References
- F. Clementi, Crit. Rev. Biotechnol. 17 (1997) 327. https://doi.org/10.3109/07388559709146618
- W. Hashimoto, O. Miyake, A. Ochia, K. Murata, J. Biosci. Bioeng. 99 (2005) 48. https://doi.org/10.1263/jbb.99.48
- T.Y. Wong, L.A. Preston, N.L. Schiller, Annu. Rev. Microbiol. 54 (2000) 289. https://doi.org/10.1146/annurev.micro.54.1.289
- P. Michaud, A. Da Costa, B. Courtois, J. Courtois, Crit. Rev. Biotechnol. 23 (2003) 233. https://doi.org/10.1080/07388550390447043
- Z. Zhang, G. Yu, H. Guan, X. Zhao, Y. Du, X. Jiang, Carbohydr. Res. 339 (2004) 1475. https://doi.org/10.1016/j.carres.2004.03.010
- J. Courtois, Curr. Opin. Microbiol. 12 (2009) 261. https://doi.org/10.1016/j.mib.2009.04.007
- K. Iwasaki, Y. Matsubara, Biosci. Biotechnol. Biochem. 64 (2000) 1067. https://doi.org/10.1271/bbb.64.1067
- M. Kurachi, T. Nakashima, C. Miyajima, Y. Iwamoto, T. Muramatsu, K. Yamaguchi, T. Oda, J. Infect. Chemother. 11 (2005) 199. https://doi.org/10.1007/s10156-005-0392-0
- N.Q. Hien, N. Nagasawa, L.X. Tham, F. Yoshii, V.H. Dang, H. Mitomo, K. Makuuchi, T. Kume, Radiat. Phys. Chem. 59 (2000) 97. https://doi.org/10.1016/S0969-806X(99)00522-8
- M. Iwamoto, M. Kurachi, T. Nakashima, D. Kim, K. Yamaguch, T. Oda, Y. Iwamoto, T. Muramatsu, FEBS Lett. 579 (2005) 4423. https://doi.org/10.1016/j.febslet.2005.07.007
- A. Kawada, N. Hiura, S. Tajima, H. Takahara, Arch. Dermatol. Res. 291 (1999) 542. https://doi.org/10.1007/s004030050451
- Y. Wang, F. Han, B. Hu, J. Li, W. Yu, Nutr. Res. 26 (2006) 597. https://doi.org/10.1016/j.nutres.2006.09.015
- M.A. Alkawash, J.S. Soothill, N.L. Schiller, APMIS 114 (2006) 131. https://doi.org/10.1111/j.1600-0463.2006.apm_356.x
- A. Boyd, A.M. Chakrabarty, Appl. Environ. Microbiol. 60 (1994) 2355.
- D.E. Kim, E.Y. Lee, H.S. Kim, Mar. Biotechnol. 11 (2009) 10. https://doi.org/10.1007/s10126-008-9114-9
- W. Hashimoto, O. Miyake, K. Momma, S. Kawai, K. Murata, J. Bacteriol. 182 (2000) 4572. https://doi.org/10.1128/JB.182.16.4572-4577.2000
- M. Iwamoto, R. Araki, K. Iriyama, T. Oda, H. Fukuda, S. Hayashida, T. Muramatsu, Biosci. Biotechnol. Biochem. 65 (2001) 133. https://doi.org/10.1271/bbb.65.133
- O. Miyake, W. Hashimoto, K. Murata, Protein Expr. Purif. 29 (2003) 33. https://doi.org/10.1016/S1046-5928(03)00018-4
- A. Ochiai, W. Hashimoto, K. Murata, Res. Microbiol. 157 (2006) 642. https://doi.org/10.1016/j.resmic.2006.02.006
- Y. Chisti, Trends Biotechnol. 26 (2008) 126. https://doi.org/10.1016/j.tibtech.2007.12.002
- P.T. Vasudevan, M. Briggs, J. Ind. Microbiol. Biotechnol. 35 (2008) 421. https://doi.org/10.1007/s10295-008-0312-2
- J.W. Shin, S.H. Choi, D.E. Kim, H.S. Kim, J.W. Lee, I.S. Lee, E.Y. Lee, Biopro. Biosys. Eng. 34 (2011) 113. https://doi.org/10.1007/s00449-010-0452-4
- H.H. Park, N. Kam, E.Y. Lee, H.S. Kim, Mar. Biotechnol. (2011), doi:10.1007/s10126-011-9402-7.
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