Araştırma Makalesi
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Yıl 2022, Cilt: 50 Sayı: 1, 65 - 76, 05.01.2022
https://doi.org/10.15671/hjbc.918700

Öz

Kaynakça

  • 1. J.A. Huntington, P.E. Stein, Structure and properties of ovalbumin, J. Chromatogr. B Biomed. Sci. Appl. 756 (2001) 189–198.
  • 2. M.D.A. Dantas, H.A. Tenório, Thiago I.B. Lopes, H.J.V. Pereira, A.J. Marsaioli, I.M. Figueiredo, J.C.C. Santos, Interactions of tetracyclines with ovalbumin, the main allergen protein from egg white: Spectroscopic and electrophoretic studies, Int. J. Biol. Macromol. 102 (2017) 505–514.
  • 3. X. Fu, Q. Liu, C. Tang, J. Luo, X. Wu, L. Lu, Z. Cai, Study on structural, rheological and foaming properties of ovalbumin by ultrasound-assisted glycation with xylose, Ultrason, Sonochem. 58 (2019) 104644.
  • 4. J.A. Huntington, P.E. Stein, Structure and properties of ovalbumin, J. Chromatogr. B 756 (2001) 189–198.
  • 5. E.D. Abeyrathne, H.Y. Lee, D.U. Ahn, Egg white proteins and their potential use in food processing or as nutraceutical and pharmaceutical agents-a review, Poult. Sci. J 92 (2013), 3292–3299.
  • 6. H.Y. Park, T.J. Yoon, H.H. Kim, Y.S. Han, H.D. Choi, Changes in the antigenicity and allergenicity of ovalbumin in chicken egg white by N-acetylglucosaminidase, Food Chem. 217 (2017) 342–345.
  • 7. L.Z. Sun, S. Elsayed, T.B. Aasen, T. Van Do, N.P. Aardal, E. Florvaag, K. Vaali, Comparison between ovalbumin and ovalbumin peptide 323–339 responses in allergic mice: Humoral and cellular aspects, Scand. J. Immunol. 71 (2010) 329–335.
  • 8. W.H. Yang, Z.C. Tu, H. Wang, X. Li, M. Tian, High-intensity ultrasound enhances the immunoglobulin IgG and IgE binding of ovalbumin, J. Sci. Food Agric. 97 (2017) 2714–2720.
  • 9. M.M. Pereira, R.A.P. Cruz, M.R. Almeida, Á.S. Lima, J.A.P. Coutinho, M.G. Freire, Single-Step Purification of Ovalbumin from Egg White Using Aqueous Biphasic Systems, Process Biochem. 51 (2016) 781–791.
  • 10. I. Roy, M.V. S. Rao, M.N. Gupta, An Integrated Process for Purification of Lysozyme, Ovalbumin, and Ovomucoid From Hen Egg White, Appl. Biochemi. Biotechnol. 111 (2003) 55-63.
  • 11. B. Jiang, J. Na, L. Wang, D. Li, C. Liu, Z. Feng, Eco-Innovation in Reusing Food By-Products: Separation of Ovalbumin from Salted Egg White Using Aqueous Two-Phase System of PEG 1000/(NH4)2SO4, Polymers 11 (2019) 238.
  • 12. K. Liu, S. Chen, H. Chen, P. Tong, J. Gao, Cross-linked ovalbumin catalyzed by polyphenol oxidase: Preparation, structure and potential allergenicity, Int. J. Biol. Macromol. 107 (2018) 2057-2064.
  • 13. S. Jalili-Firoozinezhad, M. Filippi, F. Mohabatpour, D. Letourneur, A. Scherberich, Chicken egg white: Hatching of a new old biomaterial, Mater. Today Commun. 40 (2020) 193-214.
  • 14. H. Xia, L. Wang, C. Li, B. Tian, Q. Li, H. Zhao, Q. Bai, Synthesis of fully porous silica microspheres with high specific surface area for fast HPLC separation of intact proteins and digests of ovalbumin, Microchim. Acta 187 (2020) 382.
  • 15. H. Wang, Q. Sun, J. Tan, Y. Hu, W. Yan, Z. Li, Z. Tu, Conformational alteration and the glycated sites in ovalbumin during vacuum freeze-drying induced glycation: A study using conventional spectrometry and liquid chromatography high resolution mass spectrometry, Food Chem. 318 (2020) 126519.
  • 16. F. Füss, A. Criscuolo, K. Cook, K. Scheffler, J. Bones, Cracking Proteoform Complexity of Ovalbumin with Anion-Exchange Chromatography High-Resolution Mass Spectrometry under Native Conditions, J. Proteome Res. 18 (2019) 3689-3702.
  • 17. B. Jiang, J. Na, L. Wang, D. Li, C. Liu, Z. Feng, Reutilization of Food Waste: One-Step Extration, Purification and Characterization of Ovalbumin from Salted Egg White by Aqueous Two-Phase Flotation, Foods 8 (2019) 286.
  • 18. D. Çimen, A. Denizli, Immobilize Metal Affinity Monolithic Cryogels for Cytochrome C Purification, Colloids Surf. B: Biointerfaces, 93 (2012) 29–35.
  • 19. V.M. Gun’ko, I.N. Savina, S.V. Mikhalovsky, Cryogels: Morphological, structural and adsorption characterisation. Adv. Coll. Int. Sci. 187 (2013) 1-46. 20. Y. Saylan, A. Denizli A. Supermacroporous Composite Cryogels in Biomedical Applications, Gels 5 (2019) 20.
  • 21. Z.J. Rogers, S.A. Bencherif, Cryogelation and Cryogels, Gels 5 (2019) 46.
  • 22. V.I. Lozinsky, I.Y. Galaev, F.M. Plieva, I.N. Savina, H. Jungvid, B. Mattiasson, Polymeric cryogels as promising materials of biotechnological interest. Trends Biotechnol. 21 (2003) 445–451.
  • 23. V.I. Lozinsky, A brief history of polymeric cryogels, Adv. Polym. Sci. 263 (2014) 1–48.
  • 24. A. Kumar, Supermacroporous Cryogels: Biomedical and Biotechnological Applications, Taylor Francis, 480 (2016) 52.
  • 25. D. Çimen, N. Bereli, M. Andaç, A. Denizli, Molecularly imprinted cryogel columns for Concanavalin A purification from jack bean extract. Sep Sci plus. (2018) 1–10.
  • 26. S. Asliyüce, N.Bereli, L. Uzun, M.A. Onur, R. Say, A. Denizli, Ion-imprinted supermacroporous cryogel, for in vitro removal of iron ou t of human plasma with beta thalassemia, Sep. Purif. Technol. 73 (2010) 243–249.
  • 27. G. Baydemir, N. Bereli, M. Andaç, R. Say, I.Y. Galaev, A. Denizli, Supermacroporous poly(hydroxyethyl methacrylate) based cryogel with embedded bilirubin imprinted particles, React. Funct. Polym. 69 (2009) 36–42.
  • 28. M. Andac, I.Y. Galaev, A. Denizli, Affinity based and molecularly imprinted cryogels: Applications in biomacromolecule purification, J. Chromatogr. B 1021 (2016) 69–80.
  • 29. D. Çimen, I. Göktürk, F. Yılmaz, Removal of Iron by Chelation with Molecularly Imprinted Supermacroporous Cryogel, Artif Cells Nanomed Biotechnol. 44 (2016) 1158-1166.
  • 30. X. Zhou, W. Li, X. He, L. Chen, Recent Advances in the Study of Protein Imprinting, Sep. Purif. Rev. 36 (2007) 257–283.
  • 31. T. Takeuchi, T. Hishiya, Molecular Imprinting of Proteins Emerging as a Tool for Protein Recognition, Org. Biomol. Chem. 6 (2008) 2459–2467.
  • 32. T.S. Bedwell, N. Anjum, Y. Ma, J. Czulak, A. Poma, E. Piletska, M.J. Whitcombe, S.A. Piletsky, New Protocol for Optimization of Polymer Composition for Imprinting of Peptides and Proteins, RSC Adv. 9 (2009) 27849–27855.
  • 33. K.V. Abrosimova, O.V. Shulenina, S.V. Paston, FTIR study of secondary structure of bovine serum albumin and ovalbumin, J. Phys. Conf. Ser. 769 (2016) 012016. 34. J. Milošević, J. Petrić, B. Jovčić, B. Janković, N. Polović, Exploring the potential of infrared spectroscopy in qualitative and quantitative monitoring of ovalbumin amyloid fibrillation, Spectrochim. Acta A Mol. Biomol. Spectrosc. 229 (2020) 117882.

PURIFICATION OF OVALBUMIN FROM EGG WHITE USING MOLECULAR IMPRINTED CRYOGELS

Yıl 2022, Cilt: 50 Sayı: 1, 65 - 76, 05.01.2022
https://doi.org/10.15671/hjbc.918700

Öz

Son yıllarda, dünya çapında gıda alerjisi en önemli sorunlardan biridir. Ovalbumin yumurta akında bulunan ana alerjanlardan biridir. Bu çalışmada, ovalbumin baskılanmamış ve baskılanmış poli (hidroksietil metakrilat-metakrilik asit) poli(HEMA-MAA) kriyojeller moleküler baskılama yöntemi kullanılarak sentezlenmiştir. Ovalbumin baskılanmış kriyojellerin karakterizasyonundan sonra, akış hızı, pH etkisi, başlangıçtaki ovalbumin konsantrasyonu ve sıcaklık parametrelerinin etkisi incelenmiştir. Ovalbumin baskılanmış ve baskılanmamış kriyojellerin ovalbumine karşı seçiciliğinin belirlenmesi, yarışmacı moleküller olarak lizozim ve transferrin kullanılarak gerçekleştirilmiştir. Ayrıca ovalbumin baskılanmış kriyojellerin yeniden kullanılabilirlik deneyleri gerçekleştirilmiştir. Ovalbuminin saflığı, sodyum-dodesil sülfat poliakrilamid jel elektroforezi kullanılarak yumurta akından belirlenmiştir.

Kaynakça

  • 1. J.A. Huntington, P.E. Stein, Structure and properties of ovalbumin, J. Chromatogr. B Biomed. Sci. Appl. 756 (2001) 189–198.
  • 2. M.D.A. Dantas, H.A. Tenório, Thiago I.B. Lopes, H.J.V. Pereira, A.J. Marsaioli, I.M. Figueiredo, J.C.C. Santos, Interactions of tetracyclines with ovalbumin, the main allergen protein from egg white: Spectroscopic and electrophoretic studies, Int. J. Biol. Macromol. 102 (2017) 505–514.
  • 3. X. Fu, Q. Liu, C. Tang, J. Luo, X. Wu, L. Lu, Z. Cai, Study on structural, rheological and foaming properties of ovalbumin by ultrasound-assisted glycation with xylose, Ultrason, Sonochem. 58 (2019) 104644.
  • 4. J.A. Huntington, P.E. Stein, Structure and properties of ovalbumin, J. Chromatogr. B 756 (2001) 189–198.
  • 5. E.D. Abeyrathne, H.Y. Lee, D.U. Ahn, Egg white proteins and their potential use in food processing or as nutraceutical and pharmaceutical agents-a review, Poult. Sci. J 92 (2013), 3292–3299.
  • 6. H.Y. Park, T.J. Yoon, H.H. Kim, Y.S. Han, H.D. Choi, Changes in the antigenicity and allergenicity of ovalbumin in chicken egg white by N-acetylglucosaminidase, Food Chem. 217 (2017) 342–345.
  • 7. L.Z. Sun, S. Elsayed, T.B. Aasen, T. Van Do, N.P. Aardal, E. Florvaag, K. Vaali, Comparison between ovalbumin and ovalbumin peptide 323–339 responses in allergic mice: Humoral and cellular aspects, Scand. J. Immunol. 71 (2010) 329–335.
  • 8. W.H. Yang, Z.C. Tu, H. Wang, X. Li, M. Tian, High-intensity ultrasound enhances the immunoglobulin IgG and IgE binding of ovalbumin, J. Sci. Food Agric. 97 (2017) 2714–2720.
  • 9. M.M. Pereira, R.A.P. Cruz, M.R. Almeida, Á.S. Lima, J.A.P. Coutinho, M.G. Freire, Single-Step Purification of Ovalbumin from Egg White Using Aqueous Biphasic Systems, Process Biochem. 51 (2016) 781–791.
  • 10. I. Roy, M.V. S. Rao, M.N. Gupta, An Integrated Process for Purification of Lysozyme, Ovalbumin, and Ovomucoid From Hen Egg White, Appl. Biochemi. Biotechnol. 111 (2003) 55-63.
  • 11. B. Jiang, J. Na, L. Wang, D. Li, C. Liu, Z. Feng, Eco-Innovation in Reusing Food By-Products: Separation of Ovalbumin from Salted Egg White Using Aqueous Two-Phase System of PEG 1000/(NH4)2SO4, Polymers 11 (2019) 238.
  • 12. K. Liu, S. Chen, H. Chen, P. Tong, J. Gao, Cross-linked ovalbumin catalyzed by polyphenol oxidase: Preparation, structure and potential allergenicity, Int. J. Biol. Macromol. 107 (2018) 2057-2064.
  • 13. S. Jalili-Firoozinezhad, M. Filippi, F. Mohabatpour, D. Letourneur, A. Scherberich, Chicken egg white: Hatching of a new old biomaterial, Mater. Today Commun. 40 (2020) 193-214.
  • 14. H. Xia, L. Wang, C. Li, B. Tian, Q. Li, H. Zhao, Q. Bai, Synthesis of fully porous silica microspheres with high specific surface area for fast HPLC separation of intact proteins and digests of ovalbumin, Microchim. Acta 187 (2020) 382.
  • 15. H. Wang, Q. Sun, J. Tan, Y. Hu, W. Yan, Z. Li, Z. Tu, Conformational alteration and the glycated sites in ovalbumin during vacuum freeze-drying induced glycation: A study using conventional spectrometry and liquid chromatography high resolution mass spectrometry, Food Chem. 318 (2020) 126519.
  • 16. F. Füss, A. Criscuolo, K. Cook, K. Scheffler, J. Bones, Cracking Proteoform Complexity of Ovalbumin with Anion-Exchange Chromatography High-Resolution Mass Spectrometry under Native Conditions, J. Proteome Res. 18 (2019) 3689-3702.
  • 17. B. Jiang, J. Na, L. Wang, D. Li, C. Liu, Z. Feng, Reutilization of Food Waste: One-Step Extration, Purification and Characterization of Ovalbumin from Salted Egg White by Aqueous Two-Phase Flotation, Foods 8 (2019) 286.
  • 18. D. Çimen, A. Denizli, Immobilize Metal Affinity Monolithic Cryogels for Cytochrome C Purification, Colloids Surf. B: Biointerfaces, 93 (2012) 29–35.
  • 19. V.M. Gun’ko, I.N. Savina, S.V. Mikhalovsky, Cryogels: Morphological, structural and adsorption characterisation. Adv. Coll. Int. Sci. 187 (2013) 1-46. 20. Y. Saylan, A. Denizli A. Supermacroporous Composite Cryogels in Biomedical Applications, Gels 5 (2019) 20.
  • 21. Z.J. Rogers, S.A. Bencherif, Cryogelation and Cryogels, Gels 5 (2019) 46.
  • 22. V.I. Lozinsky, I.Y. Galaev, F.M. Plieva, I.N. Savina, H. Jungvid, B. Mattiasson, Polymeric cryogels as promising materials of biotechnological interest. Trends Biotechnol. 21 (2003) 445–451.
  • 23. V.I. Lozinsky, A brief history of polymeric cryogels, Adv. Polym. Sci. 263 (2014) 1–48.
  • 24. A. Kumar, Supermacroporous Cryogels: Biomedical and Biotechnological Applications, Taylor Francis, 480 (2016) 52.
  • 25. D. Çimen, N. Bereli, M. Andaç, A. Denizli, Molecularly imprinted cryogel columns for Concanavalin A purification from jack bean extract. Sep Sci plus. (2018) 1–10.
  • 26. S. Asliyüce, N.Bereli, L. Uzun, M.A. Onur, R. Say, A. Denizli, Ion-imprinted supermacroporous cryogel, for in vitro removal of iron ou t of human plasma with beta thalassemia, Sep. Purif. Technol. 73 (2010) 243–249.
  • 27. G. Baydemir, N. Bereli, M. Andaç, R. Say, I.Y. Galaev, A. Denizli, Supermacroporous poly(hydroxyethyl methacrylate) based cryogel with embedded bilirubin imprinted particles, React. Funct. Polym. 69 (2009) 36–42.
  • 28. M. Andac, I.Y. Galaev, A. Denizli, Affinity based and molecularly imprinted cryogels: Applications in biomacromolecule purification, J. Chromatogr. B 1021 (2016) 69–80.
  • 29. D. Çimen, I. Göktürk, F. Yılmaz, Removal of Iron by Chelation with Molecularly Imprinted Supermacroporous Cryogel, Artif Cells Nanomed Biotechnol. 44 (2016) 1158-1166.
  • 30. X. Zhou, W. Li, X. He, L. Chen, Recent Advances in the Study of Protein Imprinting, Sep. Purif. Rev. 36 (2007) 257–283.
  • 31. T. Takeuchi, T. Hishiya, Molecular Imprinting of Proteins Emerging as a Tool for Protein Recognition, Org. Biomol. Chem. 6 (2008) 2459–2467.
  • 32. T.S. Bedwell, N. Anjum, Y. Ma, J. Czulak, A. Poma, E. Piletska, M.J. Whitcombe, S.A. Piletsky, New Protocol for Optimization of Polymer Composition for Imprinting of Peptides and Proteins, RSC Adv. 9 (2009) 27849–27855.
  • 33. K.V. Abrosimova, O.V. Shulenina, S.V. Paston, FTIR study of secondary structure of bovine serum albumin and ovalbumin, J. Phys. Conf. Ser. 769 (2016) 012016. 34. J. Milošević, J. Petrić, B. Jovčić, B. Janković, N. Polović, Exploring the potential of infrared spectroscopy in qualitative and quantitative monitoring of ovalbumin amyloid fibrillation, Spectrochim. Acta A Mol. Biomol. Spectrosc. 229 (2020) 117882.
Toplam 32 adet kaynakça vardır.

Ayrıntılar

Birincil Dil İngilizce
Konular Mühendislik
Bölüm Articles
Yazarlar

Duygu Çimen 0000-0002-5356-0998

Adil Denizli 0000-0001-7548-5741

Erken Görünüm Tarihi 30 Aralık 2021
Yayımlanma Tarihi 5 Ocak 2022
Kabul Tarihi 25 Mayıs 2021
Yayımlandığı Sayı Yıl 2022 Cilt: 50 Sayı: 1

Kaynak Göster

APA Çimen, D., & Denizli, A. (2022). PURIFICATION OF OVALBUMIN FROM EGG WHITE USING MOLECULAR IMPRINTED CRYOGELS. Hacettepe Journal of Biology and Chemistry, 50(1), 65-76. https://doi.org/10.15671/hjbc.918700
AMA Çimen D, Denizli A. PURIFICATION OF OVALBUMIN FROM EGG WHITE USING MOLECULAR IMPRINTED CRYOGELS. HJBC. Ocak 2022;50(1):65-76. doi:10.15671/hjbc.918700
Chicago Çimen, Duygu, ve Adil Denizli. “PURIFICATION OF OVALBUMIN FROM EGG WHITE USING MOLECULAR IMPRINTED CRYOGELS”. Hacettepe Journal of Biology and Chemistry 50, sy. 1 (Ocak 2022): 65-76. https://doi.org/10.15671/hjbc.918700.
EndNote Çimen D, Denizli A (01 Ocak 2022) PURIFICATION OF OVALBUMIN FROM EGG WHITE USING MOLECULAR IMPRINTED CRYOGELS. Hacettepe Journal of Biology and Chemistry 50 1 65–76.
IEEE D. Çimen ve A. Denizli, “PURIFICATION OF OVALBUMIN FROM EGG WHITE USING MOLECULAR IMPRINTED CRYOGELS”, HJBC, c. 50, sy. 1, ss. 65–76, 2022, doi: 10.15671/hjbc.918700.
ISNAD Çimen, Duygu - Denizli, Adil. “PURIFICATION OF OVALBUMIN FROM EGG WHITE USING MOLECULAR IMPRINTED CRYOGELS”. Hacettepe Journal of Biology and Chemistry 50/1 (Ocak 2022), 65-76. https://doi.org/10.15671/hjbc.918700.
JAMA Çimen D, Denizli A. PURIFICATION OF OVALBUMIN FROM EGG WHITE USING MOLECULAR IMPRINTED CRYOGELS. HJBC. 2022;50:65–76.
MLA Çimen, Duygu ve Adil Denizli. “PURIFICATION OF OVALBUMIN FROM EGG WHITE USING MOLECULAR IMPRINTED CRYOGELS”. Hacettepe Journal of Biology and Chemistry, c. 50, sy. 1, 2022, ss. 65-76, doi:10.15671/hjbc.918700.
Vancouver Çimen D, Denizli A. PURIFICATION OF OVALBUMIN FROM EGG WHITE USING MOLECULAR IMPRINTED CRYOGELS. HJBC. 2022;50(1):65-76.

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