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Construction and Characterization of Novel Chimeric $\\beta$-glucosidases with Cellvibrio gilvus (CG) and Thermotoga maritima (TM) by Overlapping PCR 원문보기

Biotechnology and bioprocess engineering : Bbe, v.14 no.3, 2009년, pp.266 - 273  

Kim, Jong-Deog (Department of Biotechnology, Research Center on Anti-Obesity and Health Care (RCAOHC), Chonnam National University) ,  Seo, Hyo-Jin (Department of Biotechnology, Research Center on Anti-Obesity and Health Care (RCAOHC), Chonnam National University) ,  Kiyoshi, Hayashi (National Food Research Institute)

Abstract AI-Helper 아이콘AI-Helper

In order to create novel $\beta$-glucosidase constructs, 8 kinds of chimeric $\beta$-glucosidases were constructed using overlapping polymerase chain reaction (PCR) based on Celvibrio gilvus (CG) and Thermotoga maritima (TM) genes. Two kinds of novel chimeric $\beta$...

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참고문헌 (28)

  1. Annu. Rev. Microbiol. P. Béguin 44 219 1990 10.1146/annurev.mi.44.100190.001251 Béguin, P. (1990) Molecular biology of cellulose degradation. Annu. Rev. Microbiol. 44: 219-248. 

  2. Appl. Environ. Microbiol. S. Paavilainen 59 927 1993 10.1128/AEM.59.3.927-932.1993 Paavilainen, S., J. Hellman, and T. Korpela (1993) Purification, characterization, gene cloning, and sequencing of a new beta-glucosidase from Bacillus circulans subsp. alkalophilus. Appl. Environ. Microbiol. 59: 927-932. 

  3. 10.1016/0020-711X(82)90109-4 Shewale, J. G. (1982) Beta-Glucosidase: its role in cellulase synthesis and hydrolysis of cellulose. Int. J. Biochem. 435-443. 

  4. J. Biol. Chem. A. Singh 270 21928 1995 10.1074/jbc.270.37.21928 Singh, A. and K. Hayashi (1995) Construction of chimeric β-glucosidases with improved enzymatic properties. J. Biol. Chem. 270: 21928-21935. 

  5. Biotechnol. Adv. B. R. Glick 7 361 1989 10.1016/0734-9750(89)90180-8 Glick, B. R. and J. J. Pasternak (1989) Isolation, characterization, and manipulation of cellulase genes. Biotechnol. Adv. 7: 361-386. 

  6. J. Comp. Physiol. R. Guo 178 209 2008 10.1007/s00360-007-0214-z Guo, R., M. Ding, S. L. Zhang, G. J. Xu, and F. K. Zhao (2008) Molecular cloning and characterization of two novel cellulase genes from the mollusc Ampullaria crossean. J. Comp. Physiol. 178: 209-215. 

  7. Biochem. Biophys. Res. Commun. P. Roy 336 299 2005 10.1016/j.bbrc.2005.08.067 Roy, P., S. Mishra, and T. K. Chaudhuri (2005) Cloning, sequence analysis, and characterization of a novel beta-glucosidase-like activity from Pichia etchellsii. Biochem. Biophys. Res. Commun. 336: 299-308. 

  8. Biotechnol. Bioprocess Eng. Y. M. Kim 13 40 2008 10.1007/s12257-007-0162-1 Kim, Y. M., S. H. Jung, Y. H. Chung, C. B. Yu, and I. K. Rhee (2008) Cloning and characterization of a cyclohexanone monooxygenase gene from Arthrobacter sp. L661. Biotechnol. Bioprocess Eng. 13: 40-47. 

  9. Adv. Appl. Microbiol. A. Singh 40 38 1995 Singh, A. and K. Hayashi (1995) Microbial celluoases, protein architecture, molecuar properties, and biosynthesis. Adv. Appl. Microbiol. 40: 38-44. 

  10. World J. Gastroenterol. A. L. Tao 10 2103 2004 10.3748/wjg.v10.i14.2103 Tao, A. L. and S. H. He (2004) Bridging PCR and partially overlapping primers for novel allergen gene cloning and expression insert decoration. World J. Gastroenterol. 10: 2103-2108. 

  11. Nature A. Crameri 391 288 1998 10.1038/34663 Crameri, A., S. A. Raillard, E. Bermudez, and W. P. Stemmer (1998) DNA shuffling of a family of genes from diverse species accelerates directed evolution. Nature 391: 288-291. 

  12. Biochim. Biophys. Acta. M. Lehmann 1543 408 2000 10.1016/S0167-4838(00)00238-7 Lehmann, M., L. Pasamontes, S. F. Lassen, and M. Wyss (2000) The consensus concept for thermostability engineering of proteins. Biochim. Biophys. Acta. 1543: 408-415. 

  13. Ind. J. Biochem. Biophys. S. P. Singh 39 235 2002 Singh, S. P., J. D. Kim, S. Machida, and K. Hayashi (2002) Overexpression and protein folding of a chimeric β-glucosidase constructed from Agrobacterium tumefaciens and Cellvibrio gilvus. Ind. J. Biochem. Biophys. 39: 235-239. 

  14. J. Am. Coll. Cardiol. O. Lisy 52 60 2008 10.1016/j.jacc.2008.02.077 Lisy, O., B. K. Huntley, D. J. McCormick, P. A. Kurlansky, and J. C. Burnett Jr. (2008) Design, synthesis, and actions of a novel chimeric natriuretic peptide: CDNP. J. Am. Coll. Cardiol. 52: 60-68. 

  15. Biochem. J. H. Shibuya 349 651 2000 10.1042/bj3490651 Shibuya, H., S. Kaneko, and K. Hayashi (2000) Enhancement of the thermostability and hydrolytic activity of xylanase by random gene shuffling. Biochem. J. 349: 651-656. 

  16. Biochem. J. A. Singh 305 715 1955 10.1042/bj3050715 Singh, A., K. Hayashi, T. T. HOA, Y. Kashiwagi, and K. Tokuyasu (1955) Construction and characterization of chimeric β-glucosidase. Biochem. J. 305: 715-719. 

  17. J. Gen. Microbiol. K. M. Bhat 139 2825 1993 10.1099/00221287-139-11-2825 Bhat, K. M., J. S. Gaikwad, and R. Maheshwari (1993) Purification and characterization of an extracellular β-glucosidase from thermophiic fungus S.thermophile and its influence on cellulae activity. J. Gen. Microbiol. 139: 2825-2832. 

  18. J. Biochem. S. D’Auria 126 545 1999 10.1093/oxfordjournals.jbchem.a022484 D’Auria, S., R. Nucci, M. Rossi, E. Bertoli, F. Tanfani, I. Gryczynski, H. Malak, and J. R. Lakowicz (1999) β-glucosidase from the hyperthermophilic Archaeon Sulfoobus Solfataricus: structure and activity in presence of alcohols. J. Biochem. 126: 545-552. 

  19. Appl. Environ. Microbiol. M. Lorenzo Di 71 8974 2005 10.1128/AEM.71.12.8974-8977.2005 Di Lorenzo, M., A. Hidalgo, M. Haas, and U. T. Bornscheuer (2005) Heterologous production of functional forms of Rhizopus oryzae lipase in Escherichia coli. Appl. Environ. Microbiol. 71: 8974-8977. 

  20. Biotechnol. Lett. M. E. Gasparian 29 1567 2007 10.1007/s10529-007-9446-y Gasparian, M. E., V. G. Ostapchenko, A. V. Yagolovich, I. N. Tsygannik, B. V. Chernyak, D. A. Dolgikh, and M. P. Kirpichnikov (2007) Overexpression and refolding of thioredoxin/TRAIL fusion from inclusion bodies and further purification of TRAIL after cleavage by enteropeptidase. Biotechnol. Lett. 29: 1567-1573. 

  21. J. Bacteriol. W. W. Wakarchuk 170 301 1988 10.1128/jb.170.1.301-307.1988 Wakarchuk, W. W., N. M. Greenberg, D. G. Kilburn, R. C. Miller Jr, and R. A. Warren (1988) Structure and transcription analysis of the gene encoding a cellobiase from Agrobacterium sp. strain ATCC 21400. J. Bacteriol. 170: 301-307. 

  22. J. Biochem. J. Iwahashi 111 451 1992 10.1093/oxfordjournals.jbchem.a123778 Iwahashi, J., S. Furuya, K. Mihara, and T. Omura (1992) Characterization of adrenodoxin precursor expressed in Escherichia coli. J. Biochem. 111: 451-455. 

  23. Biochemistry N. M. Parakhnevitch 70 777 2005 Parakhnevitch, N. M., A. A. Malygin, and G. G. Karpova (2005) Recombinant human ribosomal protein S16: expression, purification, refolding, and structural stability. Biochemistry 70: 777-781. 

  24. Biotechniques S. H. Pan 29 1234 2000 10.2144/00296st03 Pan, S. H. and B. A. Malcolm (2000) Reduced background expression and improved plasmid stability with pET vectors in BL21 (DE3). Biotechniques 29: 1234-1238. 

  25. Nature W. P. Stemmer 370 389 1994 10.1038/370389a0 Stemmer, W. P. (1994) Rapid evolution of a protein in vitro by DNA shuffling. Nature 370: 389-391. 

  26. FEMS Microbiol. Lett. S. Machida 159 41 1998 Machida, S., Y. YU, S. P. Singh, J. D. Kim, K. Hayashi, and Y. Kawata (1998) Overproduction of β-glucosidase as active form by Eschericha coli system coexpressing the chaperonin GroELS at 25. FEMS Microbiol. Lett. 159: 41-46. 

  27. Protein Expr. Purif. X. Wang 56 27 2007 10.1016/j.pep.2007.05.011 Wang, X., M. Fu, J. Ren, and X. Qu (2007) Evaluation of different culture conditions for high-level soluble expression of human cyclin A2 with pET vector in BL21 (DE3) and spectroscopic characterization of its inclusion body structure. Protein Expr. Purif. 56: 27-34. 

  28. Biotechnol. Bioprocess Eng. T. S. Lien 12 610 2007 10.1007/BF02931076 Lien, T. S., S. T. Yu, S. T. Wu, and J. R. Too (2007) Induction and purification of a thermophilic chitinase produced by Aeromonas sp. DYU-Too7 using glucosamine. Biotechnol. Bioprocess Eng. 12: 610-617. 

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