[1]
|
Chen, H., McGowan, E.M., Ren, N., et al. (2018) Nattokinase: A Promising Alternative in Prevention and Treatment of Cardiovascular Diseases. Biomark, 13. https://doi.org/10.1177/1177271918785130
|
[2]
|
Sumi, H., Hamada, H., Tsushima, H., et al. (1987) A Novel Fibrinolytic Enzyme (Nattokinase) in the Vegetable Cheese Natto; a Typical and Popular Soybean Food in the Japanese Diet. Experientia, 43, 1110-1111.
https://doi.org/10.1007/BF01956052
|
[3]
|
Jensen, G.S., Lenninger, M., Ero, M.P., et al. (2016) Consumption of Nattokinase Is Associated with Reduced Blood Pressure and von Willebrand Factor, a Cardiovascular Risk Marker: Results from a Randomized, Double-Blind, Placebo-Controlled, Multicenter North American Clinical Trial. Integrative and Comparative Biology, 9, 95-104.
https://doi.org/10.2147/IBPC.S99553
|
[4]
|
孟繁宇, 薛菲, 施慧. 纳豆激酶对动脉粥样硬化模型大鼠血脂及血液流变学影响[J]. 中国实验诊断学, 2013, 17(9): 1567-1569.
|
[5]
|
Ji, H., Yu, L., Liu, K., et al. (2014) Mechanisms of Nattokinase in Protection of Cerebral Ischemia. European Journal of Pharmacology, 745, 144-151. https://doi.org/10.1016/j.ejphar.2014.10.024
|
[6]
|
占慧琴, 袁志兰, 杨翎, 等. 纳豆激酶对视网膜中央静脉阻塞动物模型中闪光视网膜电图的影响[J]. 南京医科大学学报(自然科学版), 2010, 30(7): 974-976+1016.
|
[7]
|
Takabayashi, T., Imoto, Y., Sakashita, M., et al. (2017) Nattokinase, Profibrinolytic Enzyme, Effectively Shrinks the Nasal Polyp Tissue and Decreases Viscosity of Mucus. Allergology International, 66, 594-602.
https://doi.org/10.1016/j.alit.2017.03.007
|
[8]
|
(2012) Optimisation of Preparation Conditions and Properties of Phytosterol Liposome-Encapsulating Nattokinase. Natural Product Research, 26, 548-556. https://doi.org/10.1080/14786419.2010.528759
|
[9]
|
陈景鑫. 纳豆激酶微胶囊的制备及其稳定性研究[D]: [硕士学位论文]. 大庆: 黑龙江八一农垦大学, 2010.
|
[10]
|
谢建飞. 一种含有纳豆激酶和益生菌的微胶囊及其制备方法和应用[P]. 中国, CN201410618436.7. 2015-02-25.
|
[11]
|
Zhang, X., Lyu, X., Tong, Y., et al. (2020) Chitosan/Casein Based Microparticles with a Bilayer Shell-Core Structure for Oral Delivery of Nattokinase. Food & Function, 11, 10799-10816. https://doi.org/10.1039/D0FO02349C
|
[12]
|
Deepak, V., Kalishwaralal, K., Ramkumarpandian, S., et al. (2008) Optimization of Media Composition for Nattokinase Production by Bacillus subtilis Using Response Surface Methodology. Bioresource Technology, 99, 8170-8174.
https://doi.org/10.1016/j.biortech.2008.03.018
|
[13]
|
李佳增. 纳豆激酶毕赤酵母X33高效表达双启动子系统构建及发酵条件优化[D]: [硕士学位论文]. 沈阳: 辽宁大学, 2021.
|
[14]
|
Nakamura, T., Yamagata, Y. and Ichishima, E. (1992) Nucleotide Sequence of the Subtilisin NAT Gene, aprN, of Bacillus subtilis (Natto). Bioscience, Biotechnology, and Biochemistry, 56, 1869-1871.
https://doi.org/10.1271/bbb.56.1869
|
[15]
|
Yanagisawa, Y., Chatake, T., Chiba-Kamoshida, K., et al. (2010) Purification, Crystallization and Preliminary X-Ray Diffraction Experiment of Nattokinase from Bacillus subtilis Natto. Acta Crystallographica Section F, 66, 1670-1673.
https://doi.org/10.1107/S1744309110043137
|
[16]
|
Carter, P. and Wells, J.A. (1988) Dissecting the Catalytic Triad of a Serine Protease. Nature, 332, 564-568.
https://doi.org/10.1038/332564a0
|
[17]
|
Weng, Y., Yao, J., Sparks, S., et al. (2017) Nattokinase: An Oral Antithrombotic Agent for the Prevention of Cardiovascular Disease. International Journal of Molecular Sciences, 18, 523. https://doi.org/10.3390/ijms18030523
|
[18]
|
李睿, 阮文辉, 熊晓辉. 纳豆激酶的酶学性质研究[J]. 扬州大学学报(农业与生命科学版), 2015, 36(2): 106-110.
|
[19]
|
Li, Y., et al. (2010) Bioproperties of Potent Nattokinase from Bacillus subtilis YJ1. Journal of Agricultural and Food Chemistry, 58, 5737-5742. https://doi.org/10.1021/jf100290h
|
[20]
|
Li, Y., et al. (2022) Biotechnology, Bioengineering and Applications of Bacillus nattokinase. Biomolecules, 12, 980.
https://doi.org/10.3390/biom12070980
|
[21]
|
Liang, X., Jia, S., Sun, Y., et al. (2007) Secretory Expression of Nattokinase from Bacillus subtilis YF38 in Escherichia coli. Molecular Biotechnology, 37, 187-194. https://doi.org/10.1007/s12033-007-0060-y
|
[22]
|
何孝天, 刘中美, 崔文璟, 等. 介导纳豆激酶分泌表达的信号肽比较[J]. 现代食品科技, 2014, 30(5): 62-68.
|
[23]
|
Cai, D., Wei, X., Qiu, Y., et al. (2016) High-Level Expression of Nattokinase in Bacillus licheniformis by Manipulating Signal Peptide and Signal Peptidase. Journal of Applied Microbiology, 121, 704-712.
https://doi.org/10.1111/jam.13175
|
[24]
|
Jia, Y., Liu, H., Bao, W., et al. (2010) Functional Analysis of Propeptide as an Intramolecular Chaperone for in Vivo Folding of Subtilisin Nattokinase. FEBS Letters, 584, 4789-4796. https://doi.org/10.1016/j.febslet.2010.11.011
|
[25]
|
Yang, M., Wu, J., Huang, Q. and Jia, Y. (2021) Probing the Role of Catalytic Triad on the Cleavage between Intramolecular Chaperone and NK Mature Peptide. Journal of Agricultural and Food Chemistry, 69, 2348-2353.
https://doi.org/10.1021/acs.jafc.0c07238
|
[26]
|
Ikemura, H., Takagi, H. and Inouye, M. (1987) Requirement of Pro-Sequence for the Production of Active Subtilisin E in Escherichia coli. Journal of Biological Chemistry, 262, 7859-7864. https://doi.org/10.1016/S0021-9258(18)47646-6
|
[27]
|
Jain, S.C., Shinde, U., Li, Y., et al. (1998) The Crystal Structure of an Autoprocessed Ser221 Cys-Subtilisin E-Propeptide Complex at 2.0 A Resolution. Journal of Molecular Biology, 284, 137-144.
https://doi.org/10.1006/jmbi.1998.2161
|
[28]
|
田莉. 构建高产纳豆激酶基因工程菌株及酶活研究[D]: [硕士学位论文]. 武汉: 武汉工程大学, 2019.
|
[29]
|
Weng, M., Zheng, Z., Bao, W., et al. (2009) Enhancement of Oxidative Stability of the Subtilisin Nattokinase by Site-Directed Mutagenesis Expressed in Escherichia coli. Biochimica et Biophysica Acta, 1794, 1566-1572.
https://doi.org/10.1016/j.bbapap.2009.07.007
|
[30]
|
Jia, Y., Cao, X., Deng, Y., et al. (2014) Four Residues of Propeptide Are Essential for Precursor Folding of Nattokinase. Acta Biochimica et Biophysica Sinica (Shanghai), 46, 957-964. https://doi.org/10.1093/abbs/gmu093
|
[31]
|
Cai, Y.J., et al. (2011) Directed Evolution Improves the Fibrinolytic Activity of Nattokinase from Bacillus natto. FEMS Microbiology Letters, 325, 155-161. https://doi.org/10.1111/j.1574-6968.2011.02423.x
|
[32]
|
Wu, S., Feng, C., Zhong, J. and Huan, L. (2007) Roles of s3 Site Residues of Nattokinase on Its Activity and Substrate Specificity. The Journal of Biochemistry, 142, 357-364. https://doi.org/10.1093/jb/mvm142
|
[33]
|
赵菡, 周丽, 周哲敏. 通过定点突变提高纳豆激酶的酶活及热稳定性[J]. 食品与发酵工业, 2018, 44(9): 36-40+47.
|
[34]
|
Weng, M., Deng, X., Bao, W., et al. (2015) Improving the Activity of the Subtilisin Nattokinase by Site-Directed Mutagenesis and Molecular Dynamics Simulation. Biochemical and Biophysical Research Communications, 465, 580-586.
https://doi.org/10.1016/j.bbrc.2015.08.063
|
[35]
|
刘中美, 何孝天, 崔文璟, 周哲敏. 通过定点突变增强纳豆激酶的热稳定性[J]. 现代食品科技, 2015, 31(2): 37-41.
|
[36]
|
Zhao, H. and Arnold, F.H. (1999) Directed Evolution Converts Subtilisin E into a Functional Equivalent of Thermitase. Protein Engineering, 12, 47-53. https://doi.org/10.1093/protein/12.1.47
|
[37]
|
刘朔, 姜梅, 陈晓红, 等. 纳豆激酶第36位氨基酸突变对其活性及热稳定性的影响[J]. 南京农业大学学报, 2008(3): 130-136.
|