Medium optimization for the production of recombinant nattokinase by Bacillus subtilis using response surface methodology

Biotechnology Progress

Volumn 23, Issue 6, 2007, Pages 1327-1332

  Po, Ting Chen ^a,c   Chiang, Chung Jen ^b   Chao, Yun Peng ^a  

^a FENG CHIA UNIVERSITY   (Taiwan)

^b NATIONAL CHUNG HSING UNIVERSITY   (Taiwan)

^c Academia Sinica Biotechnology Center in Southern Taiwan   (Taiwan)

Author keywords

[No Author keywords available]

Indexed keywords

BACILLUS; RECOMBINANT NATTOKINASE;

CARDIOVASCULAR SYSTEM; DISEASES; GENETIC ENGINEERING; HYDROLYSIS; PH EFFECTS; PHOSPHATES;

ENZYME ACTIVITY;

NATTOKINASE; RECOMBINANT PROTEIN; SUBTILISIN; UNCLASSIFIED DRUG;

ARTICLE; BACILLUS SUBTILIS; BIOSYNTHESIS; CULTURE MEDIUM; FERMENTATION; GROWTH, DEVELOPMENT AND AGING; METABOLISM; PH;

BACILLUS SUBTILIS; CULTURE MEDIA; FERMENTATION; HYDROGEN-ION CONCENTRATION; RECOMBINANT PROTEINS; SUBTILISINS;

BACILLUS SUBTILIS; GLYCINE MAX;

EID: 37149052902     PISSN: 87567938     EISSN: None     Source Type: Journal    
DOI: 10.1021/bp070109b     Document Type: Article

References (17)

1. Viles-Gonzalez, J. F.; Fuster, V.; Badimon, J. J. Atherothrombosis: A widespread disease with unpredictable and life-threatening consequences. Eur. Heart J. 2004, 25, 1197-1207.
2. 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, 1110-1111.
3. Fujita, M.; Hong, K.; Ito, Y.; Nishimuro, S. Characterization of nattokinase-degraded products form human fibrinogen or cross-linked fibrin. Fibrinolysis 1995, 9, 157-164.
4. Sumi, H.; Hamada, H.; Nakanishi, K.; Hiratani, H. Enhancement of the fibrinolytic activity in plasma by oral administration of nattokinase. Acta Haematol. 1990, 84, 139-143.
5. Urano, T.; Ihara, H.; Umemura, K.; Suzuki, Y.; Oike, M.; Akita, S.; Tsukamoto, Y.; Suzuki, I.; Takada, A. The Profibrinolytic enzyme subtilisin NAT purified from Bacillus subtilis cleaves and inactivates plasminogen activator inhibitor Type 1. J. Biol. Chem. 2001, 276, 24690-24696.
6. Chen, P. T.; Chao, Y.-P. Enhancement production of recombinant nattokinase in Bacillus subtilis by the elimination of limiting factors. Biotechnol. Lett. 2006, 28, 1595-1600.
7. Chen, P. T.; Chiang, C. J.; Chao, Y.-P. Strategy to approach stable production of recombinant nattokinase in Bacillus subtilis. Biotechnol. Prog. 2007, 23, 808-813.
8. Wu, S.-C.; Wong, S.-L. Development of improved pUB110-based vectors for expression and secretion studies in Bacillus subtilis. J. Biotechnol. 1999, 72, 185-195.
9. Wang, P. Z.; Doi, R. H. Overlapping promoters transcribed by bacillus subtilis sigma 55 and sigma 37 RNA polymerase holoenzymes during growth and stationary phases. J. Biol. Chem. 1984, 259, 8619-8625.
10. Ahuja, S. K.; Ferreira, G. M.; Moreira, A. R. Application of Plackett-Burman design and response surface methodology to achieve exponential growth for aggregated shipworm bacteium. Biotechnol. Bioeng. 2004, 85, 666-675.
11. Plackett, R. L.; Burman, J. P. The design of optimum multifactorial experiments. Biometrika 1946, 33, 305-325.
12. Artemov, A. V.; Samuilov, V. D. Effect of polyelectrolytes on serine proteinase secretion by Bacillus subtilis. FEBS Lett. 1990, 262, 33-35.
13. Stuke, J.; Hillen, W. Regulation of carbon catabolism in Bacillus species. Annu. Rev. Microbiol. 2000, 54, 849-880.
14. Kumar, C. G. Purification and characterization of a themostable alkaline protease from alkalophilic Bacillus pumilus. Lett. Appl. Microbiol. 2002, 34, 13-17.
15. Box, G. E. P.; Behnken, D. W. Some new three level designs for the study of quantitative variables. Technometrics 1960, 2, 455-475.
16. Wu, S.; Me, L.-H.; Yao, S.-J. Optimization of submerged fermentation of nattokinase production by Bacillus subtilis with response surface methodology. Food Ferment. Ind. (Shanghai) 2003, 29, 13-17.
17. Lu, X.; Zhang, R.-H.; Peng, Y.; Shang, Y.-Z. Highly efficient gene expression of a fibrinolytic enzyme (subtilisin DFE) in Bacillus subtilis mediated by the promoter of α-amylase gene from Bacillus amyloliquefaciens. Biotechnol. Lett. 2004, 26, 1365-1369.