References
- Ahmed, S., S. Riaz, and A. Jamil. 2009. Molecular cloning of fungal xylanases: An overview. Appl. Microbiol. Biotechnol. 84: 19-35. https://doi.org/10.1007/s00253-009-2079-4
- Amberg, D., D. Burke, and J. Strathern. 2005. Methods in Yeast Genetics: A Cold Spring Harbor Laboratory Course Manual. Cold Spring Harbor Laboratory Press, NY.
- Bailey, M. J., P. Biely, and K. Poutanen. 1992. Interlaboratory testing of methods for assay of xylanase activity. J. Biotechnol. 23: 257-270. https://doi.org/10.1016/0168-1656(92)90074-J
- Beg, Q. K., M. Kapoor, L. Mahajan, and G. S. Hoondal. 2001. Microbial xylanases and their industrial applications: A review. Appl. Microbiol. Biotechnol. 56: 326-338. https://doi.org/10.1007/s002530100704
- Buchert, J., M. Tenkanen, A. Kantelinen, and L. Viikari. 1994. Application of xylanases in the pulp and paper-industry. Bioresour. Technol. 50: 65-72. https://doi.org/10.1016/0960-8524(94)90222-4
- Bulmer, M. 1991. The selection-mutation-drift theory of synonymous codon usage. Genetics 129: 897-907.
- Clare, J. J., F. B. Rayment, S. P. Ballantine, K. Sreekrishna, and M. A. Romanos. 1991. High-level expression of tetanus toxin fragment C in Pichia pastoris strains containing multiple tandem integrations of the gene. Biotechnology (NY) 9: 455-460. https://doi.org/10.1038/nbt0591-455
- Collins, T., C. Gerday, and G. Feller. 2005. Xylanases, xylanase families and extremophilic xylanases. FEMS Microbiol. Rev. 29: 3-23. https://doi.org/10.1016/j.femsre.2004.06.005
- Coughlan, M. P. and G. P. Hazlewood. 1993. Beta-1,4-D-xylandegrading enzyme systems: Biochemistry, molecular biology and applications. Biotechnol. Appl. Biochem. 17: 259-289.
- Cregg, J. M., J. L. Cereghino, J. Y. Shi, and D. R. Higgins. 2000. Recombinant protein expression in Pichia pastoris. Molec. Biotechnol. 16: 23-52. https://doi.org/10.1385/MB:16:1:23
- Damasceno, L. M., K. A. Anderson, G. Ritter, J. M. Cregg, L. J. Old, and C. A. Batt. 2007. Cooverexpression of chaperones for enhanced secretion of a single-chain antibody fragment in Pichia pastoris. Appl. Microbiol. Biotechnol. 74: 381-389. https://doi.org/10.1007/s00253-006-0652-7
- Flick, K., S. Ahuja, A. Chene, M. T. Bejarano, and Q. Chen. 2004. Optimized expression of Plasmodium falciparum erythrocyte membrane protein 1 domains in Escherichia coli. Malar. J. 3: 50. https://doi.org/10.1186/1475-2875-3-50
- Grantham, R., C. Gautier, M. Gouy, R. Mercier, and A. Pave. 1980. Codon catalog usage and the genome hypothesis. Nucleic Acids Res. 8: r49-r62.
- Griswold, K. E., N. A. Mahmood, B. L. Iverson, and G. Georgiou. 2003. Effects of codon usage versus putative 5'-mRNA structure on the expression of Fusarium solani cutinase in the Escherichia coli cytoplasm. Protein Expr. Purif. 27: 134-142. https://doi.org/10.1016/S1046-5928(02)00578-8
- Harris, G. W., R. W. Pickersgill, I. Connerton, P. Debeire, J. P. Touzel, C. Breton, and S. Perez. 1997. Structural basis of the properties of an industrially relevant thermophilic xylanase. Proteins 29: 77-86. https://doi.org/10.1002/(SICI)1097-0134(199709)29:1<77::AID-PROT6>3.0.CO;2-C
- Henrissat, B. 1991. A classification of glycosyl hydrolases based on amino acid sequence similarities. Biochem. J. 280: 309-316.
- Hershberg, R. and D. A. Petrov. 2008. Selection on codon bias. Annu. Rev. Genet. 42: 287-299. https://doi.org/10.1146/annurev.genet.42.110807.091442
- Hillier, C. J., L. A. Ware, A. Barbosa, E. Angov, J. A. Lyon, D. G. Heppner, and D. E. Lanar. 2005. Process development and analysis of liver-stage antigen 1, a preerythrocyte-stage proteinbased vaccine for Plasmodium falciparum. Infect. Immun. 73: 2109-2115. https://doi.org/10.1128/IAI.73.4.2109-2115.2005
- Inan, M., D. Aryasomayajula, J. Sinha, and M. M. Meagher. 2006. Enhancement of protein secretion in Pichia pastoris by overexpression of protein disulfide isomerase. Biotechnol. Bioeng. 93: 771-778. https://doi.org/10.1002/bit.20762
- Kim, C. H., Y. Oh, and T. H. Lee. 1997. Codon optimization for high-level expression of human erythropoietin (EPO) in mammalian cells. Gene 199: 293-301. https://doi.org/10.1016/S0378-1119(97)00384-3
- Kimchi-Sarfaty, C., J. M. Oh, I. W. Kim, Z. E. Sauna, A. M. Calcagno, S. V. Ambudkar, and M. M. Gottesman. 2007. A "silent" polymorphism in the MDR1 gene changes substrate specificity. Science 315: 525-528. https://doi.org/10.1126/science.1135308
- Kurland, C. and J. Gallant. 1996. Errors of heterologous protein expression. Curr. Opin. Biotechnol. 7: 489-493. https://doi.org/10.1016/S0958-1669(96)80050-4
- Lin-Cereghino, J., M. D. Hashimoto, A. Moy, J. Castelo, C. C. Orazem, P. Kuo, et al. 2008. Direct selection of Pichia pastoris expression strains using new G418 resistance vectors. Yeast 25: 293-299. https://doi.org/10.1002/yea.1587
- Mansur, M., C. Cabello, L. Hernandez, J. Pais, L. Varas, J. Valdes, et al. 2005. Multiple gene copy number enhances insulin precursor secretion in the yeast Pichia pastoris. Biotechnol. Lett. 27: 339-345. https://doi.org/10.1007/s10529-005-1007-7
- Miller, G. L. 1959. Use of dinitrosalicylic acid reagent for determination of reducing sugar. Anal. Chem. 31: 426-428. https://doi.org/10.1021/ac60147a030
- Moriyama, E. N. and J. R. Powell. 1997. Codon usage bias and tRNA abundance in Drosophila. J. Mol. Evol. 45: 514-523. https://doi.org/10.1007/PL00006256
- Nordberg Karlsson, E., E. Bartonek-Roxa, and O. Holst. 1997. Cloning and sequence of a thermostable multidomain xylanase from the bacterium Rhodothermus marinus. Biochim. Biophys. Acta 1353: 118-124. https://doi.org/10.1016/S0167-4781(97)00093-6
- Outchkourov, N. S., W. J. Stiekema, and M. A. Jongsma. 2002. Optimization of the expression of equistatin in Pichia pastoris. Protein Expr. Purif. 24: 18-24. https://doi.org/10.1006/prep.2001.1523
- Parmley, J. L. and L. D. Hurst. 2007. How do synonymous mutations affect fitness? Bioessays 29: 515-519. https://doi.org/10.1002/bies.20592
- Romanos, M. A., J. J. Clare, K. M. Beesley, F. B. Rayment, S. P. Ballantine, A. J. Makoff, G. Dougan, N. F. Fairweather, and I. G. Charles. 1991. Recombinant Bordetella pertussis pertactin (P69) from the yeast Pichia pastoris: High-level production and immunological properties. Vaccine 9: 901-906. https://doi.org/10.1016/0264-410X(91)90011-T
- Sinclair, G. and F. Y. Choy. 2002. Synonymous codon usage bias and the expression of human glucocerebrosidase in the methylotrophic yeast, Pichia pastoris. Protein Expr. Purif. 26: 96-105. https://doi.org/10.1016/S1046-5928(02)00526-0
- Singh, N. D., V. L. B. DuMont, M. J. Hubisz, R. Nielsen, and C. F. Aquadro. 2007. Patterns of mutation and selection at synonymous sites in Drosophila. Molec. Biol. Evol. 24: 2687-2697. https://doi.org/10.1093/molbev/msm196
- Techapun, C., N. Poosaran, M. Watanabe, and K. Sasaki. 2003. Thermostable and alkaline-tolerant microbial cellulase-free xylanases produced from agricultural wastes and the properties required for use in pulp bleaching bioprocesses: A review. Process Biochem. 38: 1327-1340. https://doi.org/10.1016/S0032-9592(02)00331-X
- Torronen, A. and J. Rouvinen. 1995. Structural comparison of two major endo-1,4-xylanases from Trichoderma reesei. Biochemistry 34: 847-856. https://doi.org/10.1021/bi00003a019
- Vassileva, A., D. A. Chugh, S. Swaminathan, and N. Khanna. 2001. Effect of copy number on the expression levels of hepatitis B surface antigen in the methylotrophic yeast Pichia pastoris. Protein Expr. Purif. 21: 71-80. https://doi.org/10.1006/prep.2000.1335
- Walsh, G. A., R. F. Power, and D. R. Headon. 1993. Enzymes in the animal-feed industry. Trends Biotechnol. 11: 424-430. https://doi.org/10.1016/0167-7799(93)90006-U
- Wang, Y. R., H. L. Zhang, Y. Z. He, H. Y. Luo, and B. Yao. 2007. Characterization, gene cloning, and expression of a novel xylanase XYNB from Streptomyces olivaceoviridis A1. Aquaculture 267: 328-334. https://doi.org/10.1016/j.aquaculture.2007.03.005
- Williams, P. E. V. 1997. Poultry production and science: Future directions in nutrition. Worlds Poult. Sci. J. 53: 33-48. https://doi.org/10.1079/WPS19970004
- Woo, J. H., Y. Y. Liu, A. Mathias, S. Stavrou, Z. R. Wang, J. Thompson, and D. M. Neville. 2002. Gene optimization is necessary to express a bivalent anti-human anti-T cell immunotoxin in Pichia pastoris. Protein Expr. Purif. 25: 270-282. https://doi.org/10.1016/S1046-5928(02)00009-8
- Wright, F. 1990. The "effective number of codons" used in a gene. Gene 87: 23-29. https://doi.org/10.1016/0378-1119(90)90491-9
- Yadava, A. and C. F. Ockenhouse. 2003. Effect of codon optimization on expression levels of a functionally folded malaria vaccine candidate in prokaryotic and eukaryotic expression systems. Infect. Immun. 71: 4961-4969. https://doi.org/10.1128/IAI.71.9.4961-4969.2003
- Zhu, T., M. Guo, Z. Tang, M. Zhang, Y. Zhuang, J. Chu, and S. Zhang. 2009. Efficient generation of multi-copy strains for optimizing secretory expression of porcine insulin precursor in yeast Pichia pastoris. J. Appl. Microbiol. 107: 954-963. https://doi.org/10.1111/j.1365-2672.2009.04279.x
Cited by
- Production of α-Cyclodextrin Glycosyltransferase in Bacillus megaterium MS941 by Systematic Codon Usage Optimization vol.60, pp.41, 2012, https://doi.org/10.1021/jf302819h
- Enhanced production of α-cyclodextrin glycosyltransferase in Escherichia coli by systematic codon usage optimization vol.39, pp.12, 2012, https://doi.org/10.1007/s10295-012-1185-y
- Improved Expression and Characterization of a Multidomain Xylanase from Thermoanaerobacterium aotearoense SCUT27 in Bacillus subtilis vol.63, pp.28, 2012, https://doi.org/10.1021/acs.jafc.5b01259