Enhancement of the thermostability and activity of mesophilic Clostridium cellulovorans EngD by in vitro DNA recombination with Clostridium thermocellum CelE

Journal of Bioscience and Bioengineering

Volumn 109, Issue 4, 2010, Pages 331-336

  Lee, Chae Yoeng ^a   Yu, Kyung Ok ^a   Kim, Seung Wook ^a   Han, Sung Ok ^a  

^a Korea University   (South Korea)

Author keywords

Cellulase; Clostridium cellulovorans; Clostridium thermocellum; in vitro DNA recombination; Thermostability

Indexed keywords

AMINO ACID SUBSTITUTION; CATALYTIC ACTIVITY; CHARGED RESIDUES; CLOSTRIDIUM CELLULOVORANS; CLOSTRIDIUM THERMOCELLUM; DNA RECOMBINATION; ENDOGLUCANASES; ENZYMATIC ACTIVITIES; IN-VITRO; MESOPHILIC; MOLECULAR ENGINEERING; MUTANT LIBRARIES; RELATIVE ACTIVITIES; SITE DIRECTED MUTAGENESIS; THERMAL STABILITY;

AMINO ACIDS; CLONING; DNA; ENZYME ACTIVITY; GENES; ORGANIC ACIDS;

CLOSTRIDIUM;

GLUCAN SYNTHASE;

AMINO ACID SUBSTITUTION; ARTICLE; BACTERIAL GENE; BIOENGINEERING; CATALYSIS; CELE GENE; CLOSTRIDIUM CELLULOVORANS; CLOSTRIDIUM THERMOCELLUM; CONTROLLED STUDY; CRYSTAL STRUCTURE; DNA RECOMBINATION; DNA SEQUENCE; ENZYME ACTIVITY; HUMAN; IN VITRO STUDY; MESOPHILIC BACTERIUM; NONHUMAN; NUCLEOTIDE SEQUENCE; SITE DIRECTED MUTAGENESIS; TEMPERATURE DEPENDENCE; THERMOSTABILITY;

AMINO ACID SUBSTITUTION; BASE SEQUENCE; CELLULASES; CLOSTRIDIUM CELLULOVORANS; CLOSTRIDIUM THERMOCELLUM; DIRECTED MOLECULAR EVOLUTION; DNA PRIMERS; DNA, BACTERIAL; ENZYME STABILITY; KINETICS; MODELS, MOLECULAR; MUTAGENESIS, SITE-DIRECTED; RECOMBINANT PROTEINS;

CLOSTRIDIUM CELLULOVORANS; CLOSTRIDIUM THERMOCELLUM;

EID: 77649243409     PISSN: 13891723     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jbiosc.2009.10.014     Document Type: Article

References (43)

1. Nakazawa H., Okada K., Onodera T., Ogasawara W., Okada H., and Morikawa Y. Directed evolution of endoglucanase III (Cel12A) from Trichoderma reesei. Appl. Microbiol. Biotechnol. 83 (2009) 649-657
2. Han S.O., Yukawa H., Inui M., and Doi R.H. Regulation of expression of cellulosomal cellulase and hemicellulase genes in Clostridium cellulovorans. J. Bacteriol. 185 (2003) 6067-6075
3. Wonganu B., Pootanakit K., Boonyapakron K., Champreda V., Tanapongpipat S., and Eurwilaichitr L. Cloning, expression and characterization of a thermotolerant endoglucanase from Syncephalastrum racemosum (BCC18080) in Pichia pastoris. Protein Expr. Purif. 58 (2008) 78-86
4. Lin L., Meng X., Liu P., Hong Y., Wu G., Huang X., Li C., Dong J., Xiao L., and Liu Z. Improved catalytic efficiency of endo-beta-1,4-glucanase from Bacillus subtilis BME-15 by directed evolution. Appl. Microbiol. Biotechnol. 82 (2009) 671-679
5. Hong J., Wang Y., Kumagai H., and Tamaki H. Construction of thermotolerant yeast expressing thermostable cellulase genes. J. Biotechnol. 130 (2007) 114-123
6. Song J.K., and Rhee J.S. Simultaneous enhancement of thermostability and catalytic activity of phospholipase A(1) by evolutionary molecular engineering. Appl. Environ. Microbiol. 66 (2000) 890-894
7. Zhao H., Giver L., Shao Z., Affholter J.A., and Arnold F.H. Molecular evolution by staggered extension process (StEP) in vitro recombination. Nat. Biotechnol. 16 (1998) 258-261
8. Eijsink V.G.H., Gaseidnes S., Borchert T.V., and van den Burg B. Directed evolution of enzyme stability. Biomol. Eng. 22 (2005) 21-30
9. Lehmann M., and Wyss M. Engineering proteins for thermostability: the use of sequence alignments versus rational design and directed evolution. Curr. Opin. Biotechnol. 12 (2001) 371-375
10. van der Veen B.A., Skov L.K., Potocki-Veronese G., Gajhede M., Monsan P., and Remaud-Simeon M. Increased amylosucrase activity and specificity, and identification of regions important for activity, specificity and stability through molecular evolution. FEBS J. 273 (2006) 673-681
11. Emond S., Andre I., Jaziri K., Potocki-Veronese G., Mondon P., Bouayadi K., Kharrat H., Monsan P., and Remaud-Simeon M. Combinatorial engineering to enhance thermostability of amylosucrase. Prot. Sci. 17 (2008) 967-976
12. Zhao H., and Zha W. In vitro 'sexual' evolution through the PCR-based staggered extension process (StEP). Nat. Protoc. 1 (2006) 1865-1871
13. Doi R.H., Kosugi A., Murashima K., Tamaru Y., and Han S.O. Cellulosomes from mesophilic bacteria. J. Bacteriol. 185 (2003) 5907-5914
14. Cho H.Y., Yukawa H., Inui M., Doi R.H., and Wong S.L. Production of minicellulosomes from Clostridium cellulovorans in Bacillus subtilis WB800. Appl. Environ. Microbiol. 70 (2004) 5704-5707
15. Lamed R., Setter E., and Bayer E.A. Characterization of a cellulose-binding, cellulase-containing complex in Clostridium thermocellum. J. Bacteriol. 156 (1983) 828-836
16. Newcomb M., Chen C.Y., and Wu J.H. Induction of the celC operon of Clostridium thermocellum by laminaribiose. Proc. Natl. Acad. Sci. U. S. A. 104 (2007) 3747-3752
17. Aguinaldo A.M., and Arnold F.H. Staggered extension process (StEP) in vitro recombination. Methods Mol. Biol. 231 (2003) 105-110
18. Murashima K., Kosugi A., and Doi R.H. Thermostabilization of cellulosomal endoglucanase EngB from Clostridium cellulovorans by in vitro DNA recombination with non-cellulosomal endoglucanase EngD. Mol. Microbiol. 45 (2002) 617-626
19. Pogulis R.J., Vallejo A.N., and Pease L.R. In vitro recombination and mutagenesis by overlap extension PCR. Methods Mol. Biol. 57 (1996) 167-176
20. Thierry W., Fabrice L., and Petrus J.P. A modified overlap extension PCR method to create chimeric genes in the absence of restriction enzymes. Biotechnol. Tech. 12 (1998) 653-657
21. Xiao Z., Wang P., Qu Y., Gao P., and Wang T. Cold adaptation of a mesophilic cellulase, EG III from Trichoderma reesei, by directed evolution. Sci. China C. Life Sci. 45 (2002) 337-343
22. Hakamada Y., Koike K., Yoshimatsu T., Mori H., Kobayashi T., and Ito S. Thermostable alkaline cellulase from an alkaliphilic isolate, Bacillus sp. KSM-S237. Extremophiles 1 (1997) 151-156
23. Kim M.S., and Lei X.G. Enhancing thermostability of Escherichia coli phytase AppA2 by error-prone PCR. Appl. Microbiol. Biotechnol. 79 (2008) 69-75
24. Leemhuis H., Nightingale K.P., and Hollfelder F. Directed evolution of a histone acetyltransferase-enhancing thermostability, whilst maintaining catalytic activity and substrate specificity. FEBS J. 275 (2008) 5635-5647
25. Cherry J.R., Lamsa M.H., Schneider P., Vind J., Svendsen A., Jones A., and Pedersen A.H. Directed evolution of a fungal peroxidase. Nat. Biotechnol. 17 (1999) 379-384
26. Shao Z., Zhao H., Giver L., and Arnold F.H. Random-priming in vitro recombination: an effective tool for directed evolution. Nucleic Acids. Res. 26 (1998) 681-683
27. Volkov A.A., Shao Z., and Arnold F.H. Recombination and chimeragenesis by in vitro heteroduplex formation and in vivo repair. Nucleic Acids. Res. e18 (1999) 27
28. Crameri A., Raillard S.A., Bermudez E., and Stemmer W.P. DNA shuffling of a family of genes from diverse species accelerates directed evolution. Nature 391 (1998) 288-291
29. Chan M.K., Mukund S., Kletzin A., Adams M.W., and Rees D.C. Structure of a hyperthermophilic tungstopterin enzyme, aldehyde ferredoxin oxidoreductase. Science 267 (1995) 1463-1469
30. Hurley J.H., Baase W.A., and Matthews B.W. Design and structural analysis of alternative hydrophobic core packing arrangements in bacteriophage T4 lysozyme. J. Mol. Biol. 224 (1992) 1143-1159
31. Anderson D.E., Hurley J.H., Nicholson H., Baase W.A., and Matthews B.W. Hydrophobic core repacking and aromatic-aromatic interaction in the thermostable mutant of T4 lysozyme Ser 117→Phe. Protein Sci. 2 (1993) 1285-1290
32. Tanner J.J., Hecht R.M., and Krause K.L. Determinants of enzyme thermostability observed in the molecular structure of Thermus aquaticus d-glyceraldehyde-3-phosphate dehydrogenase at 25 Angstroms resolution. Biochemistry 35 (1996) 2597-2609
33. Korolev S., Nayal M., Barnes W.M., Di Cera E., and Waksman G. Crystal structure of the large fragment of Thermus aquaticus DNA polymerase I at 2.5-A resolution: structural basis for thermostability. Proc. Natl. Acad. Sci. U.S.A. 92 (1995) 9264-9268
34. Bhuiya M.W., Sakuraba H., Ohshima T., Imagawa T., Katunuma N., and Tsuge H. The first crystal structure of hyperthermostable NAD-dependent glutamate dehydrogenase from Pyrobaculum islandicum. J. Mol. Biol. 345 (2005) 325-337
35. Karlstrom M., Stokke R., Steen I.H., Birkeland N.K., and Ladenstein R. Isocitrate dehydrogenase from the hyperthermophile Aeropyrum pernix: X-ray structure analysis of a ternary enzyme-substrate complex and thermal stability. J. Mol. Biol. 345 (2005) 559-577
36. Karshikoff A., and Ladenstein R. Ion pairs and the thermotolerance of proteins from hyperthermophiles: a "traffic rule" for hot roads. Trends Biochem. Sci. 26 (2001) 550-556
37. Pakula A.A., and Sauer R.T. Reverse hydrophobic effects relieved by amino-acid substitutions at a protein surface. Nature 344 (1990) 363-364
38. Sweet R.M., and Eisenberg D. Correlation of sequence hydrophobicities measures similarity in three-dimensional protein structure. J. Mol. Biol. 171 (1983) 479-488
39. Wu L.C., Lee J.X., Huang H.D., Liu B.J., and Horng J.T. An expert system to predict protein thermostability using decision tree. Expert Syst. Appl. 36 (2009) 9007-9014
40. Stephens D.E., Singh S., and Permaul K. Error-prone PCR of a fungal xylanase for improvement of its alkaline and thermal stability. FEMS Microbiol. Lett. 293 (2009) 42-47
41. Kunugi S., Fujiwara S., Kidokoro S., Endo K., and Hanzawa S. Single-point amino acid substitutions at the 119th residue of thermolysin and their pressure-induced activation. FEBS Lett. 462 (1999) 231-235
42. Marx C.K., Hertel T.C., and Pietzsch M. Random mutagenesis of a recombinant microbial transglutaminase for the generation of thermostable and heat-sensitive variants. J. Biotechnol. 136 (2008) 156-162
43. Kaper T., Brouns S.J., Geerling A.C., De Vos W.M., and Van der Oost J. DNA family shuffling of hyperthermostable beta-glycosidases. Biochem. J. 368 (2002) 461-470