Synthesis and characterization of chimeric proteins based on cellulase and xylanase from an insect gut bacterium

Applied and Environmental Microbiology

Volumn 77, Issue 14, 2011, Pages 4859-4866

  Adlakha, Nidhi ^a   Rajagopa, Raman ^a,b   Kumar, Saravanan ^a   Reddy, Vanga Siva ^a   Yazdani, Syed Shams ^a  

^a INTERNATIONAL CENTRE FOR GENETIC ENGINEERING AND BIOTECHNOLOGY ICGEB   (India)

^b UNIVERSITY OF DELHI   (India)

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL FLORA; BIFUNCTIONAL; BIFUNCTIONAL ENZYMES; CHIMERIC PROTEINS; ENCODING GENES; END TO END; GUT BACTERIA; NATIVE ENZYMES; OPTIMAL ACTIVITY; PLANT BIOMASS; SECONDARY STRUCTURES; SPECIFIC ACTIVITY; SUBSTRATE RANGE; THREE-DIMENSIONAL STRUCTURE; XYLANASES;

AMINO ACIDS; BIOMASS; BIOSYNTHESIS; CATALYSTS; CIRCULAR DICHROISM SPECTROSCOPY; CLONING; DICHROISM; ENCODING (SYMBOLS); ESCHERICHIA COLI; GENE ENCODING; HYDROLYSIS; THREE DIMENSIONAL;

ENZYME ACTIVITY;

BACTERIAL PROTEIN; CELLULASE; ENDO 1,4 BETA XYLANASE; HYBRID PROTEIN;

BACTERIUM; BIODEGRADATION; CELLULOSE; CLONE; ENZYME ACTIVITY; GENE EXPRESSION; HYDROLYSIS; MOTH; PH; PHYTOMASS; PROTEIN; RECOMBINATION; SECRETION; SPECTROSCOPY; SUBSTRATE; TEMPERATURE EFFECT;

ANIMAL; ARTICLE; BIOSYNTHESIS; CHEMISTRY; CIRCULAR DICHROISM; ESCHERICHIA COLI; GASTROINTESTINAL TRACT; GENETICS; ISOLATION AND PURIFICATION; LEPIDOPTERA; METABOLISM; MICROBIOLOGY; MOLECULAR GENETICS; NUCLEOTIDE SEQUENCE; PAENIBACILLUS;

ANIMALS; BACTERIAL PROTEINS; CELLULASE; CIRCULAR DICHROISM; ENDO-1,4-BETA XYLANASES; ESCHERICHIA COLI; GASTROINTESTINAL TRACT; LEPIDOPTERA; MOLECULAR SEQUENCE DATA; PAENIBACILLUS; RECOMBINANT FUSION PROTEINS;

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI; GOSSYPIUM HIRSUTUM; HELICOVERPA ARMIGERA; HEXAPODA; PAENIBACILLUS;

EID: 79961063240     PISSN: 00992240     EISSN: 10985336     Source Type: Journal    
DOI: 10.1128/AEM.02808-10     Document Type: Article

References (37)

1. An, J. M., et al. 2005. Evaluation of a novel bifunctional xylanase-cellulase constructed by gene fusion. Enzyme Microb. Technol. 36:989-995.
2. Beliën, T., S. Van Campenhout, J. Robben, and G. Volckaert. 2006. Microbial endoxylanases: effective weapons to breach the plant cell-wall barrier or, rather, triggers of plant defense systems? Mol. Plant Microbe Interact. 19: 1072-1081.
3. Berg Miller, M. E., et al. 2009. Diversity and strain specificity of plant cell wall degrading enzymes revealed by the draft genome of Ruminococcus flavefaciens FD-1. PLoS One 4:e6650.
4. Cho, K. M., et al. 2008. Cloning of two cellulase genes from endophytic Paenibacillus polymyxa GS01 and comparison with cel 44C-man 26A. J. Basic Microbiol. 48:464-472.
5. Dashtban, M., M. Maki, K. T. Leung, C. Mao, and W. Qin. 2010. Cellulase activities in biomass conversion: measurement methods and comparison. Crit. Rev. Biotechnol. 30:302-309.
6. de Vries, R. P., and J. Visser. 2001. Aspergillus enzymes involved in degradation of plant cell wall polysaccharides. Microbiol. Mol. Biol. Rev. 65:497-522.
7. Fan, Z., J. R. Werkman, and L. Yuan. 2009. Engineering of a multifunctional hemicellulase. Biotechnol. Lett. 31:751-757.
8. Flint, H. J., E. A. Bayer, M. T. Rincon, R. Lamed, and B. A. White. 2008. Polysaccharide utilization by gut bacteria: potential for new insights from genomic analysis. Nat. Rev. Microbiol. 6:121-131.
9. Flint, H. J., J. Martin, C. A. McPherson, A. S. Daniel, and J. X. Zhang. 1993. A bifunctional enzyme, with separate xylanase and beta(1,3-1,4)-glucanase domains, encoded by the xynD gene of Ruminococcus flavefaciens. J. Bacteriol. 175:2943-2951.
10. Gilbert, H. J., and G. Hazlewood. 1993. Bacterial cellulases and xylanases. J. Gen. Microbiol. 139:187-194.
11. Han, S. J., Y. J. Yoo, and H. S. Kang. 1995. Characterization of a bifunctional cellulase and its structural gene. J. Biol. Chem. 270:26012-26019.
12. Heinzelman, P., et al. 2009. A family of thermostable fungal cellulases created by structure-guided recombination. Proc. Natl. Acad. Sci. U. S. A. 106:5610-5615.
13. Hong, S. Y., et al. 2006. Assembling a novel bifunctional cellulase-xylanase from Thermotoga maritima by end-to-end fusion. Biotechnol. Lett. 28:1857-1862.
14. Hongoh, Y., et al. 2008. Complete genome of the uncultured Termite Group 1 bacteria in a single host protist cell. Proc. Natl. Acad. Sci. U. S. A. 105:5555-5560.
15. Hwang, I. T., et al. 2010. Cloning and characterization of a xylanase, KRICT PX1 from the strain Paenibacillus sp. HPL-001. Biotechnol. Adv. 28:594-601.
16. Kataeva, I. A., et al. 2009. Genome sequence of the anaerobic, thermophilic, and cellulolytic bacterium "Anaerocellum thermophilum" DSM 6725. J. Bacteriol. 191:3760-3761.
17. Lee, H. J., et al. 2000. Cloning, expression and nucleotide sequences of two xylanase genes from Paenibacillus sp. Biotechnol. Lett. 22:387-392.
18. Li, W., W. W. Zhang, M. M. Yang, and Y. L. Chen. 2008. Cloning of the thermostable cellulase gene from newly isolated Bacillus subtilis and its expression in Escherichia coli. Mol. Biotechnol. 40:195-201.
19. Lu, P., and M. G. Feng. 2008. Bifunctional enhancement of a beta-glucanasexylanase fusion enzyme by optimization of peptide linkers. Appl. Microbiol. Biotechnol. 79:579-587.
20. Lynd, L. R., et al. 2008. How biotech can transform biofuels. Nat. Biotechnol. 26:169-172.
21. Maki, M., K. T. Leung, and W. Qin. 2009. The prospects of cellulaseproducing bacteria for the bioconversion of lignocellulosic biomass. Int. J. Biol. Sci. 5:500-516.
22. Margeot, A., B. Hahn-Hagerdal, M. Edlund, R. Slade, and F. Monot. 2009. New improvements for lignocellulosic ethanol. Curr. Opin. Biotechnol. 20: 372-380.
23. Martinez, D., et al. 2008. Genome sequencing and analysis of the biomassdegrading fungus Trichoderma reesei (syn. Hypocrea jecorina). Nat. Biotechnol. 26:553-560.
24. Morelle, W., and J. C. Michalski. 2007. Analysis of protein glycosylation by mass spectrometry. Nat. Protoc. 2:1585-1602.
25. Niku-Paavola, M.-L., A. Lappalainen, T.-M. Enari, and M. Nummi. 1985. A new appraisal of the endoglucanases of the fungus Trichoderma reesei. Biochem. J. 231:75-81.
26. Onsori, H., M. R. Zamani, M. Motallebi, and N. Zarghami. 2005. Identification of over producer strain of endo-b-1,4-glucanase in Aspergillus species: characterization of crude carboxymethyl cellulase. Afr. J. Biotechnol. 4:26-30.
27. Park, D. S., et al. 2009. Paenibacillus pectinilyticus sp. nov., isolated from the gut of Diestrammena apicalis. Int. J. Syst. Evol. Microbiol. 59:1342-1347.
28. Park, J.-N., et al. 2001. Cloning of a Paenibacillus sp. endo-β-1,4-glucanase gene and its coexpression with the Endomyces fibuliger β-glucosidase gene in Saccharomyces cerevisiae. J. Microbiol. Biotechnol. 11:685-692.
29. Pérez-Avalos, O., L. M. Sánchez-Herrera, L. M. Salgado, and T. Ponce-Noyola. 2008. A bifunctional endoglucanase/endoxylanase from Cellulomonas flavigena with potential use in industrial processes at different pH. Curr. Microbiol. 57:39-44.
30. Qin, Y., X. Wei, X. Song, and Y. Qu. 2008. Engineering endoglucanase II from Trichoderma reesei to improve the catalytic efficiency at a higher pH optimum. J. Biotechnol. 135:190-195.
31. Raussens, V., J. M. Ruysschaert, and E. Goormaghtigh. 2003. Protein concentration is not an absolute prerequisite for the determination of secondary structure from circular dichroism spectra: a new scaling method. Anal. Biochem. 319:114-121.
32. Sánchez, C. 2009. Lignocellulosic residues: biodegradation and bioconversion by fungi. Biotechnol. Adv. 27:185-194.
33. Schäfer, A., et al. 1996. Hemicellulose-degrading bacteria and yeasts from the termite gut. J. Appl. Bacteriol. 80:471-478.
34. Stephanopoulos, G. 2007. Challenges in engineering microbes for biofuels production. Science 315:801-804.
35. Warnecke, F., et al. 2007. Metagenomic and functional analysis of hindgut microbiota of a wood-feeding higher termite. Nature 450:560-565.
36. Wenzel, M., I. Schönig, M. Berchtold, P. Kämpfer, and H. König. 2002. Aerobic and facultatively anaerobic cellulolytic bacteria from the gut of the termite Zootermopsis angusticollis. J. Appl. Microbiol. 92:32-40.
37. Zhang, Y. 2008. I-TASSER server for protein 3D structure prediction. BMC Bioinformatics 9:40.