BibTex RIS Kaynak Göster

Proteic Feeder Effect on Glucose Oxidase Aggregates Formation

Yıl 2008, Cilt: 36 Sayı: 4, 313 - 318, 01.12.2008

Öz

In this study, it is aimed to prepare cross-linked glucose oxidase GOD aggregates by using different proteic feeders.Bovine serum albumin BSA , gelatine and collagen were used separately as proteic feeders in the aggregate preparation process. The initial enzyme concentration was kept constant as 0.05 mg/ml. The amount of BSA varied from1 to 50 mg and the amount of gelatine and collagen were in the range of 5- 75 mg. A cross-linker, glutaraldehyde 2% v/v has been used in order to form GOD aggregates with proteic feeder. The highest immobilization efficiency wasfound when BSA feeder was used. Activities of both free and immobilised GOD were obtained by measuring theamount of hydrogen peroxide formed from glucose conversion, by using spectrophotometer. The maximum activitieswere obtained at following proteic feeder amounts: BSA 5 mg, collagen 60 mg, gelatine 50 mg. Kinetic parametersof native and immobilised enzyme have been calculated by using Lineweaver-Burk plots in the substrate range of0.01-1 M . The maximum reaction rates for free and immobilised enzyme with different proteic feeders, BSA, gelatine and collagen were calculated as 66.29, 12.22, 9.29, 4.53 mM/min-1, respectively. The corresponding saturationconstants of systems with the maximum activity were 7.9, 11.37, 22.58, 33.6 mM, respectively

Kaynakça

  • 1. Mosbach, K. Immobilised enzymes and cells (Part B) Methods Enzymology, Vol. 135 (1987)
  • 2. Hartmeier W. Immobilised Biocatalysts, Springer-Verlag. (1988)
  • 3. Rocchietti S., Urritia A. S. V., Pregnolata M., Tagliani A., Guisan j. M., Fernandez-Lafuente R., Tereni M.; Influence of the enzyme derivative preparation and substrate structure on the enantioselective of penicillin G acylase, Enzyme Microb. Technol, 31:88-93 (2002)
  • 4. Cabral J. M. S. Kennedy J. F. Immobilisation techniques for altering thermal stability of enzymes, Thermo stability of Enzymes, edited by Gupta M. N. Berlin, Springer-Verlag, 163- 179, (1993).
  • 5. Boller T, Meier C, Menzler S: Eupergit oxirane acrylic beads: how to make the enzyme fit for biocatalysts. Org Process Res Develop, 6:509- 519. (2002).
  • 6. Cao L, van Rantwijk F, Sheldon RA: Crosslinked enzyme aggregates, a simple and effective method for the immobilisation of penicilin acylase.Org Lett, 2.1361-1364 (2000)
  • 7. Rothstein F: Differential precipitation of proteins: science and technology. In Protein Purification Process Engineering, Edited by Harrison RG. New York: Marcel Dekker, Inc;:115-208. (1994).
  • 8. Broun G. B., Chemically aggregates enzymes. In Methods in Enzymology, Vol.44 (Mosbach K., Ed) Academic Press, New York, 263-269, (1977).
  • 9. Gupta M. N., Applications of cross-linking techniques to enzyme/ protein stabilization and bioconjugate preparation, Biocatalyst design for Stability and Specificity Series, Am. Chem. Soc., Washington, D. C., 307-324, (1993).
  • 10. Batra R., Gupta M. N., Non-covalent immobilization of Potato (Solanum tuberosum) polyphenoloxidase on Chitin, Biotechnol. Appl. Biochem, 19: 209-215 (1994).
  • 11. Chen J., Zhang J., Han B., Li J., Feng X., Synthesis of cross-linked aggregates in CO2- expanded micellar solutions, Colloids and Surfaces B: Biointerfaces, 48: 72-76, (2006).
  • 12. Tyagi R., Batra R., Gupta M. N., Amorphous enzyme aggregates: Stability towards heat and aqueous-organic co solvents mixtures, Enzymes and Microbial Technology, 24: 348- 354, (1999).
  • 13. Sigma Technical Bulletin No: 510, Sigma Chemical Co., St. Louis,(1983).
  • 14. Ozyilmaz G., Tukel S. S., Alptekin Oz., Activity and storage stability of immobilised glucose oxidase onto magnesium silicate, Journal of Molecular Catalysis B: Enzymatic, 35: 154-160, (2005).
Yıl 2008, Cilt: 36 Sayı: 4, 313 - 318, 01.12.2008

Öz

Kaynakça

  • 1. Mosbach, K. Immobilised enzymes and cells (Part B) Methods Enzymology, Vol. 135 (1987)
  • 2. Hartmeier W. Immobilised Biocatalysts, Springer-Verlag. (1988)
  • 3. Rocchietti S., Urritia A. S. V., Pregnolata M., Tagliani A., Guisan j. M., Fernandez-Lafuente R., Tereni M.; Influence of the enzyme derivative preparation and substrate structure on the enantioselective of penicillin G acylase, Enzyme Microb. Technol, 31:88-93 (2002)
  • 4. Cabral J. M. S. Kennedy J. F. Immobilisation techniques for altering thermal stability of enzymes, Thermo stability of Enzymes, edited by Gupta M. N. Berlin, Springer-Verlag, 163- 179, (1993).
  • 5. Boller T, Meier C, Menzler S: Eupergit oxirane acrylic beads: how to make the enzyme fit for biocatalysts. Org Process Res Develop, 6:509- 519. (2002).
  • 6. Cao L, van Rantwijk F, Sheldon RA: Crosslinked enzyme aggregates, a simple and effective method for the immobilisation of penicilin acylase.Org Lett, 2.1361-1364 (2000)
  • 7. Rothstein F: Differential precipitation of proteins: science and technology. In Protein Purification Process Engineering, Edited by Harrison RG. New York: Marcel Dekker, Inc;:115-208. (1994).
  • 8. Broun G. B., Chemically aggregates enzymes. In Methods in Enzymology, Vol.44 (Mosbach K., Ed) Academic Press, New York, 263-269, (1977).
  • 9. Gupta M. N., Applications of cross-linking techniques to enzyme/ protein stabilization and bioconjugate preparation, Biocatalyst design for Stability and Specificity Series, Am. Chem. Soc., Washington, D. C., 307-324, (1993).
  • 10. Batra R., Gupta M. N., Non-covalent immobilization of Potato (Solanum tuberosum) polyphenoloxidase on Chitin, Biotechnol. Appl. Biochem, 19: 209-215 (1994).
  • 11. Chen J., Zhang J., Han B., Li J., Feng X., Synthesis of cross-linked aggregates in CO2- expanded micellar solutions, Colloids and Surfaces B: Biointerfaces, 48: 72-76, (2006).
  • 12. Tyagi R., Batra R., Gupta M. N., Amorphous enzyme aggregates: Stability towards heat and aqueous-organic co solvents mixtures, Enzymes and Microbial Technology, 24: 348- 354, (1999).
  • 13. Sigma Technical Bulletin No: 510, Sigma Chemical Co., St. Louis,(1983).
  • 14. Ozyilmaz G., Tukel S. S., Alptekin Oz., Activity and storage stability of immobilised glucose oxidase onto magnesium silicate, Journal of Molecular Catalysis B: Enzymatic, 35: 154-160, (2005).
Toplam 14 adet kaynakça vardır.

Ayrıntılar

Birincil Dil İngilizce
Bölüm Research Article
Yazarlar

Yasemin İspirli Bu kişi benim

Hakan Ayhan Bu kişi benim

Yayımlanma Tarihi 1 Aralık 2008
Yayımlandığı Sayı Yıl 2008 Cilt: 36 Sayı: 4

Kaynak Göster

APA İspirli, Y., & Ayhan, H. (2008). Proteic Feeder Effect on Glucose Oxidase Aggregates Formation. Hacettepe Journal of Biology and Chemistry, 36(4), 313-318.
AMA İspirli Y, Ayhan H. Proteic Feeder Effect on Glucose Oxidase Aggregates Formation. HJBC. Aralık 2008;36(4):313-318.
Chicago İspirli, Yasemin, ve Hakan Ayhan. “Proteic Feeder Effect on Glucose Oxidase Aggregates Formation”. Hacettepe Journal of Biology and Chemistry 36, sy. 4 (Aralık 2008): 313-18.
EndNote İspirli Y, Ayhan H (01 Aralık 2008) Proteic Feeder Effect on Glucose Oxidase Aggregates Formation. Hacettepe Journal of Biology and Chemistry 36 4 313–318.
IEEE Y. İspirli ve H. Ayhan, “Proteic Feeder Effect on Glucose Oxidase Aggregates Formation”, HJBC, c. 36, sy. 4, ss. 313–318, 2008.
ISNAD İspirli, Yasemin - Ayhan, Hakan. “Proteic Feeder Effect on Glucose Oxidase Aggregates Formation”. Hacettepe Journal of Biology and Chemistry 36/4 (Aralık 2008), 313-318.
JAMA İspirli Y, Ayhan H. Proteic Feeder Effect on Glucose Oxidase Aggregates Formation. HJBC. 2008;36:313–318.
MLA İspirli, Yasemin ve Hakan Ayhan. “Proteic Feeder Effect on Glucose Oxidase Aggregates Formation”. Hacettepe Journal of Biology and Chemistry, c. 36, sy. 4, 2008, ss. 313-8.
Vancouver İspirli Y, Ayhan H. Proteic Feeder Effect on Glucose Oxidase Aggregates Formation. HJBC. 2008;36(4):313-8.

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