Full Length Research Paper
References
|
Chen HJ, Eileen MG, Nina R, Sara L, Najah N, Fatima SK (2018). Nattokinase: A Promising Alternative in Prevention and Treatment of Cardiovascular Diseases. Biomarker Insights 13:117727191878513-. |
|
|
Chityala S, Venkata DV, Ahmad J, Prakasham RS (2015). High yield expression of novel glutaminase freel-asparaginase II ofPectobacterium carotovorumMTCC 1428 in Bacillus subtilisWB800N. Bioprocess and Biosystems Engineering 38(11):2271-2284. |
|
|
Dabbagh F, Negahdaripour M, Berenjian A, Behfar A, Mohammadi F, Zamani M (2014). Nattokinase: production and application. Applied Microbiology and Biotechnology 98(22):9199-9206. |
|
|
Fujita M, Nomura K, Hong K, Ito Y, Asada A, Nishimuro S(1993). Purification and Characterization of a Strong Fibrinolytic Enzyme (Nattokinase) in the Vegetable Cheese Natto, a Popular Soybean Fermented Food in Japan. Biochemical and Biophysical Research Communications 197(3):0-1347. |
|
|
Fujita M, Hong K, Ito Y, Fujii R, Kariya K, Nishimuro S (1995). Thrombolytic Effect of Nattokinase on a Chemically Induced Thrombosis Model in Rat. Biological and Pharmaceutical Bulletin 18(10):1387-1391. |
|
|
Glick BR(1995). Metabolic Load and Heterologous Gene Expression. Biotechnology Advances 13(2):247-261. |
|
|
Guan C, Cui W, Cheng J, Zhou L, Liu Z, Zhou Z(2016). Development of an efficient autoinducible expression system by promoter engineering in Bacillus subtilis. Microbial Cell Factories 15(1):66. |
|
|
Hsia CH, Shen MC, Lin JS, Wen YK, Yang NC (2009). Nattokinase decrease plasma levels of fibrinogen, factor VII, and factor VIII in human subjects. Nutrition Research 29(3):190-196. |
|
|
Jia Y, Liu H, Bao W, Weng M, Chen W, Cai Y(2010). Functional analysis of propeptide as an intramolecular chaperone for in vivo folding of subtilis in nattokinase. Febs Letters 584(23):4789-4796. |
|
|
Kurosawa Y, Nirengi S, Homma T, Esaki K, Ohta M, Clark JF (2015). A single-dose of oral nattokinase potentiates thrombolysis and anti-coagulation profiles. Scientific Reports 5:11601. |
|
|
Lee BH, Lai YS, Wu SC (2015). Antioxidation, angiotensin converting enzyme inhibition activity, nattokinase, and antihypertension of Bacillus subtilis (natto)-fermented pigeon pea. Journal of Food and Drug Analysis 23(4):750-757. |
|
|
Lampe BJ, English JC (2016). Toxicological assessment of nattokinase derived from Bacillus subtilis var. natto. Food and Chemical Toxicology An International Journal Published for the British Industrial Biological Research Association 88:87-99. |
|
|
Laemmli UK (1970). Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680-685. |
|
|
Luan C, Zhang HW, Song DG, Xie YG, Feng G, Wang YZ (2014). Expressing antimicrobial peptide cathelicidin-BF in Bacillus subtilis using SUMO technology. Applied Microbiology and Biotechnology 98(8):3651-3658. |
|
|
Metkar SK, Girigoswami A, Murugesan R, Girigoswami K (2017). In vitro and in vivo insulin amyloid degradation mediated by Serratiopeptidase. Materials Science and Engineering 70(1):728-735. |
|
|
Man LL, Xiang DJ, Zhang CL (2018). Strain Screening from Traditional Fermented Soybean Foods and Induction of Nattokinase Production in Bacillus subtilis MX-6. Probiotics and Antimicrobial Proteins 11(1):283-294. |
|
|
Nagata C, Wada K, Tamura T, Konishi K, Goto Y, Koda S (2017). Dietary soy and natto intake and cardiovascular disease mortality in Japanese adults: the Takayama study. The American Journal of Clinical Nutrition 105(2):426-431. |
|
|
Nakamura T, Yamagata Y, Ichishima E (1992). Nucleotide Sequence of the Subtilis in NAT Gene, aprN, of Bacillus subtilis (natto). Bioscience Biotechnology and Biochemistry 56(11):1869-1871. |
|
|
Ni H, Guo PC, Jiang WL, Fan XM, Luo XY, Li HH (2016). Expression of nattokinase in Escherichia coli and renaturation of its inclusion body. Journal of Biotechnology:S0168165616302905. |
|
|
Nishito Y, Osana Y, Hachiya T, Popendorf K, Toyoda A, Fujiyama A (2010). Whole genome assembly of a natto production strain Bacillus subtilis natto from very short read data. BMC Genomics 11(1):243-0. |
|
|
Nakagawa M, Ueyama M, Tsuruta H, Uno T, Kanamaru K, Mikami B (2010). Functional Analysis of the Cucumisin Propeptide as a Potent Inhibitor of Its Mature Enzyme. Journal of Biological Chemistry 285(39):29797-29807. |
|
|
Nandana V, Singh S, Singh AN, Dubey VK (2014). Procerain B, a cysteine protease from Calotropis procera, requires N-terminus pro-region for activity: cDNA cloning and expression with pro-sequence. Protein Expression and Purification 103:16-22. |
|
|
Nguyen TT, Quyen TD, Le HT (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. Microbial Cell Factories 12(1):1-11. |
|
|
Park KJ, Kang JI, Kim TS, Yeo IH (2012). The Antithrombotic and Fibrinolytic Effect of Natto in Hypercholesterolemia Rats. Preventive Nutrition and Food Science 17(1):78-82. |
|
|
Peng Y, Yang X, Zhang Y (2005). Microbial fibrinolytic enzymes: An overview of source, production, properties, and thrombolytic activity in vivo. Applied Microbiology and Biotechnology 69(2):126-132. |
|
|
Ren N, Chen H, Li Y, McGowan E, Lin Y (2017). A clinical study on the effect of nattokinase on carotid artery atherosclerosis and hyperlipidaemia. Chinese Medical Journal 97(26):2038-2042. |
|
|
Sone M, Falzon LM (2005). The role of tryptophan residues in the autoprocessing of prosubtilisin E. BBA - Proteins and Proteomics 1749(1):15-22. |
|
|
Sumi H, Hamada H, Tsushima H, Mihara H, Muraki H(1987). A novel fibrinolytic enzyme (nattokinase) in the vegetable cheese Natto; a typical and popular soybean food in the Japanese diet. Experientia 43(10):1110-1111. |
|
|
Sumi H, Hamada H, Tsushima H, Mihara H(1988). 155 A novel strong fibrinolytic enzyme (Nattokinase) in the vegetable cheese "NATTO". Fibrinolysis 2(1):67. |
|
|
Sumi H, Hamada H, Nakanishi K, Hiratani H(1990). Enhancement of the Fibrinolytic Activity in Plasma by Oral Administration of Nattokinases. Acta Haematologica 84(3):139-143. |
|
|
Tu Q, Yin J, Fu J, Herrmann J, Li Y, Yin Y(2016). Room temperature electrocompetent bacterial cells improve DNA transformation and recombineering efficiency. Scientific Reports 6:24648. |
|
|
Vojcic L, Despotovic D, Martinez R, Maurer KH, Schwaneberg U (2012). An efficient transformation method for Bacillus subtilis DB104. Applied Microbiology and Biotechnology 94(2):487-493. |
|
|
Wei X, Zhou Y, Chen J, Cai D, Wang D, Qi G (2015). Efficient expression of nattokinase in Bacillus licheniformis: host strain construction and signal peptide optimization. Journal of Industrial Microbiology and Biotechnology 42(2):287-295. |
|
|
Wu SM, Feng C, Zhong J, Huan LD (2011). Enhanced production of recombinant nattokinase in Bacillus subtilis by promoter optimization. World Journal of Microbiology and Biotechnology 27(1):99-106. |
|
|
Weng M, Zheng Z, Bao W, Cai Y, Yin Y, Zou G (2009). Enhancement of oxidative stability of the subtilisin nattokinase by site-directed mutagenesis expressed in Escherichia coli. BBA - Proteins and Proteomics 1794(11):1566-1572. |
|
|
Yabuta Y, Takagi H, Inouye M (2001). Folding pathway mediated by an intramolecular chaperone: propeptide release modulates activation precision of pro-subtilisin. Journal of Biological Chemistry 276(48):44427-44434. |
|
|
Zhou J, Li X, Xia J, Wen Y, Zhou J, Yu Z (2018). The role of temperature and bivalent ions in preparing competent Escherichia coli. 3 Biotech 8(5):222. |
|
Copyright © 2025 Author(s) retain the copyright of this article.
This article is published under the terms of the Creative Commons Attribution License 4.0
