Transgenic soybean seed as protein expression system: Aqueous extraction of recombinant β-glucuronidase

Applied Biochemistry and Biotechnology

Volumn 160, Issue 4, 2010, Pages 1157-1167

  Robić, Goran ^a   Farinas, Cristiane S ^b   Rech, Elíbio L ^c   Miranda, Everson A ^a  

^a UNIVERSITY OF CAMPINAS   (Brazil)

^b EMBRAPA CERRADOS   (Brazil)

^c EMBRAPA RECURSOS GENÉTICOS E BIOTECNOLOGIA   (Brazil)

Author keywords

Downstream processing; Extraction; Recombinant protein; Soyben seed; Transgenic plants

Indexed keywords

BIOCONVERSION; BIOREACTORS; EXTRACTION; IONIC STRENGTH; PLANTS (BOTANY); SEED;

AQUEOUS EXTRACTION; BETA-GLUCURONIDASE; DOWNSTREAM-PROCESSING; ENGINEERING STANDPOINT; INFLUENCE OF PH; PROTEIN EXPRESSION SYSTEMS; TRANSGENIC PLANTS; TRANSGENIC SOYBEAN;

RECOMBINANT PROTEINS;

BETA GLUCURONIDASE; CARBOHYDRATE; PHENOL DERIVATIVE; PROTEIN; RECOMBINANT ENZYME;

AQUEOUS SOLUTION; ARTICLE; BIOREACTOR; CORN; ENZYME ACTIVITY; EXTRACTION; GENE EXPRESSION SYSTEM; IONIC STRENGTH; NONHUMAN; PH; PLANT SEED; PROTEIN EXPRESSION; SOYBEAN; TRANSGENIC PLANT;

GLYCINE MAX; ZEA MAYS;

EID: 77949294118     PISSN: 02732289     EISSN: None     Source Type: Journal    
DOI: 10.1007/s12010-009-8637-5     Document Type: Article

References (26)

1. EE Hood SL Woodard ME Horn 2002 Current Opinion in Biotechnology 13 630 635 10.1016/S0958-1669(02) 00351-8 10.1016/S0958-1669(02)00351-8 1:CAS:528:DC%2BD38XptlWltr4%3D
2. Delaney, D.E. (2002). In Production of recombinant proteins from transgenic crops (E. E., Hood, J.A., Howard (Ed.), (pp. 139-158). Kluwer Academic Publishers, Dordrecht.
3. SL Woodard JM Mayor MR Bailey DK Baker RT Love JR Lane DE Delaney JM McComas-Wagner HD Mallubhotia EE Hood 2003 Biotechnology and Applied Biochemistry 38 123 130 10.1042/BA20030026 10.1042/BA20030026 1:CAS:528:DC%2BD3sXnsVyjtbg%3D
4. TJ Menkhaus Y Bai C Zhang ZL Nikolov CE Glatz 2004 Biotechnology Progress 20 1001 1014 10.1021/bp040011m 10.1021/bp040011m 1:CAS:528:DC%2BD2cXjs1Kgtrs%3D
5. CS Farinas A Leite EA Miranda 2005 Biotechnology Progress 21 1466 1471 10.1021/bp050103r 10.1021/bp050103r 1:CAS:528:DC%2BD2MXotFSisrk%3D
6. Q Zhong Z Gu CE Glatz 2006 Journal of Agricultural and Food Chemistry 54 8086 8092 10.1021/jf061921h 10.1021/jf061921h 1:CAS:528:DC%2BD28XpslKitL4%3D
7. L Zeitlin SS Olmsted TR Moench MS Co BJ Martinell VM Paradkar DR Russel C Queen RA Cone KJ Whaley 1998 Nature Biotechnology 16 1361 1364 10.1038/4344 10.1038/4344 1:CAS:528:DyaK1cXnslOmu7Y%3D
8. R Philip DW Darnowski PJ Maughan LO Vodkin 2001 Plant Science 161 323 335 10.1016/S0168-9452(01) 00420-4 10.1016/S0168-9452(01)00420-4 1:CAS:528:DC%2BD3MXltVaqtL0%3D
9. DA Russel LA Spatola T Dian VM Paradkar DR Dufield JA Carrol MR Schlitter 2005 Biotechnology and Bioengineering 89 775 782 10.1002/bit.20366 10.1002/bit.20366
10. G Robić CS Farinas EL Rech SMA Bueno EA Miranda 2006 Biochemical Engineering Journal 32 7 12 10.1016/j.bej.2006.08.010 10.1016/j.bej.2006.08.010
11. RA Jefferson SM Burgess D Hirsh 1986 Proceedings of the National Academy of Sciences of the United States of America 83 8447 8451 10.1073/pnas.83.22.8447 10.1073/pnas.83.22.8447 1:CAS:528:DyaL2sXksVOgsg%3D%3D
12. ME Horn SL Woodard JA Howard 2004 Plant Cell Reports 22 711 720 10.1007/s00299-004-0767-1 10.1007/s00299-004-0767-1 1:CAS:528: DC%2BD2cXjt1yku74%3D
13. AR Kusnadi RL Evangelista EE Hood JA Howard ZL Nikolov 1998 Biotechnology and Bioengineering 60 44 52 10.1002/(SICI) 1097-0290(19981005) 60:1<44::AID-BIT5>3.0.CO;2-0 10.1002/(SICI)1097-0290(19981005)60: 1<44::AID-BIT5>3.0.CO;2-0 1:CAS:528:DyaK1cXls1ymt7Y%3D
14. C Zhang CE Glatz 1999 Biotechnology Progress 15 12 18 10.1021/bp980110y 10.1021/bp980110y 1:CAS:528:DyaK1MXit1E%3D
15. C Zhang TL Love JM Jilka CE Glatz 2001 Biotechnology Progress 17 161 167 10.1021/bp000140c 10.1021/bp000140c 1:CAS:528:DC%2BD3cXotFymsbk%3D
16. Y Bai ZL Nikolov CE Glatz 2002 Biotechnology Progress 18 1301 1305 10.1021/bp020132r 10.1021/bp020132r 1:CAS:528:DC%2BD38XnvF2hur8%3D
17. TJ Menkhaus C Pate A Krech CE Glatz 2004 Biotechnology and Bioengineering 86 108 114 10.1002/bit.20039 10.1002/bit.20039 1:CAS:528:DC%2BD2cXis1aks7Y%3D
18. FJL Aragão L Sarokin GR Vianna EL Rech 2000 Theoretical and Applied Genetics 101 1 106 10.1007/s001220051441 10.1007/s001220051441
19. MMA Bradford 1976 Analytical Biochemistry 72 248 254 10.1016/0003- 2697(76) 90527-3 10.1016/0003-2697(76)90527-3 1:CAS:528:DyaE28XksVehtrY%3D
20. UK Laemmli 1970 Nature 227 680 685 10.1038/227680a0 10.1038/227680a0 1:CAS:528:DC%2BD3MXlsFags7s%3D
21. WJ Wolf RE Peterson ML Schaer 1992 Journal of Agricultural and Food Chemistry 40 1809 1816 10.1021/jf00022a016 10.1021/jf00022a016 1:CAS:528:DyaK38XlvFSgt74%3D
22. ML Price LG Butler 1977 Journal of Agricultural and Food Chemistry 25 1268 1273 10.1021/jf60214a034 10.1021/jf60214a034 1:CAS:528:DyaE2sXlvValu7o%3D
23. GL Miller 1959 Analytical Chemistry 31 426 428 10.1021/ac60147a030 10.1021/ac60147a030 1:CAS:528:DyaG1MXmtFKiuw%3D%3D
24. Box, G. E. P. (1978). Statistics for experimenters. New York, NY: Wiley.
25. AK Smith SJ Circle 1938 Industrial & Engineering Chemistry 30 1414 1418 10.1021/ie50348a014 10.1021/ie50348a014 1:CAS:528:DyaA1MXmvFSi
26. F Sosulski K Krygier L Hogge 1982 Journal of Agricultural and Food Chemistry 30 337 340 10.1021/jf00110a030 10.1021/jf00110a030 1:CAS:528:DyaL38XhtVaksL0%3D