Characterization of AprE176, a Fibrinolytic Enzyme from Bacillus subtilis HK176 |
Jeong, Seon-Ju
(Division of Applied Life Science (BK21 Plus), Graduate School, Gyeongsang National University)
Heo, Kyeong (Division of Applied Life Science (BK21 Plus), Graduate School, Gyeongsang National University) Park, Ji Yeong (Division of Applied Life Science (BK21 Plus), Graduate School, Gyeongsang National University) Lee, Kang Wook (Institute of Agriculture and Life Science, Gyeongsang National University) Park, Jae-Yong (Department of Food Science and Nutrition, Catholic University of Daegu) Joo, Sang Hoon (College of Pharmacy, Catholic University of Daegu) Kim, Jeong Hwan (Division of Applied Life Science (BK21 Plus), Graduate School, Gyeongsang National University) |
1 | Bryan PN. 2000. Protein engineering of subtilisin. Biochim. Biophys. Acta 1543: 203-222. DOI ScienceOn |
2 | Cadwell RC, Joyce GF. 1994. Mutagenic PCR. Genome Res. 3: S136-S140. DOI |
3 | Estell DA, Graycar TP, Wells JA. 1985. Engineering an enzyme by site-directed mutagenesis to be resistant to chemical oxidation. J. Biol. Chem. 260: 6518-6521. |
4 | Ghasemi Y, Dabbagh F, Ghasemmian A. 2012. Cloning of a fibrinolytic enzyme (subtilisin) gene from Bacillus subtilis in Escherichia coli. Mol. Biotechnol. 52: 1-7. DOI ScienceOn |
5 | Heo K, Cho KM, Lee CK, Kim GM, Shin JH, Kim JS, Kim JH. 2013. Characterization of a fibrinolytic enzyme secreted by Bacillus amyloliquefaciens CB1 and its gene cloning. J. Microbiol. Biotechnol. 23: 974-983. DOI ScienceOn |
6 | Jaouadi B, Aghajari N, Haser R, Bejar S. 2010. Enhancement of the thermostability and the catalytic efficiency of Bacillus pumilus CBS protease by site-directed mutagenesis. Biochimie 92: 360-369. DOI ScienceOn |
7 | Jeong S-J, Kwon G-H, Chun J, Kim JS, Park C-S, Kwon DY, Kim JH. 2007. Cloning of fibrinolytic enzyme gene from Bacillus subtilis isolated from cheonggukjang and its expression in protease-deficient Bacillus subtilis strain. J. Microbiol. Biotechnol. 17: 1018-1023. |
8 | Killer M, Ladurner G, Kunz AB, Kraus J. 2010. Current endovascular treatment of acute stroke and future aspects. Drug Discov. Today 15: 640-647. DOI ScienceOn |
9 | Jeong S-J, Cho KM, Lee CK, Kim GM, Shin JH, Kim JS, Kim JH. 2014. Overexpression of aprE2, a fibrinolytic enzyme gene from Bacillus subtilis CH3-5, in Escherichia coli and the properties of AprE2. J. Microbiol. Biotechnol. 24: 969-978. DOI ScienceOn |
10 | Jo H-D, Kwon G-H, Park J-Y, Cha J, Song Y-S, Kim JH. 2011. Cloning and overexpression of aprE3-17 encoding the major fibrinolytic protease of Bacillus licheniformis CH 3-17. Biotechnol. Bioproc. Eng. 16: 352-359. DOI ScienceOn |
11 | Khurana J, Singh R, Kaur J. 2011. Engineering of Bacillus lipase by directed evolution for enhanced thermal stability: effect of isoleucine to threonine mutation at protein surface. Mol. Biol. Rep. 38: 2919-2926. DOI |
12 | Kim GM, Lee AR, Lee KW, Park J-Y, Chun J, Cha J, et al. 2009. Characterization of a 27 kDa fibrinolytic enzyme from Bacillus amyloliquefaciens CH51 isolated from cheonggukjang. J. Microbiol. Biotechnol. 19: 997-1004. DOI |
13 | Kim S-H, Choi N-S. 2000. Purification and characterization of subtilisin DJ-4 secreted by Bacillus sp. strain DJ-4 screened from doen-jang. Biosci. Biotechnol. Biochem. 64: 1722-1725. DOI ScienceOn |
14 | Kim SB, Lee DW, Cheigh CI, Choe EA, Lee SJ, Hong YH, et al. 2006. Purification and characterization of a fibrinolytic subtilisin-like protease of Bacillus subtilis TP-6 from an Indonesian fermented soybean, tempeh. J. Ind. Microbiol. Biotechnol. 33: 436-444. DOI |
15 | Kim W, Choi K, Kim Y, Park H, Choi J, Lee Y, et al. 1996. Purification and characterization of a fibrinolytic enzyme produced from Bacillus sp. strain CK 11-4 screened from chungkook-jang. Appl. Environ. Microbiol. 62: 2482–2488. |
16 | Liu B, Zhang J, Fang Z, Gu L, Liao X, Du G, Chen J. 2013. Enhanced thermostability of keratinase by computational design and empirical mutation. J. Ind. Microbiol. Biotechnol. 40: 697-704. DOI ScienceOn |
17 | Kim YW, Choi JH, Kim JW, Park C, Kim JW, Cha H, et al. 2003. Directed evolution of Thermus maltogenic amylase toward enhanced thermal resistance. Appl. Environ. Microbiol. 69: 4866-4874. DOI |
18 | Martinez R, Jakob F, Tu R, Siegert P, Maurer K-H, Schwaneberg U. 2012. Increasing activity and thermal resistance of Bacillus gibsonii alkaline protease (BgAP) by directed evolution. Biotechnol. Bioeng. 110: 711-720. DOI ScienceOn |
19 | Kwon GH, Lee HA, Park JY, Kim JS, Lim J, Park CS, et al. 2009. Development of a RAPD-PCR method for identification of Bacillus species isolated from cheonggukjang. Int. J. Food Microbiol. 129: 282-287. DOI ScienceOn |
20 | Lee S-Y, Yu S-N, Choi H-J, Kim K-Y, Kim S-H, Choi Y-L, et al. 2013. Cloning and characterization of a thermostable and alkaline fibrinolytic enzyme from a soil metagenome. Afr. J. Biotechnol. 12: 6389-6399. DOI |
21 | McPhalenf CA, James MNG. 1988. Structural comparison of two serine proteinase-protein inhibitor complexes: Eglin-C-Subtilisin Carlsberg and CI-2-Subtilisin Novo. Biochemistry 27: 6582-6598. DOI ScienceOn |
22 | Nakamura T, Yamagata Y, Ichishima E. 1992. Nucleotide sequence of the subtilisin NAT gene, aprN, of Bacillus subtilis (natto). Biosci. Biotechnol. Biochem. 56: 1869-1871. DOI ScienceOn |
23 | Pantoliano MW, Whitlow M, Wood JF, Rollence ML, Finzel BC, Gilliland GL, et al. 1988. The engineering of binding affinity at metal ion binding sites for the stabilization of proteins: subtilisin as a test case. Biochemistry 27: 8311-8317. DOI ScienceOn |
24 | Stephens DE, Singh S, Permaul K. 2009. Error-prone PCR of a fungal xylanase for improvement of its alkaline and thermal stability. FEMS Microbiol. Lett. 293: 42-47. DOI ScienceOn |
25 | Peng Y, Huang Q, Zhang R-H, Zhang Y-Z. 2003. Purification and characterization of a fibrinolytic enzyme produced by Bacillus amyloliquefaciens DC-4 screened from douchi, a traditional Chinese soybean food. Comp. Biochem. Phys. B 134: 45-52. DOI ScienceOn |
26 | Tina KG, Bhadra R, Srinivasan N. 2007. PIC: protein interactions calculator. Nucleic Acids Res. 35: W473-W476. DOI |
27 | Peng Y, Yang XJ, Xiao L, Zhang YZ. 2004. Cloning and expression of a fibrinolytic enzyme (subtilisin DFE) gene from Bacillus amyloliquefaciens DC-4 in Bacillus subtilis. Res. Microbiol. 155: 167-173. DOI ScienceOn |
28 | Schwede T. 2003. SWISS-MODEL: an automated protein homology-modeling server. Nucleic Acids Res. 31: 3381-3385. DOI ScienceOn |
29 | 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: 1110-1111. DOI ScienceOn |
30 | Uehara R, Angkawidjaja C, Koga Y, Kanaya S. 2013. Formation of the high-affinity calcium binding site in prosubtilisin E with the insertion sequence IS1 of Pro-Tk-subtilisin. Biochemistry 52: 9080-9088. DOI ScienceOn |
31 | Wang C, Du M, Zheng D, Kong F, Zu G, Feng Y. 2009. Purification and characterization of nattokinase from Bacillus subtilis Natto B-12. J. Agric. Food Chem. 57: 9722-9729. DOI ScienceOn |
32 | Yeo WS, Seo MJ, Kim MJ, Lee HH, Kang BW, Park JU, et al. 2011. Biochemical analysis of a fibrinolytic enzyme purified from Bacillus subtilis strain A1. J. Microbiol. 49: 376-380. DOI |
33 | Bryan P, Alexander P, Strausberg S, Schwarz F, Lan W, Gilliland G, Gallagher DT. 1992. Energetics of folding subtilisin BPN’. Biochemistry 31: 4937-4945. DOI ScienceOn |
34 | Yin LJ, Lin HH, Jiang ST. 2010. Bioproperties of potent nattokinase from Bacillus subtilis YJ1. J. Agric. Food Chem. 58: 5737-5742. DOI ScienceOn |
35 | Dower WJ, Miller JF, Ragsdale CW. 1988. High efficiency transformation of E. coli by high voltage electroporation. Nucleic Acids Res. 16: 6127-6145. DOI |
36 | Agrebi R, Haddar A, Hmidet N, Jellouli K, Manni L, Nasri M. 2009. BSF1 fibrinolytic enzyme from a marine bacterium Bacillus subtilis A26: purification, biochemical and molecular characterization. Process Biochem. 44: 1252-1259. DOI ScienceOn |
37 | Bradford MM. 1976. A 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 ScienceOn |