References
- Albertson, P. A. 1958. Particle fractionation in liquid two-phase systems. Biochim. Biophys. Acta 27:378–395. doi:https://doi.org/10.1016/0006-3002(58)90345-7.
- Anson, M. L. 1938. The estimation of pepsin, trypsin, papain, and cathepsin with hemoglobin. J. Gen. Physiol. 22:79–89. doi:https://doi.org/10.1085/jgp.22.1.79.
- Ashipala, O. K., and Q. He. 2008. Optimization of fibrinolytic enzyme production by Bacillus subtilis DC-2 in aqueous two-phase system (poly-ethylene glycol 4000 and sodium sulfate). Bioresour. Technol. 99:4112–4119. doi:https://doi.org/10.1016/j.biortech.2007.09.029.
- Baskir, J. N., T. A. Hantton, and U. W. Sutter. 1989. Protein partitioning in two-phase aqueous polymer system. Biotechnol. Bioeng. 34:541–558. doi:https://doi.org/10.1002/bit.260340414.
- Borah, D., R. N. S. Yadav, A. Sangra, L. Shahin, and A. K. Chaubey. 2012. Production, purification and characterization of nattokinase from Bacillus subtilis, isolated from tea garden soil samples of Dibrugarh, Assam. Asian J. Pharm. Clin. Res. 5 (Suppl 3):124–125.
- Bradford, M. M. 1976. Rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72:248–254. doi:https://doi.org/10.1016/0003-2697(76)90527-3.
- Chen, H., E. M. McGowan, N. Ren, S. Lal, N. Nassif, F. Shad-Kaneez, X. Qu, and Y. Lin. 2018. Nattokinase: A promising alternative in prevention and treatment of cardiovascular diseases. Biomark. Insight. 13:1177271918785130. doi:https://doi.org/10.1177/1177271918785130.
- Choi, N. S., K. H. Yoo, J. H. Hahm, K. S. Yoon, K. T. Chang, B. H. Hyun, P. J. Maeng, and S. H. Kim. 2005. Purification and characterization of a new peptidase, bacillopeptidase DJ-2, having fibrinolytic activity: Produced by Bacillus sp. DJ-2 from Doen-Jang. J. Microbiol. Biotechnol. 15:72–79.
- Choi, N. S., K. T. Chang, P. J. Maeng, and S. H. Kim. 2004. Cloning, expression, and fibrin (ogen)olytic properties of a subtilisin DJ-4 gene from Bacillus sp. DJ-4. FEMS Microbiol. Lett. 236:325–331. doi:https://doi.org/10.1111/j.1574-6968.2004.tb09665.x.
- Cruz Filho, R. F. D., J. G. Dos Santos, R. A. Palheta, V. C. Santos-Ebinuma, D. A. Viana Marques, and M. F. S. Teixeira. 2020. Comparison of conventional and extractive fermentation using aqueous two-phase system to extract fibrinolytic proteases produced by Bacillus stearothermophilus DPUA 1729. Prep. Biochem. Biotechnol. 26:1–10.
- Deepak, V., K. Kalishwaralal, S. Ramkumarpandian, S. V. Babu, S. R. Senthilkumar, and G. Sangiliyandi. 2008. Optimization of media composition for Nattokinase production by Bacillus subtilis using response surface methodology. Bioresour. Technol. 99:8170–8174. doi:https://doi.org/10.1016/j.biortech.2008.03.018.
- Environmental Protection Agency (EPA). 1997. Bacillus subtilis Final Risk Assessment. Washington, D.C.: US Environmental Protection Agency.
- Frias, J., D. Toubarro, A. Fraga, C. Botelho, J. Teixeira, J. Pedrosa, and N. Simões. 2021. Purification and characterization of a thrombolytic enzyme produced by a new strain of Bacillus subtilis. J. Microbiol. Biotechnol. 31:327–337. doi:https://doi.org/10.4014/jmb.2008.08010.
- Fujita, M., K. Hong, Y. Ito, S. Misawa, N. Takeuchi, K. Kariya, and S. Nishimuro. 1995. Transport of nattokinase across the rat intestinal tract. Biol. Pharm. Bull. 18:1194–1196. doi:https://doi.org/10.1248/bpb.18.1194.
- Fujita, M., K. Nomura, K. Hong, Y. Ito, A. Asada, and S. Nishimuro. 1993. Purification and character of a strong fibrinolytic enzyme (nattokinase) in the vegetable cheese natto, a popular soybean fermented food in Japan. Biochem. Biophys. Res. Commun. 197:1340–1347. doi:https://doi.org/10.1006/bbrc.1993.2624.
- Hernick, M., and C. Fierke. 2010. Mechanisms of Metal-Dependent Hydrolases in Metabolism. In Comprehensive Natural Products II, ed. H. W. (B) Liu, and L. Mander, 547–581. Amsterdam: Elsevier.
- Hu, Y., D. Yu, Z. Wang, J. Hou, R. Tyagi, Y. Liang, and Y. Hu. 2019. Purification and characterization of a novel, highly potent fibrinolytic enzyme from Bacillus subtilis DC27 screened from Douchi, a traditional Chinese fermented soybean food. Sci. Rep. 9:9235. doi:https://doi.org/10.1038/s41598-019-45686-y.
- Iqbal, M., Y. Tao, S. Xie, Y. Zhu, D. Chen, X. Wang, L. Huang, D. Peng, A. Sattar, M. A. B. Shabbir, et al. 2016. Aqueous two-phase system (ATPS): An overview and advances in its applications. Biol. Proced. Online 18:18. doi:https://doi.org/10.1186/s12575-016-0048-8.
- Ishida, N., A. Okubo, H. Kawai, S. Yamazaki, and S. Toda. 1980. Interaction of amino acids with transition metal ions in solution (I) solution structure of L-lysine with Co(II) and Cu(II) ions as studied by nuclear magnetic resonance spectroscopy. Agric. Biol. Chem. 44:263–270.
- Jayachandran, M., and B. Xu. 2019. An insight into the health benefits of fermented soy products. Food Chem. 271:362–371. doi:https://doi.org/10.1016/j.foodchem.2018.07.158.
- Jeong, S. J., K. Heo, J. Y. Park, K. W. Lee, J. Y. Park, S. H. Joo, and J. H. Kim. 2015. Characterization of AprE176, a fibrinolytic enzyme from Bacillus subtilis HK176. J. Microbiol. Biotechnol. 25:89–97. doi:https://doi.org/10.4014/jmb.1409.09087.
- Johansson, G. 1985. Partitioning of Proteins. In Partitioning in aqueous two-phase systems: Theory, methods, uses, and applications to biotechnology, ed. Walter, H., Brooks, D. E., and Fisher, D, 161–226. Cambridge, Massachusetts: Academic Press.
- Ju, S., Z. Cao, C. Wong, Y. Liu, M. F. Foda, Z. Zhang, and J. Li. 2019. Isolation and optimal fermentation condition of the Bacillus subtilis subsp. natto strain WTC016 for nattokinase production. Fermentation 5:92. doi:https://doi.org/10.3390/fermentation5040092.
- Kim, J. M., H. J. Suh, S. W. Ahn, M. S. Kim, and S. H. Oh. 2002. Fibrinolytic enzyme production by Bacillus subtilis KH-4 isolated from. Deonjang. Neutr. Food 7:417–420.
- Kim, W., K. Choi, Y. Kim, H. Park, J. Choi, Y. Lee, H. Oh, I. Kwon, and S. Lee. 1996. Purification and characterization of a fibrinolytic enzyme produced from Bacillus sp. strain CK11-4 screened from Chungkook-Jang. Appl. Environ. Microbiol. 62:2482–2488. doi:https://doi.org/10.1128/aem.62.7.2482-2488.1996.
- Lee, C. H., and S. I. Sandler. 1990. Vancomycin partitioning in aqueous two-phase system: Effect of pH, salts, and an affinity ligand. Biotechnol. Bioeng. 35:408–416. doi:https://doi.org/10.1002/bit.260350408.
- Lee, J. W., S. Y. Park, W. A. Choi, K. H. Lee, Y. K. Jeong, I. S. Kong, and S. H. Park. 1999. Production of a fibrinolytic enzyme in bioreactor culture by Bacillus subtilis BK-17. J. Microbiol. Biotechnol. 9:443–449.
- Lin, H. T. V., G. J. Wu, M. C. Hsieh, S. H. Chang, and G. J. Tsai. 2015. Purification and characterization of nattokinase from cultural filtrate of red alga porphyra dentata fermented by Bacillus subtilis N1. J. Mar. Sci. Technol. 23:240–248.
- Loc, N. H., N. T. T. Mien, and D. T. B. Thuy. 2010. Purification of extracellular α-amylase from Bacillus subtilis by partitioning in a polyethylene glycol/potassium phosphate aqueous two-phase system. Ann. Microbiol. 60:623–628. doi:https://doi.org/10.1007/s13213-010-0100-x.
- Lucy, J., P. F. Raharjo, E. Elvina, L. Florencia, A. I. Susanti, and R. Pinontoan. 2019. Clot lysis activity of Bacillus subtilis G8 isolated from Japanese fermented natto soybeans. Appl. Food Biotechnol. 6:101–109.
- Man, L., and D. J. Xiang. 2019. Stability of nattokinase produced by Bacillus subtilis MX-6 from douchi. China Cond. 44:25–28.
- Nagai, T., K. Yamada, M. Yoshimura, K. Ishikawa, Y. Miyamoto, K. Hashimoto, Y. Noda, A. Nitta, and T. Nabeshima. 2004. The tissue plasminogen activator-plasmin system participates in the rewarding effect of morphine by regulating dopamine release. PNAS 101:3650–3655. doi:https://doi.org/10.1073/pnas.0306587101.
- Nascimento, T. P., A. E. Sales, C. S. Porto, R. M. P. Brandão, G. M. de Campos-takaki, J. A. C. Teixeira, T. S. Porto, A. L. F. Porto, and A. Converti. 2016. Purification of a fibrinolytic protease from Mucor subtilissimus UCP 1262 by aqueous two-phase systems (PEG/sulfate). J. Chromatogr. B 1025:16–24. doi:https://doi.org/10.1016/j.jchromb.2016.04.046.
- Nguyen, T. T., D. T. Quyen, and H. T. Le. 2013. Cloning and enhancing production of a detergent- and organic-solvent-resistant nattokinase from Bacillus subtilis VTCC-DVN-12-01 by using an eight-protease-gene-deficient Bacillus subtilis WB800. Microb. Cell Fact. 12:79. doi:https://doi.org/10.1186/1475-2859-12-79.
- Peng, Y., Q. Huang, R. H. Zhang, and Y. Z. Zhang. 2003. Purification and characterization of a fibrinolytic enzyme produced by Bacillus amyloliquefaciens DC-4 screened from douchi, a traditional Chinese soybean food. Comp. Biochem. Physiol. B Biochem. Mol. Biol. 134:45–52. doi:https://doi.org/10.1016/S1096-4959(02)00183-5.
- Peng, Y., X. Yang, and Y. Zhang. 2005. Microbial fibrinolytic enzymes: An overview of sources, production, properties, and thrombolytic activity in vivo. Appl. Microbiol. Biotechnol. 69:126–132.
- Pinontoan, R., A. S. Elvina, and J. Jo. 2021. Fibrinolytic characteristics of Bacillus subtilis G8 isolated from natto. Biosci. Microbiota. Food Health 40 (3):144–149. Article: 2020-071. doi:https://doi.org/10.12938/bmfh.2020-071.
- Raju, E. V. N., and G. Divakar. 2014. An overview on microbial fibrinolytic proteases. Int. J. Pharm. Sci. Res. 5:643–656.
- Roth, V. 2016. Doubling Time Computing. http://www.doubling-time.com/compute.php (Accessed April 29. 2020).
- Sahoo, A., B. Mahanty, A. Daverey, and K. Dutta. 2020. Nattokinase production from Bacillus subtilis using cheese whey: Effect of nitrogen supplementation and dynamic modelling. J. Water Process Eng. 38:101533. doi:https://doi.org/10.1016/j.jwpe.2020.101533.
- Scawen, M. D., and P. M. Hammond. 2002. Downstream processing: Protein extraction and purification. In Molecular Biology and Biotechnology, ed. J. M. Walker and R. Rapley, 461–496. UK: The Royal Society of Chemistry.
- Sharma, D., S. K. Shekhar, A. Kumar, and J. Godheja. 2020. Isolation, characterization, production and purification of fibrinolytic enzyme nattokinase from Bacillus subtilis. Int. J. Pharm. Sci. Res. 11:1768–1776.
- Silva, A. V., J. M. Nascimento, C. H. Rodrigues, D. C. S. Nascimento, R. M. P. B. Costa, D. A. V. Marques, A. C. L. Leite, M. V. B. Figueiredo, L. Pastrana, A. Converti, et al. 2020. Partial purification of fibrinolytic and fibrinogenolytic protease from Gliricidia sepium seeds by aqueous two-phase system. Biocatal. Agric. Biotechnol. 27:101669. doi:https://doi.org/10.1016/j.bcab.2020.101669.
- Silva, G. M. M., D. A. V. Marques, T. S. Porto, J. L. Lima Filho, J. A. C. Teixeira, A. Pessoa Junior, and A. L. F. Porto. 2013. Extraction of fibrinolytic proteases from Streptomyces sp. DPUA1576 using PEG-phosphate aqueous two-phase systems. Fluid. Phase Equ. 339:52–57. doi:https://doi.org/10.1016/j.fluid.2012.11.033.
- Singh, P., R. Negi, V. Sharma, A. Rani, Pallavi, and R. Prasad. 2008. Production of fibrinolytic enzyme (Nattokinase) from Bacillussp. Indo. Am. J. Pharm. Sci. 5:379–383.
- Souza, F., J. Nascimento, A. E. Sales, N. M. Silva, J. C. Marcos, T. S. Porto, A. Teixeira José, and A. L. F. Porto. 2012. Partitioning of fibrinolytic protease from Bacillus sp. UFPEDA 485 by aqueous two-phase systems using PEG/sodium sulfate. XI Reunião Regional Nordeste da SBBq, 4th International Symposium in Biochemistry of Macromolecules and Biotechnology, Recife, Brazil, Dec 5-7.
- Suwanmanon, K., and P. C. Hsieh. 2014. Isolating Bacillus subtilis and optimizing its fermentative medium for GABA and nattokinase production. CyTA - J. Food 1:282–290. doi:https://doi.org/10.1080/19476337.2013.848472.
- Thu, N. T. A., N. T. M. Khue, N. D. Huy, N. Q. D. Tien, and N. H. Loc. 2020. Characterizations and fibrinolytic activity of serine protease from Bacillus subtilis C10. Curr. Pharm. Biotechnol. 21:110–116. doi:https://doi.org/10.2174/1389201020666191002145415.
- Urano, T., H. Ihara, K. Umemura, Y. Suzuki, M. Oike, S. Akita, Y. Tsukamoto, I. Suzuki, and A. Takada. 2001. The Profibrinolytic enzyme subtilisin NAT purified from Bacillus subtilis cleaves and inactivates plasminogen activator inhibitor type 1. J. Biol. Chem. 276:24690–24696. doi:https://doi.org/10.1074/jbc.M101751200.
- Vázquez-Villegas, P., E. Espitia-Saloma, M. A. Torres-Acosta, F. Ruiz-Ruiz, M. Rito-Palomares, and O. Aguilar. 2018. Factorial and economic evaluation of an aqueous two-phase partitioning pilot plant for invertase recovery from spent brewery yeast. Front Chem. 6:454. doi:https://doi.org/10.3389/fchem.2018.00454.
- VKM. (2016). Risk assessment of the biological plant protection product Serenade ASO, with the organism Bacillus subtilis QST 713. Opinion of the Panel on Plant Protection Products of the Norwegian Scientific Committee for Food Safety. VKM Report 2016: 21. Oslo, Norway.
- Wang, C., M. Du, D. Zheng, F. Kong, G. Zu, and Y. Feng. 2009. Purification and characterization of nattokinase from Bacillus subtilis natto B-12. J. Agric. Food Chem. 57:9722–9729. doi:https://doi.org/10.1021/jf901861v.
- Weng, Y., J. Yao, S. Sparks, and K. Y. Wang. 2017. Nattokinase: An oral antithrombotic agent for the prevention of cardiovascular disease. Int. J. Mol. Sci. 18:523. doi:https://doi.org/10.3390/ijms18030523.
- Xu, Y., G. Q. He, and J. J. Li. 2005. Effective extraction of elastase from Bacillus sp. fermentation broth using aqueous two-phase system. J. Zheijang Univ. Sci. B 6:1087–1094. doi:https://doi.org/10.1631/jzus.2005.B1087.
- Zhi, W., J. Song, J. Bi, and F. Ouyang. 2004. Partial purification of α-amylase from culture supernatant of Bacillus subtilis in aqueous two-phase systems. Bioprocess Biosyst. Eng. 27:3–7. doi:https://doi.org/10.1007/s00449-004-0369-x.