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Current Pharmaceutical Biotechnology

Editor-in-Chief

ISSN (Print): 1389-2010
ISSN (Online): 1873-4316

Review Article

Fibrinolytic Enzyme - An Overview

Author(s): Parveen Abdul Rahim and Devika Rengaswamy*

Volume 23, Issue 11, 2022

Published on: 31 March, 2022

Page: [1336 - 1345] Pages: 10

DOI: 10.2174/1389201023666220104143113

Price: $65

Abstract

Cardiovascular diseases, like coronary heart disease or artery disorders (arteriosclerosis, including artery solidification), heart failure (myocardial infarction), arrhythmias, congestive heart condition, stroke, elevated vital signs (hypertension), rheumatic heart disorder, and other circulatory system dysfunctions are the most common causes of death worldwide. Cardiovascular disorders are treated with stenting, coronary bypass surgery grafting, anticoagulants, antiplatelet agents, and other pharmacological and surgical procedures; however, these have limitations due to their adverse effects. Fibrinolytic agents degrade fibrin through enzymatic and biochemical processes. There are various enzymes that are currently used as a treatment for CVDs, like streptokinase, nattokinase, staphylokinase, urokinase, etc. These enzymes are derived from various sources, like bacteria, fungi, algae, marine organisms, plants, snakes, and other organisms. This review deals with the fibrinolytic enzymes, their mechanisms, sources, and their therapeutic potential.

Keywords: Enzyme, fibrinolytic agents, biocatalyst, cardiovascular disease, therapeutic potential, fibrinolysis.

Graphical Abstract

[1]
Choi, J.M.; Han, S.S.; Kim, H.S. Industrial applications of enzyme biocatalysis: Current status and future aspects. Biotechnol. Adv., 2015, 33(7), 1443-1454.
[http://dx.doi.org/10.1016/j.biotechadv.2015.02.014]
[2]
Kraut, J. How do enzymes work? Science, 1988, 242(4878), 533-540.Available from: . https://www.researchgate.net/publication/31985414 Accessed on: Mar. 22, 2021.
[http://dx.doi.org/10.1126/science.3051385]
[3]
Bommarius, A.S.; Paye, M.F. Stabilizing biocatalysts. Chem. Soc. Rev., 2013, 42(15), 6534-6565.
[http://dx.doi.org/10.1039/c3cs60137d] [PMID: 23807146]
[4]
James, J.; Simpson, B.K. Application of enzymes in food processing. Crit. Rev. Food Sci. Nutr., 1996, 36(5), 437-463.
[http://dx.doi.org/10.1080/10408399609527735] [PMID: 8725673]
[5]
Carpio, C.; González, P.; Ruales, J.; Batista-Viera, F. Bone-bound enzymes for food industry application. Food Chem., 2000, 68(4), 403-409.
[http://dx.doi.org/10.1016/S0308-8146(99)00193-4]
[6]
Chung, S.Y.; Seki, H.; Fujisawa, Y.; Shimoda, Y.; Hiraga, S.; Nomura, Y.; Saito, K.; Ishimoto, M.; Muranaka, T. A cellulose synthase-derived enzyme catalyses 3-O-glucuronosylation in saponin biosynthesis. Nat. Commun., 2020, 11(1), 5664.
[http://dx.doi.org/10.1038/s41467-020-19399-0] [PMID: 33199711]
[7]
Doshi, R.; Shelke, V. Enzymes in textile industry-An environment-friendly approach. Indian J. Fibre & Textile Res., 2001, 26, 202-205.
[8]
Araújo, R.; Casal, M.; Cavaco-Paulo, A. Application of enzymes for textile fibres processing. Biocatal. Biotransform., 2008, 26(5), 332-349.
[http://dx.doi.org/10.1080/10242420802390457]
[9]
Madhu, A.; Chakraborty, J.N. Developments in application of enzymes for textile processing. J. Cleaner Production, 2017, 145, 114-133.
[http://dx.doi.org/10.1016/j.jclepro.2017.01.013]
[10]
Bajpai, P. Application of enzymes in the pulp and paper industry. Biotechnol. Prog., 1999, 15(2), 147-157.
[http://dx.doi.org/10.1021/bp990013k] [PMID: 10194388]
[11]
Buchert, J.; Tenkanen, M.; Kantelinen, A.; Viikari, L. Application of xylanases in the pulp and paper industry. Bioresour. Technol., 1994, 50(1), 65-72.
[http://dx.doi.org/10.1016/0960-8524(94)90222-4]
[12]
Eriksson, K.E.L. Biotechnology in the pulp and paper industry. Wood Sci. Technol., 1990, 24(1), 79-101.
[http://dx.doi.org/10.1007/BF00225309]
[13]
Singh, G.; Kaur, S.; Khatri, M.; Arya, S.K. Biobleaching for pulp and paper industry in India: Emerging enzyme technology. Biocatalysis Agricultural Biotechnol., 2019, 17, 558-565.
[http://dx.doi.org/10.1016/j.bcab.2019.01.019]
[14]
Vojcic, L. Advances in protease engineering for laundry detergents. New Biotechnol., 2015, 32(6), 629-634.
[http://dx.doi.org/10.1016/j.nbt.2014.12.010]
[15]
Jain, D.; Pancha, I.; Mishra, S.K.; Shrivastav, A.; Mishra, S. Purification and characterization of haloalkaline thermoactive, solvent stable and SDS-induced protease from Bacillus sp.: A potential additive for laundry detergents. Bioresour. Technol., 2012, 115, 228-236.
[http://dx.doi.org/10.1016/j.biortech.2011.10.081] [PMID: 22100240]
[16]
Ansorge-Schumacher, M.B.; Thum, O. Immobilised lipases in the cosmetics industry. Chem. Soc. Rev., 2013, 42(15), 6475-6490.
[http://dx.doi.org/10.1039/c3cs35484a] [PMID: 23515487]
[17]
Sim, Y.C. Stabilization of papain and lysozyme for application to cosmetic products. Biotechnol. Lett., 2000, 22(2), 137-140.
[http://dx.doi.org/10.1023/A:1005670323912]
[18]
Banchhor, M.; Saraf, S. PHCOG REV.: Review article potentiality of papain as an antiaging agent in cosmetic formulation. Available from:. http://www.phcogrev.com Accessed: Mar. 24, 2021.
[19]
Ojha, B.K.; Singh, P.K.; Shrivastava, N. Enzymes in the animal feed industry.In: Enzymes in Food Biotechnology: Production, Applications, and Future Prospects; Elsevier, 2018, pp. 93-109.
[20]
Walsh, G.A.; Power, R.F.; Headon, D.R. Enzymes in the animal-feed industry. Trends In: Biotechnol., 1993, 11(10), 424-430.
[http://dx.doi.org/10.1016/0167-7799(93)90006-U]
[21]
Choct, M. Enzymes for the feed industry: Past, present and future. 2006, 62(1), 5-15.
[http://dx.doi.org/10.1079/WPS200480]
[22]
Bedford, M.R. The evolution and application of enzymes in the animal feed industry: the role of data interpretation. Br. Poult. Sci., 2018, 59(5), 486-493.
[http://dx.doi.org/10.1080/00071668.2018.1484074] [PMID: 29877713]
[23]
Maximov, V.; Reukov, V.; Vertegel, A.A. Targeted delivery of therapeutic enzymes. J. Drug Deliv. Sci. Technol., 2009, 19(5), 311-320.
[http://dx.doi.org/10.1016/S1773-2247(09)50066-4]
[24]
Farhadi, S.A.; Bracho-Sanchez, E.; Freeman, S.L.; Keselowsky, B.G.; Hudalla, G.A. Enzymes as Immunotherapeutics. Bioconjug. Chem., 2018, 29(3), 649-656.
[http://dx.doi.org/10.1021/acs.bioconjchem.7b00719] [PMID: 29285931]
[25]
Baldo, B.A. Enzymes approved for human therapy: indications, mechanisms and adverse effects. BioDrugs, 2015, 29(1), 31-55.
[http://dx.doi.org/10.1007/s40259-015-0116-7] [PMID: 25648140]
[26]
Weisfeldt, M.L.; Zieman, S.J. Advances in the prevention and treatment of cardiovascular disease. Health Aff. (Millwood), 2007, 26(1), 25-37.
[http://dx.doi.org/10.1377/hlthaff.26.1.25] [PMID: 17211011]
[27]
Sherry, S.; Johnson, A.; Tillett, W.S. The action of streptococcal desoxyribose nuclease (streptodornase),’ in vitro and on purulent pleural exudations of patients. J. Clin. Invest., 1949, 28(5 Pt 2), 1094-1104.
[28]
Ouriel, K. A history of thrombolytic therapy. J. Endovasc. Ther., 2004, 11(Suppl. 2), II-128-II–133.
[http://dx.doi.org/10.1177/15266028040110S614]
[29]
Tillett, W.S.; Garner, R.L. The fibrinolytic activity of hemolytic streptococci. J. Exp. Med., 1933, 58(4), 485-502.
[http://dx.doi.org/10.1084/jem.58.4.485] [PMID: 19870210]
[30]
Tow, D.E.; Wagner, H.N., Jr; Holmes, R.A. Urokinase in pulnonary embolism. N. Engl. J. Med., 1967, 277(22), 1161-1167.
[http://dx.doi.org/10.1056/NEJM196711302772202] [PMID: 6058603]
[31]
Sasahara, A.A. Urokinase: Past, present, and future. Tech. Vasc. Interv. Radiol., 1998, 1(4), 170-178.
[http://dx.doi.org/10.1016/S1089-2516(98)80223-0]
[32]
Stephani, L.; Tjandrawinata, R.R.; Afifah, D.N.; Lim, Y.; Ismaya, W.T.; Suhartono, M.T. Food origin fibrinolytic enzyme with multiple ac-tions. Hayati J. Biosci., 2017, 24(3), 124-130.
[http://dx.doi.org/10.1016/j.hjb.2017.09.003]
[33]
Chitte, R.R.; Dey, S. Potent fibrinolytic enzyme from a thermophilic Streptomyces megasporus strain SD5. Lett. Appl. Microbiol., 2000, 31(6), 405-410.
[http://dx.doi.org/10.1046/j.1365-2672.2000.00831.x] [PMID: 11123546]
[34]
Ambrus, J.L.; Ambrus, C.M.; Back, N.; Sokal, J.E.; Collins, G.L. Clinical and experimental studies on fibrinolytic enzymes. Ann. N. Y. Acad. Sci., 1957, 68(1), 97-136.
[http://dx.doi.org/10.1111/j.1749-6632.1957.tb42616.x] [PMID: 13479023]
[35]
Kim, W.; Choi, K.; Kim, Y.; Park, H.; Choi, J.; Lee, Y.; Oh, H.; Kwon, I.; Lee, S. Purification and characterization of a fibrinolytic enzyme produced from Bacillus sp. strain CK 11-4 screened from Chungkook-Jang. Appl. Environ. Microbiol., 1996, 62(7), 2482-2488.
[http://dx.doi.org/10.1128/aem.62.7.2482-2488.1996] [PMID: 8779587]
[36]
Peng, Y.; Huang, Q.; Zhang, R.H.; Zhang, Y.Z. Purification and characterization of a fibrinolytic enzyme produced by Bacillus amyloliquefa-ciens DC-4 screened from douchi, a traditional Chinese soybean food. Comp. Biochem. Physiol. B Biochem. Mol. Biol., 2003, 134(1), 45-52.
[http://dx.doi.org/10.1016/S1096-4959(02)00183-5] [PMID: 12524032]
[37]
Monkhouse, F.C.; Daramola, F.; Gillespie, R.J. The action of a proteolytic enzyme from aspergillus oryzae on. Can. J. Physiol. Pharmacol., 1964, 42, 377-384.
[http://dx.doi.org/10.1139/y64-047]
[38]
Rovati, J.I.; Delgado, O.D.; Figueroa, L.I.C.; Fariña, J.I. A novel source of fibrinolytic activity: Bionectria sp., an unconventional enzyme-producing fungus isolated from Las Yungas rainforest (Tucumán, Argentina). World J. Microbiol. Biotechnol., 2010, 26(1), 55-62.
[http://dx.doi.org/10.1007/s11274-009-0142-z]
[39]
Xiao-Lan, L.; Lian-Xiang, D.; Fu-Ping, L.; Xi-Qun, Z.; Jing, X. Purification and characterization of a novel fibrinolytic enzyme from Rhizo-pus chinensis 12. Appl. Microbiol. Biotechnol., 2005, 67(2), 209-214.
[http://dx.doi.org/10.1007/s00253-004-1846-5] [PMID: 15614557]
[40]
Shirasaka, N.; Naitou, M.; Okamura, K.; Kusuda, M.; Fukuta, Y.; Terashita, T. Purification and characterization of a fibrinolytic protease from Aspergillus oryzae KSK-3. Mycoscience, 2012, 53(5), 354-364.
[http://dx.doi.org/10.1007/S10267-011-0179-3]
[41]
el-Aassar, S.A.; el-Badry, H.M.; Abdel-Fattah, A.F. The biosynthesis of proteases with fibrinolytic activity in immobilized cultures of Peni-cillium chrysogenum H9. Appl. Microbiol. Biotechnol., 1990, 33(1), 26-30.
[http://dx.doi.org/10.1007/BF00170564] [PMID: 1367445]
[42]
El-Aassar, S.A. Production and properties of fibrinolytic enzyme in solid state cultures of Fusarium pallidoroseum. Biotechnol. Lett., 1995, 17(9), 943-948.
[http://dx.doi.org/10.1007/BF00127431]
[43]
Fayek, K.I.; Foda, M.S.; Naggar, M.R. Production physiology and properties of a novel fungal fibrinolytic enzyme. Z. Allg. Mikrobiol., 1976, 16(6), 417-423.
[http://dx.doi.org/10.1002/jobm.19760160602] [PMID: 10688]
[44]
Tao, S.; Beihui, L.; Peng, L.; Deming, L.; Zuohu, L. New solid-state fermentation process for repeated batch production of fibrinolytic en-zyme by Fusarium oxysporum. Process Biochem., 1998, 33(4), 419-422.
[http://dx.doi.org/10.1016/S0032-9592(97)00096-4]
[45]
Wu, B.; Wu, L.; Chen, D.; Yang, Z.; Luo, M. Purification and characterization of a novel fibrinolytic protease from Fusarium sp. CPCC 480097. J. Ind. Microbiol. Biotechnol., 2009, 36(3), 451-459.
[http://dx.doi.org/10.1007/s10295-008-0516-5] [PMID: 19142678]
[46]
Ueda, M.; Kubo, T.; Miyatake, K.; Nakamura, T. Purification and characterization of fibrinolytic alkaline protease from Fusarium sp. BLB. Appl. Microbiol. Biotechnol., 2007, 74(2), 331-338.
[http://dx.doi.org/10.1007/s00253-006-0621-1] [PMID: 17221202]
[47]
Lee, J.S.; Baik, H.S.; Park, S.S. Purification and characterization of two novel fibrinolytic proteases from mushroom, Fomitella fraxinea. J. Microbiol. Biotechnol., 2006, 16(2), 264-271.
[48]
Shen, M.H.; Kim, J.S.; Sapkota, K.; Park, S.E.; Choi, B.S.; Kim, S.; Lee, H.H.; Kim, C.S.; Chun, H.S.; Ryoo, C.I.; Kim, S.J. Purification, char-acterization, and cloning of fibrinolytic metalloprotease from Pleurotus ostreatus mycelia. J. Microbiol. Biotechnol., 2007, 17(8), 1271-1283.
[PMID: 18051595]
[49]
Choi, H-S.; Sa, Y-S. Fibrinolytic and antithrombotic protease from Ganoderma lucidum. Mycologia, 2000, 92(3), 545-552.
[http://dx.doi.org/10.2307/3761514]
[50]
Kim, J.H.; Kim, Y.S. Characterization of a metalloenzyme from a wild mushroom, Tricholoma saponaceum. Biosci. Biotechnol. Biochem., 2001, 65(2), 356-362.
[http://dx.doi.org/10.1271/bbb.65.356] [PMID: 11302169]
[51]
Cha, W.S.; Park, S.S.; Kim, S.J.; Choi, D. Biochemical and enzymatic properties of a fibrinolytic enzyme from Pleurotus eryngii cultivated under solid-state conditions using corn cob. Bioresour. Technol., 2010, 101(16), 6475-6481.
[http://dx.doi.org/10.1016/j.biortech.2010.02.048] [PMID: 20413306]
[52]
Sharjahan, M.A. Fibrinolytic activities of Mycosynthesized selenium nanoparticles with selected culinary mushrooms., 2017.
[53]
Silva, P. E.da C.e.; de Barros, R.C.; Albuquerque, W.W.C.; Brandão, R.M.P.; Bezerra, R.P.; Porto, A.L.F. In vitro thrombolytic activity of a purified fibrinolytic enzyme from Chlorella vulgaris. J. Chromatogr. B Analyt. Technol. Biomed. Life Sci., 2018, 1092, 524-529.
[http://dx.doi.org/10.1016/j.jchromb.2018.04.040]
[54]
Matsubara, K.; Matsuura, Y.; Sumi, H.; Hori, K.; Miyazawa, K. A fibrinolytic enzyme from the green alga Codium latum activates plasmino-gen. Fish. Sci., 2002, 68(2), 455-457.
[http://dx.doi.org/10.1046/j.1444-2906.2002.00448.x]
[55]
Wu, W.; Hasumi, K.; Peng, H.; Hu, X.; Wang, X.; Bao, B. Fibrinolytic compounds isolated from a brown alga, Sargassum fulvellum. Mar. Drugs, 2009, 7(2), 85-94.
[http://dx.doi.org/10.3390/md7020085] [PMID: 19597573]
[56]
Sumi, H.; Nakajima, N.; Mihara, H. Fibrinolysis relating substances in marine creatures. Comp. Biochem. Physiol., 1992, 102(1), 163-167.
[http://dx.doi.org/10.1016/0305-0491(92)90290-8]
[57]
Nakajima, N.; Mihara, H.; Sumi, H. Characterization of potent fibrinolytic enzymes in earthworm, Lumbricus rubellus. Biosci. Biotechnol. Biochem., 1993, 57(10), 1726-1730.
[http://dx.doi.org/10.1271/bbb.57.1726] [PMID: 7764268]
[58]
Bi, Q.; Han, B.; Feng, Y.; Jiang, Z.; Yang, Y.; Liu, W. Antithrombotic effects of a newly purified fibrinolytic protease from Urechis unicinc-tus. Thromb. Res., 2013, 132(2), e135-e144.
[http://dx.doi.org/10.1016/j.thromres.2013.07.001] [PMID: 23891134]
[59]
Tian, Z.; Li, B.; Guo, L.; Wu, M.; Fu, T.; Cheng, H.; Zhu, H. Purification and biochemical characterization of a novel fibrinolytic enzyme, PSLTro01, from a medicinal animal Porcellio scaber Latreille. Int. J. Biol. Macromol., 2015, 80, 536-546.
[http://dx.doi.org/10.1016/j.ijbiomac.2015.06.046] [PMID: 26123818]
[60]
Ahn, M.Y.; Hahn, B.S.; Ryu, K.S.; Kim, J.W.; Kim, I.; Kim, Y.S. Purification and characterization of a serine protease with fibrinolytic ac-tivity from the dung beetles, Catharsius molossus. Thromb. Res., 2003, 112(5-6), 339-347.
[http://dx.doi.org/10.1016/j.thromres.2004.01.005] [PMID: 15041280]
[61]
Rajput, M.S.; Mathur, V.; Agrawal, P.; Chandrawanshi, H.K.; Pilaniya, U. Fibrinolytic activity of kaempferol isolated from the fruits of La-genaria siceraria (Molina). Standley. Nat. Prod. Res., 2011, 25(19), 1870-1875.
[http://dx.doi.org/10.1080/14786419.2010.540760] [PMID: 21861768]
[62]
Kim, D.W.; Choi, J.H.; Park, S.E.; Kim, S.; Sapkota, K.; Kim, S.J. Purification and characterization of a fibrinolytic enzyme from Petasites japonicus. Int. J. Biol. Macromol., 2015, 72, 1159-1167.
[http://dx.doi.org/10.1016/j.ijbiomac.2014.09.046] [PMID: 25316419]
[63]
Al-Snafi, A.E. Therapeutic properties of medicinal plants: A review of plants with hypolipidemic, hemostatic, fibrinolytic and anticoagulant effects (part 1). Asian J. Pharm. Sci. Technol., 2015, 5, 271-284. Available from: www.ajpst.com Accessed on: Apr. 03, 2021..
[64]
Choi, J.H.; Kim, D.W.; Park, S.E.; Choi, B.S.; Sapkota, K.; Kim, S.; Kim, S.J. Novel thrombolytic protease from edible and medicinal plant Aster yomena (Kitam.) Honda with anticoagulant activity: purification and partial characterization. J. Biosci. Bioeng., 2014, 118(4), 372-377.
[http://dx.doi.org/10.1016/j.jbiosc.2014.03.004] [PMID: 24746735]
[65]
Patel, G.K.; Kawale, A.A.; Sharma, A.K. Purification and physicochemical characterization of a serine protease with fibrinolytic activity from latex of a medicinal herb Euphorbia hirta. Plant Physiol. Biochem., 2012, 52, 104-111.
[http://dx.doi.org/10.1016/j.plaphy.2011.12.004] [PMID: 22305073]
[66]
Cesarman-Maus, G.; Hajjar, K.A. Molecular mechanisms of fibrinolysis. Br. J. Haematol., 2005, 129(3), 307-321.
[http://dx.doi.org/10.1111/j.1365-2141.2005.05444.x] [PMID: 15842654]
[67]
Zorio, E.; Gilabert-Estellés, J.; España, F.; Ramón, L.A.; Cosín, R.; Estellés, A. Fibrinolysis: the key to new pathogenetic mechanisms. Curr. Med. Chem., 2008, 15(9), 923-929.
[http://dx.doi.org/10.2174/092986708783955455] [PMID: 18473800]
[68]
Niewiarowski, S. The mechanism of fibrinolysis., Pol. Arch. Med. wewntrznej, 1955, 25(1 a), 227-228..
[69]
Astrup, T.; Müllertz, S. The fibrin plate method for estimating fibrinolytic activity. Arch. Biochem. Biophys., 1952, 40(2), 346-351.
[http://dx.doi.org/10.1016/0003-9861(52)90121-5] [PMID: 12997222]
[70]
Zywicka-Lopaciuk, H. Fibrinolytic therapy. Pol. Tyg. Lek., 1962, 17(December), 1157-1161.
[PMID: 14004178]
[71]
Sherry, S.; Fletcher, A.P.; Alkjaersig, N. Fibrinolysis and fibrinolytic activity in man. Physiol. Rev., 1959, 39(2), 343-382.
[http://dx.doi.org/10.1152/physrev.1959.39.2.343] [PMID: 13645238]
[72]
Le, N.A. Cardiovascular disease. Curr. Opin. Lipidol., 2007, 18(6), 692-695.
[http://dx.doi.org/10.1097/MOL.0b013e3282f20df8] [PMID: 17993815]
[73]
Pala, R.; Anju, V.T.; Dyavaiah, M.; Busi, S.; Nauli, S.M. Nanoparticle-mediated drug delivery for the treatment of cardiovascular diseases. Int. J. Nanomedicine, 2020, 15, 3741-3769.
[http://dx.doi.org/10.2147/IJN.S250872] [PMID: 32547026]
[74]
Fitzmaurice, D.A.; Blann, A.D.; Lip, G.Y.H. Bleeding risks of antithrombotic therapy. BMJ, 2002, 325(7368), 828-831.
[http://dx.doi.org/10.1136/bmj.325.7368.828] [PMID: 12376447]
[75]
Castellino, F.J.; Powell, J.R. Human plasminogen. Methods Enzymol., 1981, 80(Pt C), 365-378.
[http://dx.doi.org/10.1016/S0076-6879(81)80031-6] [PMID: 6210827]
[76]
Hommel, M.; Cornu, C.; Boutitie, F.; Boissel, J.P. Thrombolytic therapy with streptokinase in acute ischemic stroke. N. Engl. J. Med., 1996, 335(3), 145-150.
[http://dx.doi.org/10.1056/NEJM199607183350301] [PMID: 8657211]
[77]
Ko, J.H.; Park, D.K.; Kim, I.C.; Lee, S.H.; Byun, S.M. High-level expression and secretion of streptokinase in Escherichia coli. Biotechnol. Lett., 1995, 17(10), 1019-1024.
[http://dx.doi.org/10.1007/BF00143093]
[78]
Szarka, S.J.; Sihota, E.G.; Habibi, H.R.; Wong, S. Staphylokinase as a plasminogen activator component in recombinant fusion proteins. Appl. Environ. Microbiol., 1999, 65(2), 506-513.
[http://dx.doi.org/10.1128/AEM.65.2.506-513.1999] [PMID: 9925575]
[79]
Banerjee, A.; Chisti, Y.; Banerjee, U.C. Streptokinase-a clinically useful thrombolytic agent. Biotechnol. Adv., 2004, 22(4), 287-307.
[http://dx.doi.org/10.1016/j.biotechadv.2003.09.004] [PMID: 14697452]
[80]
Sumi, H.; Hamada, H.; Tsushima, H.; Mihara, H.; Muraki, H. A novel fibrinolytic enzyme (nattokinase) in the vegetable cheese Natto; a typical and popular soybean food in the Japanese diet. Experientia, 1987, 43(10), 1110-1111.
[http://dx.doi.org/10.1007/BF01956052] [PMID: 3478223]
[81]
Oka, K.; Hirano, T.; Homma, M.; Ishii, H.; Murakami, K.; Mogami, S.; Motizuki, A.; Morita, H.; Takeya, K.; Itokawa, H. Satisfactory sepa-ration and MS-MS spectrometry of six surfactins isolated from Bacillus subtilis natto. Chem. Pharm. Bull. (Tokyo), 1993, 41(5), 1000-1002.
[http://dx.doi.org/10.1248/cpb.41.1000] [PMID: 8339332]
[82]
Takagaki, S.; Suzuki, M.; Suzuki, E.; Hasumi, K. Unsaturated fatty acids enhance the fibrinolytic activity of subtilisin NAT (nattokinase). J. Food Biochem., 2020, 44(8)e13326
[http://dx.doi.org/10.1111/jfbc.13326] [PMID: 32572985]
[83]
Dabbagh, F. Nattokinase: production and application. Appl. Microbiol. Biotechnol., 2014, 98(22), 9199-9206.
[http://dx.doi.org/10.1007/s00253-014-6135-3]
[84]
Cai, D.; Wei, X.; Qiu, Y.; Chen, Y.; Chen, J.; Wen, Z.; Chen, S. High-level expression of nattokinase in Bacillus licheniformis by manipulat-ing signal peptide and signal peptidase. J. Appl. Microbiol., 2016, 121(3), 704-712.
[http://dx.doi.org/10.1111/jam.13175] [PMID: 27159567]
[85]
Kim, J.Y.; Gum, S.N.; Paik, J.K.; Lim, H.H.; Kim, K.C.; Ogasawara, K.; Inoue, K.; Park, S.; Jang, Y.; Lee, J.H. Effects of nattokinase on blood pressure: A randomized, controlled trial. Hypertens. Res., 2008, 31(8), 1583-1588.
[http://dx.doi.org/10.1291/hypres.31.1583] [PMID: 18971533]
[86]
Markland, F.S. Snake venom fibrinogenolytic and fibrinolytic enzymes: An updated inventory. Registry of exogenous hemostatic factors of the scientific and standardization committee of the international society on thrombosis and haemostasis. Thromb. Haemost., 1998, 79(3), 668-674.
[http://dx.doi.org/10.1055/s-0037-1614964] [PMID: 9531060]

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