypertensive rats. Food Chemistry, 174, 37–43. https://doi.org/https://doi.org/10.1016/j.foodchem.2014.11.013
- Patten, G. S., Abeywardena, M. Y., & Bennett, L. E. (2016). Inhibition of angiotensin converting enzyme, angiotensin II receptor blocking, and blood pressure lowering bioactivity across plant families. Critical Reviews in Food Science and Nutrition, 56(2), 181–214. https://doi.org/https://doi.org/10.1080/10408398.2011.651176
- Pujiastuti, D. Y., Amin, M. N. G., Alamsjah, M. A., & Hsu, J.-L. (2019). Marine organisms as potential sources of bioactive peptides that inhibit the activity of angiotensin I-converting enzyme: A review. Molecules, 24(14), 2541. https://doi.org/https://doi.org/10.3390/molecules24142541
- Raji, V., Loganathan, C., Sadhasivam, G., Kandasamy, S., Poomani, K., & Thayumanavan, P. (2020). Purification of fucoxanthin from sargassum wightii greville and understanding the inhibition of angiotensin 1-converting enzyme: An in vitro and in silico studies. International Journal of Biological Macromolecules, 148, 696–703. https://doi.org/https://doi.org/10.1016/j.ijbiomac.2020.01.140
- Rohit, A. C., Sathisha, K., & Aparna, H. S. (2012). A variant peptide of buffalo colostrum beta-lactoglobulin inhibits angiotensin I-converting enzyme activity. European Journal of Medicinal Chemistry, 53, 211–219. https://doi.org/https://doi.org/10.1016/j.ejmech.2012.03.057
- Sato, M., Hosokawa, T., Yamaguchi, T., Nakano, T., Muramoto, K., Kahara, T., Funayama, K., Kobayashi, A., & Nakano, T. (2002). Angiotensin I-converting enzyme inhibitory peptides derived from wakame (Undaria pinnatifida) and their antihypertensive effect in spontaneously hypertensive rats. Journal of Agricultural and Food Chemistry, 50(21), 6245–6252. https://doi.org/https://doi.org/10.1021/jf020482t
- Wijesekara, I., & Kim, S.-K. (2010). Angiotensin I-converting enzyme (ACE) inhibitors from marine resources: Prospects in the pharmaceutical industry. Marine Drugs, 8(4), 1080–1093. https://doi.org/https://doi.org/10.3390/md8041080
- Wu, Q., Du, J., Jia, J., & Kuang, C. (2016). Production of ACE inhibitory peptides from sweet sorghum grain protein using alcalase: Hydrolysis kinetic, purification and molecular docking study. Food Chemistry, 199, 140–149. https://doi.org/https://doi.org/10.1016/j.foodchem.2015.12.012
- Yang, Y., Li, A., Zhong, Z., & Xie, M. (2019). Angiotensin converting enzyme inhibitory peptide fractions from Tibet wild peach kernel protein hydrolysates. Acta Alimentaria, 48(4), 495–506. https://doi.org/https://doi.org/10.1556/066.2019.48.4.11
- Yuan, J., Zheng, Y., Wu, Y., Chen, H., Tong, P., & Gao, J. (2020). Double enzyme hydrolysis for producing antioxidant peptide from egg white: Optimization, evaluation, and potential allergenicity. Journal of Food Biochemistry, 44(2), e13113. https://doi.org/https://doi.org/10.1111/jfbc.13113