{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,8,31]],"date-time":"2026-08-31T20:55:49Z","timestamp":1788209749456,"version":"build-2803163510"},"reference-count":59,"publisher":"MDPI AG","issue":"13","license":[{"start":{"date-parts":[[2021,6,23]],"date-time":"2021-06-23T00:00:00Z","timestamp":1624406400000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100009509","name":"Kementerian Riset Teknologi Dan Pendidikan Tinggi Republik Indonesia","doi-asserted-by":"publisher","award":["WCR Program 2325 \/IT3.L1\/PN\/2021."],"award-info":[{"award-number":["WCR Program 2325 \/IT3.L1\/PN\/2021."]}],"id":[{"id":"10.13039\/501100009509","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Molecules"],"abstract":"<jats:p>The Angiotensin-I-converting enzyme (ACE) is a peptidase with a significant role in the regulation of blood pressure. Within this work, a systematic review on the enzymatic preparation of Angiotensin-I-Converting Enzyme inhibitory (ACEi) peptides is presented. The systematic review is conducted by following PRISMA guidelines. Soybeans and velvet beans are known to have high protein contents that make them suitable as sources of parent proteins for the production of ACEi peptides. Endopeptidase is commonly used in the preparation of soybean-based ACEi peptides, whereas for velvet bean, a combination of both endo- and exopeptidase is frequently used. Soybean glycinin is the preferred substrate for the preparation of ACEi peptides. It contains proline as one of its major amino acids, which exhibits a potent significance in inhibiting ACE. The best enzymatic treatments for producing ACEi peptides from soybean are as follows: proteolytic activity by Protease P (Amano-P from Aspergillus sp.), a temperature of 37 \u00b0C, a reaction time of 18 h, pH 8.2, and an E\/S ratio of 2%. On the other hand, the best enzymatic conditions for producing peptide hydrolysates with high ACEi activity are through sequential hydrolytic activity by the combination of pepsin-pancreatic, an E\/S ratio for each enzyme is 10%, the temperature and reaction time for each proteolysis are 37 \u00b0C and 0.74 h, respectively, pH for pepsin is 2.0, whereas for pancreatin it is 7.0. As an underutilized pulse, the studies on the enzymatic hydrolysis of velvet bean proteins in producing ACEi peptides are limited. Conclusively, the activity of soybean-based ACEi peptides is found to depend on their molecular sizes, the amino acid residues, and positions. Hydrophobic amino acids with nonpolar side chains, positively charged, branched, and cyclic or aromatic residues are generally preferred for ACEi peptides.<\/jats:p>","DOI":"10.3390\/molecules26133822","type":"journal-article","created":{"date-parts":[[2021,6,23]],"date-time":"2021-06-23T11:28:41Z","timestamp":1624447721000},"page":"3822","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":26,"title":["Enzymatic Preparation of Bioactive Peptides Exhibiting ACE Inhibitory Activity from Soybean and Velvet Bean: A Systematic Review"],"prefix":"10.3390","volume":"26","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-1378-5367","authenticated-orcid":false,"given":"Azis Boing","family":"Sitanggang","sequence":"first","affiliation":[{"name":"Department of Food Science and Technology, Kampus IPB Darmaga, IPB University, Bogor 16680, Indonesia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jessica Eka","family":"Putri","sequence":"additional","affiliation":[{"name":"Department of Food Science and Technology, Kampus IPB Darmaga, IPB University, Bogor 16680, Indonesia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Nurheni Sri","family":"Palupi","sequence":"additional","affiliation":[{"name":"Department of Food Science and Technology, Kampus IPB Darmaga, IPB University, Bogor 16680, Indonesia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Emmanuel","family":"Hatzakis","sequence":"additional","affiliation":[{"name":"Department of Food Science and Technology, The Ohio State University, 2015 Fyffe Rd, Columbus, OH 43210, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Elvira","family":"Syamsir","sequence":"additional","affiliation":[{"name":"Department of Food Science and Technology, Kampus IPB Darmaga, IPB University, Bogor 16680, Indonesia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Slamet","family":"Budijanto","sequence":"additional","affiliation":[{"name":"Department of Food Science and Technology, Kampus IPB Darmaga, IPB University, Bogor 16680, Indonesia"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2021,6,23]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"441","DOI":"10.1161\/CIRCULATIONAHA.115.018912","article-title":"Global disparities of hypertension prevalence and control","volume":"134","author":"Mills","year":"2016","journal-title":"Circulation"},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"2224","DOI":"10.1016\/S0140-6736(12)61766-8","article-title":"A comparative risk assessment of burden of disease and injury attributable to 67 risk factors and risk factor clusters in 21 regions, 1990\u20132010: A systematic analysis for the global burden of disease study 2010","volume":"380","author":"Lim","year":"2012","journal-title":"Lancet"},{"key":"ref_3","first-page":"e596","article-title":"2019 ACC\/AHA Guideline on the primary prevention of cardiovascular disease: A Report of the American College of Cardiology\/American Heart Association Task Force on Clinical Practice Guidelines","volume":"140","author":"Arnett","year":"2019","journal-title":"Circulation"},{"key":"ref_4","doi-asserted-by":"crossref","first-page":"836","DOI":"10.1016\/S0140-6736(79)92186-X","article-title":"Captopril in the treatment of clinical hypertension and cardiac failure","volume":"314","author":"Atkinson","year":"1979","journal-title":"Lancet"},{"key":"ref_5","doi-asserted-by":"crossref","first-page":"29","DOI":"10.1093\/fqs\/fyx006","article-title":"Bioactive peptides: A review","volume":"1","year":"2017","journal-title":"Food Qual. Saf."},{"key":"ref_6","doi-asserted-by":"crossref","first-page":"102639","DOI":"10.1016\/j.ifset.2021.102639","article-title":"Continuous production of tempe-based bioactive peptides using an automated enzymatic membrane reactor","volume":"68","author":"Sitanggang","year":"2021","journal-title":"Innov. Food Sci. Emerg. Technol."},{"key":"ref_7","doi-asserted-by":"crossref","first-page":"123","DOI":"10.1016\/j.jff.2019.04.050","article-title":"Regulatory requirements of bioactive peptides (protein hydrolysates) from food proteins","volume":"58","author":"Chalamaiah","year":"2019","journal-title":"J. Funct. Foods"},{"key":"ref_8","doi-asserted-by":"crossref","unstructured":"Chatterjee, C., Gleddie, S., and Xiao, C.-W. (2018). Soybean bioactive peptides and their functional properties. Nutrients, 10.","DOI":"10.3390\/nu10091211"},{"key":"ref_9","doi-asserted-by":"crossref","unstructured":"Syah, D., Sitanggang, A.B., Faradilla, R.F., Trisna, V., Karsono, Y., and Septianita, D.A. (2015). The influences of coagulation conditions and storage proteins on the textural properties of soy-curd (tofu). CYTA J. Food, 13.","DOI":"10.1080\/19476337.2014.948071"},{"key":"ref_10","doi-asserted-by":"crossref","first-page":"116","DOI":"10.3923\/pjn.2012.116.122","article-title":"Chemical composition and nutritional evaluation of velvet bean seeds (Mucuna utilis) for domestic consumption and industrial utilization in Nigeria","volume":"11","author":"Balogun","year":"2012","journal-title":"Pak. J. Nutr."},{"key":"ref_11","doi-asserted-by":"crossref","first-page":"4568","DOI":"10.1021\/jf060264q","article-title":"Angiotensin I-converting enzyme inhibitory peptide derived from glycinin, the 11S globulin of soybean (Glycine max)","volume":"54","author":"Gowda","year":"2006","journal-title":"J. Agric. Food Chem."},{"key":"ref_12","first-page":"89","article-title":"A method for isolation of 2S, 7S and 11S proteins of soybean","volume":"7","author":"Rao","year":"1977","journal-title":"Prep. Biochem."},{"key":"ref_13","doi-asserted-by":"crossref","first-page":"2968","DOI":"10.3390\/molecules17032968","article-title":"Isolation of glycinin (11S) from lipid-reduced soybean flour: Effect of processing conditions on yields and purity","volume":"17","author":"Deng","year":"2012","journal-title":"Molecules"},{"key":"ref_14","doi-asserted-by":"crossref","first-page":"C247","DOI":"10.1111\/j.1750-3841.2006.00028.x","article-title":"Effects of NaCl concentration on salting-in and dilution during salting-out on soy protein fractionation","volume":"71","author":"Deak","year":"2006","journal-title":"J. Food Sci."},{"key":"ref_15","doi-asserted-by":"crossref","first-page":"285","DOI":"10.1007\/s11746-999-0233-x","article-title":"Pilot-plant fractionation of soybean glycinin and \u03b2-conglycinin","volume":"76","author":"Wu","year":"1999","journal-title":"J. Am. Oil Chem. Soc."},{"key":"ref_16","first-page":"767","article-title":"ACE-I inhibitory peptide fractions from enzymatic hydrolysates of velvet bean (Mucuna pruriens)","volume":"4","author":"CP","year":"2013","journal-title":"Agric. Sci."},{"key":"ref_17","first-page":"1691","article-title":"ACE inhibitory, hypotensive and antioxidant peptide fractions from Mucuna pruriens proteins","volume":"39","author":"Ruiz","year":"2014","journal-title":"Proc. Biochem."},{"key":"ref_18","doi-asserted-by":"crossref","first-page":"390","DOI":"10.1016\/j.bcab.2017.05.001","article-title":"Purification of Mucuna pruriens (L) peptide fractions and evaluation of their ACE inhibitory effect","volume":"10","author":"Tuz","year":"2017","journal-title":"Biocatal. Agric. Biotechnol."},{"key":"ref_19","doi-asserted-by":"crossref","first-page":"4768","DOI":"10.1021\/jf970035r","article-title":"Effect of sodium sulfite, sodium bisulfite, cysteine, and pH on protein solubility and sodium dodecyl sulfate\u2212polyacrylamide gel electrophoresis of soybean milk base","volume":"45","author":"Abtahi","year":"1997","journal-title":"J. Agric. Food Chem."},{"key":"ref_20","first-page":"357","article-title":"Nutritional quality and physicochemical properties of Mucuna bean (Mucuna pruriens L.) protein isolates","volume":"17","author":"Mugendi","year":"2010","journal-title":"Int. Food Res. J."},{"key":"ref_21","doi-asserted-by":"crossref","first-page":"923","DOI":"10.3390\/biom3040923","article-title":"Research applications of proteolytic enzymes in molecular biology","volume":"3","year":"2013","journal-title":"Biomolecules"},{"key":"ref_22","doi-asserted-by":"crossref","first-page":"543","DOI":"10.1111\/j.1745-4514.2002.tb00772.x","article-title":"Identification of angiotensin I-converting enzyme inhibitory peptides derived from the peptic digest of soybean protein","volume":"26","author":"Chen","year":"2002","journal-title":"J. Food Biochem."},{"key":"ref_23","doi-asserted-by":"crossref","first-page":"61","DOI":"10.1111\/j.1745-4514.2004.tb00055.x","article-title":"Soybean protein-derived hydrolysate affects blood pressure in spontaneously hypertensive rats","volume":"28","author":"Chen","year":"2004","journal-title":"J. Food Biochem."},{"key":"ref_24","doi-asserted-by":"crossref","first-page":"127193","DOI":"10.1016\/j.foodchem.2020.127193","article-title":"Membrane-based preparative methods and bioactivities mapping of tempe-based peptides","volume":"329","author":"Sitanggang","year":"2020","journal-title":"Food Chem."},{"key":"ref_25","doi-asserted-by":"crossref","first-page":"501","DOI":"10.1021\/jf000695n","article-title":"Hypotensive and physiological effect of angiotensin converting enzyme inhibitory peptides derived from soy protein on spontaneously hypertensive rats","volume":"49","author":"Wu","year":"2001","journal-title":"J. Agric. Food Chem."},{"key":"ref_26","doi-asserted-by":"crossref","first-page":"1023","DOI":"10.1007\/s11746-015-2655-y","article-title":"Amino acid profiles of 44 soybean lines and ACE-I inhibitory activities of peptide fractions from selected lines","volume":"92","author":"Rayaprolu","year":"2015","journal-title":"J. Am. Oil Chem. Soc."},{"key":"ref_27","doi-asserted-by":"crossref","first-page":"358","DOI":"10.1016\/j.lwt.2018.08.045","article-title":"Optimization of ACE inhibitory peptides from black soybean by microwave-assisted enzymatic method and study on its stability","volume":"98","author":"Li","year":"2018","journal-title":"LWT"},{"key":"ref_28","doi-asserted-by":"crossref","first-page":"2191","DOI":"10.1016\/j.procbio.2004.08.010","article-title":"Production of angiotensin I-converting enzyme inhibitory peptides from soybean protein with Monascus purpureus acid proteinase","volume":"40","author":"Kuba","year":"2005","journal-title":"Process Biochem."},{"key":"ref_29","doi-asserted-by":"crossref","first-page":"C164","DOI":"10.1111\/j.1365-2621.2006.tb15612.x","article-title":"Identification of an angiotensin I-converting enzyme inhibitory peptides from protein hydrolysates by a soybean protease and the antihypertensive effects of hydrolysates in 4 spontaneously hypertensive model rats","volume":"71","author":"Kodera","year":"2006","journal-title":"J. Food Sci."},{"key":"ref_30","doi-asserted-by":"crossref","unstructured":"Mart\u00ednez-Medina, G.A., Barrag\u00e1n, A.P., Ruiz, H.A., Ilyina, A., Mart\u00ednez Hern\u00e1ndez, J.L., Rodr\u00edguez-Jasso, R.M., Hoyos-Concha, J.L., and Aguilar-Gonz\u00e1lez, C.N. (2019). Fungal proteases and production of bioactive peptides for the food industry. Enzymes in Food Biotechnology, Elsevier.","DOI":"10.1016\/B978-0-12-813280-7.00014-1"},{"key":"ref_31","doi-asserted-by":"crossref","first-page":"3369","DOI":"10.1021\/jf048174d","article-title":"Angiotensin I converting enzyme inhibitory peptides from in vitro pepsin\u2013pancreatin digestion of soy protein","volume":"53","author":"Lo","year":"2005","journal-title":"J. Agric. Food Chem."},{"key":"ref_32","doi-asserted-by":"crossref","first-page":"e12418","DOI":"10.1111\/jfbc.12418","article-title":"Bioactive peptides derived from bovine and porcine co-products: A review","volume":"41","author":"Lafarga","year":"2017","journal-title":"J. Food Biochem."},{"key":"ref_33","doi-asserted-by":"crossref","first-page":"227","DOI":"10.1016\/0309-1740(84)90039-1","article-title":"Effects of reaction variables on the hydrolysis of lean beef tissue by alcalase","volume":"11","author":"Munro","year":"1984","journal-title":"Meat Sci."},{"key":"ref_34","doi-asserted-by":"crossref","first-page":"29","DOI":"10.1016\/0014-5793(74)80327-3","article-title":"Kinetics of pepsin-catalysed transpeptidation: Evidence for the \u201camino-enzyme\u201d intermediate","volume":"46","author":"Antonov","year":"1974","journal-title":"FEBS Lett."},{"key":"ref_35","doi-asserted-by":"crossref","unstructured":"Wang, R., Edrington, T.C., Storrs, S.B., Crowley, K.S., Ward, J.M., Lee, T.C., Liu, Z.L., Li, B., and Glenn, K.C. (2017). Analyzing pepsin degradation assay conditions used for allergenicity assessments to ensure that pepsin susceptible and pepsin resistant dietary proteins are distinguishable. PLoS ONE, 12.","DOI":"10.1371\/journal.pone.0171926"},{"key":"ref_36","doi-asserted-by":"crossref","unstructured":"Awuor, O.L., Edward Kirwa, M., Betty, M., and Jackim, M.F. (2017). Optimization of alcalase hydrolysis conditions for production of dagaa (Rastrineobola argentea) protein hydrolysate with antioxidative properties. Ind. Chem., 3.","DOI":"10.4172\/2469-9764.1000122"},{"key":"ref_37","doi-asserted-by":"crossref","first-page":"2143","DOI":"10.1016\/j.ijbiomac.2020.10.060","article-title":"Use of Alcalase in the production of bioactive peptides: A review","volume":"165","author":"Siar","year":"2020","journal-title":"Int. J. Biol. Macromol."},{"key":"ref_38","doi-asserted-by":"crossref","first-page":"954","DOI":"10.3136\/nskkk1962.38.954","article-title":"Production, purification and properties of acid proteinase from genus Monascus","volume":"38","author":"Yasuda","year":"1991","journal-title":"Nippon. Shokuhin Kogyo Gakkaishi"},{"key":"ref_39","doi-asserted-by":"crossref","first-page":"1241","DOI":"10.1016\/j.foodchem.2010.10.042","article-title":"Hydrolysis of \u03b2-lactoglobulin by trypsin under acidic pH and analysis of the hydrolysates with MALDI\u2013TOF\u2013MS\/MS","volume":"125","author":"Cheison","year":"2011","journal-title":"Food Chem."},{"key":"ref_40","doi-asserted-by":"crossref","first-page":"872","DOI":"10.1021\/jf00106a048","article-title":"Chymotrypsin hydrolysis of soybean protein","volume":"29","author":"Kimball","year":"1981","journal-title":"J. Agric. Food Chem."},{"key":"ref_41","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1100\/2012\/564932","article-title":"Optimization of acid protease production by Aspergillus niger I1 on shrimp peptone using statistical experimental design","volume":"2012","author":"Siala","year":"2012","journal-title":"Sci. World J."},{"key":"ref_42","first-page":"363","article-title":"Properties of proteolytic enzyme from ginger (Zingiber officinale Roscoe)","volume":"20","author":"Foo","year":"2013","journal-title":"Int. Food Res. J."},{"key":"ref_43","unstructured":"Miwa, T. (1999). Characterization of novel cysteine proteases from germinating cotyledons of soybean [Glycine max (L.) Merrill]. J. Biochem."},{"key":"ref_44","first-page":"563","article-title":"Investigation of enzymatic optimization by flavourzyme and celluclast for soy protein hydrolysate powder","volume":"3","author":"Hoa","year":"2014","journal-title":"Int. J. Adv. Pharm. Biol. Chem."},{"key":"ref_45","doi-asserted-by":"crossref","first-page":"301","DOI":"10.1016\/j.foodhyd.2014.01.013","article-title":"Soy proteins: A review on composition, aggregation and emulsification","volume":"39","author":"Nishinari","year":"2014","journal-title":"Food Hydrocoll."},{"key":"ref_46","doi-asserted-by":"crossref","first-page":"551","DOI":"10.1007\/s13197-011-0517-7","article-title":"Physical characteristics and nutritional composition of some new soybean (Glycine max (L.) Merrill) genotypes","volume":"51","author":"Sharma","year":"2014","journal-title":"J. Food Sci. Technol."},{"key":"ref_47","doi-asserted-by":"crossref","first-page":"1680","DOI":"10.1007\/BF02541665","article-title":"The structure and complexity of the 11S polypeptides in soybeans","volume":"62","author":"Nielsen","year":"1985","journal-title":"J. Am. Oil Chem. Soc."},{"key":"ref_48","doi-asserted-by":"crossref","first-page":"310","DOI":"10.1263\/jbb.106.310","article-title":"Angiotensin-I converting enzyme (ACE) inhibitory mechanism of tripeptides containing aromatic residues","volume":"106","author":"Kobayashi","year":"2008","journal-title":"J. Biosci. Bioeng."},{"key":"ref_49","doi-asserted-by":"crossref","first-page":"44","DOI":"10.1016\/j.cofs.2015.05.002","article-title":"Structure and function of plant protein-derived antihypertensive peptides","volume":"4","author":"Aluko","year":"2015","journal-title":"Curr. Opin. Food Sci."},{"key":"ref_50","doi-asserted-by":"crossref","first-page":"e12572","DOI":"10.1111\/jfbc.12572","article-title":"Molecular interactions, bioavailability, and cellular mechanisms of angiotensin-converting enzyme inhibitory peptides","volume":"43","author":"Fan","year":"2019","journal-title":"J. Food Biochem."},{"key":"ref_51","doi-asserted-by":"crossref","first-page":"891","DOI":"10.1038\/nrd1227","article-title":"ACE revisited: A new target for structure-based drug design","volume":"2","author":"Acharya","year":"2003","journal-title":"Nat. Rev. Drug Discov."},{"key":"ref_52","doi-asserted-by":"crossref","first-page":"561","DOI":"10.1016\/j.foodchem.2010.09.048","article-title":"Angiotensin I-converting enzyme (ACE) inhibitory peptides derived from arachin by simulated gastric digestion","volume":"125","author":"Jimsheena","year":"2011","journal-title":"Food Chem."},{"key":"ref_53","doi-asserted-by":"crossref","first-page":"6244","DOI":"10.1039\/C9FO01546A","article-title":"A comprehensive review of bioactive peptides obtained from animal byproducts and their applications","volume":"10","author":"Bechaux","year":"2019","journal-title":"Food Funct."},{"key":"ref_54","doi-asserted-by":"crossref","first-page":"130","DOI":"10.1016\/j.biomed.2012.06.005","article-title":"Angiotensin I-converting enzyme inhibitory peptides: Inhibition mode, bioavailability, and antihypertensive effects","volume":"2","author":"Jao","year":"2012","journal-title":"BioMedicine"},{"key":"ref_55","doi-asserted-by":"crossref","first-page":"4983","DOI":"10.1021\/jf0105081","article-title":"Characterization of \u03b2-conglycinin and glycinin soy protein fractions from four selected soybean genotypes","volume":"49","author":"Riblett","year":"2001","journal-title":"J. Agric. Food Chem."},{"key":"ref_56","first-page":"64","article-title":"How to Write a Systematic Review: A Step-by-Step Guide","volume":"23","author":"Carey","year":"2013","journal-title":"Univ. Pa. Orthop. J."},{"key":"ref_57","doi-asserted-by":"crossref","first-page":"229","DOI":"10.1186\/s13643-017-0623-3","article-title":"Mapping evidence on the distribution of human papillomavirus-related cancers in sub-Saharan Africa: Scoping review protocol","volume":"6","author":"Lekoane","year":"2017","journal-title":"Syst. Rev."},{"key":"ref_58","doi-asserted-by":"crossref","unstructured":"Moher, D., Liberati, A., Tetzlaff, J., and Altman, D.G. (2009). Preferred Reporting Items for Systematic Reviews and Meta-Analyses: The PRISMA Statement. PLoS Med., 6.","DOI":"10.1371\/journal.pmed.1000097"},{"key":"ref_59","doi-asserted-by":"crossref","first-page":"365","DOI":"10.2174\/0929867323666161101140214","article-title":"Daidzein and its effects on brain","volume":"24","author":"Ahmed","year":"2017","journal-title":"Curr. Med. Chem."}],"container-title":["Molecules"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/1420-3049\/26\/13\/3822\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,10,11]],"date-time":"2025-10-11T06:21:49Z","timestamp":1760163709000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/1420-3049\/26\/13\/3822"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2021,6,23]]},"references-count":59,"journal-issue":{"issue":"13","published-online":{"date-parts":[[2021,7]]}},"alternative-id":["molecules26133822"],"URL":"https:\/\/doi.org\/10.3390\/molecules26133822","relation":{},"ISSN":["1420-3049"],"issn-type":[{"value":"1420-3049","type":"electronic"}],"subject":[],"published":{"date-parts":[[2021,6,23]]}}}