Laboratory scale production of the human recombinant iduronate 2-sulfate sulfatase-Like from Pichia pastoris

African Journal of Biotechnology

Volumn 8, Issue 9, 2009, Pages 1786-1792

  Córdoba Ruiz, Henry A ^a   Poutou Piñales, Raúl A ^a   Echeverri Peña, Olga Y ^a   Algecira Enciso, Néstor A ^b   Landázuri, Patricia ^a,c   Sáenz, Homero ^a,d   Barrera Avellaneda, Luis A ^a  

^a PONTIFICIA UNIVERSIDAD JAVERIANA   (Colombia)

^b UNIVERSIDAD NACIONAL DE COLOMBIA   (Colombia)

^c UNIVERSIDAD DEL QUINDÍO   (Colombia)

^d UNIVERSIDAD CENTROCCIDENTAL LISANDRO ALVARADO   (Venezuela)

Author keywords

Hunter syndrome; Iduronate 2 sulfate sulfatase; Methanol induction; Monod model; Pichia pastoris

Indexed keywords

IDURONATE 2 SULFATASE; PHOSPHATE; RECOMBINANT ENZYME; RECOMBINANT IDURONATE 2 SULFATASE; SODIUM CHLORIDE; UNCLASSIFIED DRUG;

ARTICLE; CONTROLLED STUDY; CULTURE MEDIUM; CULTURE TECHNIQUE; ENZYME ACTIVITY; ENZYME KINETICS; FUNGUS CULTURE; MOLECULAR CLONING; NONHUMAN; PICHIA PASTORIS; PROTEIN EXPRESSION;

PICHIA PASTORIS;

EID: 66449098524     PISSN: None     EISSN: 16845315     Source Type: Journal    
DOI: None     Document Type: Article

References (27)

1. Amador E, Almazán M, Quintana M, Poutou RA, Candelario M (1994). Estudio preliminar de la estabilidad de los bancos de células primarios para la producción de interferón alfa recombinante. Biotecnol. Aplic. 11(1): 60-63.
2. Cereghino GP, Cereghino J, Sunga AJ, Johnson MA, Lim M, Gleeson MAG, Cregg JM (2001). New selectable marker/auxotrophic host strain combinations for molecular genetic manipulation of Pichia pastoris. Gene. 263: 159-169. (Pubitemid 32167065)
3. Córdoba H (2004). Estudio de la producción a nivel de laboratorio de la enzima iduronato 2-sulfato humana recombinante (IDShr) en Pichia pastoris. Facultad de Ingeniería Química. Tesis de Maestría. Universidad Nacional de Colombia. Bogotá, DC.
4. Córdoba H, Algecira N, Poutou RA, Barrera LA (2003). Pichia pastoris una alternativa para la producción de glicoproteínas humanas de uso terapéutico. Estrategias de fermentación. Rev. Col. Biotecnol. 5(2): 73-84.
5. Cos C, Ramón R, Montesinos JL, Valero F (2006). Operational strategies, monitoring and control of heterologous protein production in the methylotrophic yeast Pichia pastoris under different promoters: A review. Microb. Cell Fac. 5: 17.
6. Cregg JM, Vedvick TS, Raschke WC (1993). Recent advances in the expression of foreign genes in Pichia pastoris. Biotechnol., 11: 905-910.
7. d'Anjou MC, Daugulis AJ (1997). A model-based feeding strategy for feed-batch fermentation of recombinant Pichia pastoris. Biotechnol. Tech. 11(12): 865-868.
8. Doran PM (1998). Principios de ingeniería de los bioprocesos. Zaragoza, España, Acribia SA., p. 468.
9. Hubner U (1993). Production of alkaline serine protease subtilisin calsbreg by Bacillus licheniformis on complex medium in a stirred tank reactor. Appl. Microbiol. Biotechnol. 40: 182-188.
10. Inan M, Meagher MM, Plantz BA, Sinha J (2005). Causes of proteolytic degradation of secreted recombinant proteins produced in methylotrophic yeast Pichia pastoris: case study with recombinant ovine interferon-T. Biotechnol. Bioeng. 89(1): 102-111.
11. Invitrogen (1996). Pichia expression kit. Protein expression. A manual of methods for expression of recombinant proteins in P. pastoris. Cat. No. K1710-01. California, USA, Invitrogene: p. 134.
12. Jahic M, Rotticci-Mulder JC, Martinelle M, Hult K, Enfors SO (2002). Modeling of growth and energy metabolism of Pichia pastoris producing a fusion protein. Biopro. Biocat. Eng. 24: 385-393.
13. + strain. Enz. Microb. Technol. 39: 936-944.
14. Landázuri P (2002). Clonación del cDNA de la iduronato 2-sulfato sulfatasa humana. Expresión de la enzima en Escherichia coli y Pichia pastoris. Instituto de Errores Innatos del Metabolismo. Tesis Doctoral. Pontificia Universidad Javeriana. Bogotá
15. Lowry OH, Rosebrough NJ, Lewis Farr A, Randall R (1951). Protein measurement with the folin phenol reagent. J. Biol. Chem., pp. 265-275.
16. Mendoza DF, Algecira NA, Córdoba H, Barrera LA (2008). A simple structured model for recombinant IDShr protein production in Pichia pastoris. Biotechnol. Let. 30: 1727-1734.
17. Parkinson EJ, Muller V, Hopwood JJ, Brooks DA (2004). Iduronate 2- sulphatase protein detection in plasma from mucopolysaccharidosis type II patients. Mol. Gen. Metabol. 81: 58-64.
18. Poutou RA, Amador E, Candelario M (1994). Banco de células primario (BCP): Caracterización y papel en la producción de proteínas recombinantes. Biotecnol. Aplic. 11: 55-59.
19. Poutou RA, Córdoba H, Quevedo BE, Landázuri P, Echeverri OY, Sáenz H, Vanegas A, Acero J, Gónzalez A, Herrera J, Algecira N, Caicedo L, Barrera LA (2005a). Expresión de iduronato 2-sulfato sulfatasa humana recombinante (IDShr) en Pichia pastoris. Univ. Scient. 10(1): 75-96.
20. Poutou RA, Quevedo BE, Córdoba H, Sáenz H, Barrera LA (2005b). Influencia de la fuente de carbono sobre la expresión de proteínas aoxin cursive1-reguladas en Pichia pastoris. NOVA 3(3): 75-87.
21. Rodríguez E, Sánchez K, Roca H, Delgado JM (1997) Different methanol feeding strategies to recombinant Pichia pastoris cultures producing high level of dextranase. Biotechol. Tech. 11(7): 461-466.
22. Rose AH, Harrison JS (1989). The yeast. Metabolism and physiology of yeast. London, Academic Press. 3.
23. Schuller HJ (2003). Transcriptional control of nonfermentative metabolism in the yeast Saccharomyces cerevisiae. Curr. Gen. 43: 139-160.
24. Trinh LB, Phue JN, Shiloach J (2003). Effect of methanol feeding strategies on production and yield of recombinant mouse endostatin from Pichia pastoris. Biotechnol. Bioeng. 82(4): 438-444. (Pubitemid 36505882)
25. Voznyi YV, Keulemans LM, Diggelen OP (2001). A fluorogenic enzyme assay for the diagnosis of MPS II (Hunter disease). J. Inherit. Metabolism, 24: 675-680. (Pubitemid 33130088)
26. Wolf K (1996). Nonconventional yeast in biotechnology. A handbook. Berlin, Springer Verlag: p. 618.
27. Zhang W, Bevins MA, Plantz BA, Smith LA, Meagher MM (2000). Modeling Pichia pastoris growth on methanol and optimizing the production of a recombinant protein, the heavy-chain fragment c of botulinum neurotoxin, serotype a. Biotechnol. Bioeng. 70(1): 1-8.