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Volumn 33, Issue 3, 2008, Pages 294-305

Do co-spray dried excipients offer better lysozyme stabilisation than single excipients?

Author keywords

Excipient mixtures; Lysozyme; Protein stabilisation; Spray drying; Stability study

Indexed keywords

EXCIPIENT; LYSOZYME; MANNITOL; SORBITOL; TREHALOSE;

EID: 39649088233     PISSN: 09280987     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.ejps.2007.12.007     Document Type: Article
Times cited : (31)

References (41)
  • 2
    • 0018789680 scopus 로고
    • Increased thermal stability of proteins in the presence of sugars
    • Back J.F., Oakenfull D., and Smith M.B. Increased thermal stability of proteins in the presence of sugars. Biochemistry 18 23 (1979) 5191-5196
    • (1979) Biochemistry , vol.18 , Issue.23 , pp. 5191-5196
    • Back, J.F.1    Oakenfull, D.2    Smith, M.B.3
  • 3
    • 0034111889 scopus 로고    scopus 로고
    • Investigations on polymorphism of mannitol/sorbitol mixtures after spray-drying using differential scanning calorimetry X-ray diffraction and near infrared spectroscopy.
    • Bauer H., Herkert T., Bartels M., Kovar K.A., Schwarz E., and Schmidt P.C. Investigations on polymorphism of mannitol/sorbitol mixtures after spray-drying using differential scanning calorimetry X-ray diffraction and near infrared spectroscopy. Pharm. Ind. 62 3 (2000) 231-235
    • (2000) Pharm. Ind. , vol.62 , Issue.3 , pp. 231-235
    • Bauer, H.1    Herkert, T.2    Bartels, M.3    Kovar, K.A.4    Schwarz, E.5    Schmidt, P.C.6
  • 4
    • 0028151971 scopus 로고
    • Infrared and Raman spectroscopic studies of interaction between trehalose and lysozyme
    • Belton P.S., and Gil A.M. Infrared and Raman spectroscopic studies of interaction between trehalose and lysozyme. Biopolymers 34 (1994) 957-961
    • (1994) Biopolymers , vol.34 , pp. 957-961
    • Belton, P.S.1    Gil, A.M.2
  • 5
    • 0031744109 scopus 로고    scopus 로고
    • Influence of pH on lysozyme conformation revealed by dielectric spectroscopy
    • Bonincontro A., De Francesco A., and Onori G. Influence of pH on lysozyme conformation revealed by dielectric spectroscopy. Colloids Surf. B: Biointerfaces 12 1 (1998) 1-5
    • (1998) Colloids Surf. B: Biointerfaces , vol.12 , Issue.1 , pp. 1-5
    • Bonincontro, A.1    De Francesco, A.2    Onori, G.3
  • 6
    • 0032949245 scopus 로고    scopus 로고
    • A central composite design to investigate the thermal stabilisation of lysozyme
    • Branchu S. A central composite design to investigate the thermal stabilisation of lysozyme. Pharm. Res. 16 5 (1999) 702-708
    • (1999) Pharm. Res. , vol.16 , Issue.5 , pp. 702-708
    • Branchu, S.1
  • 8
    • 0015761481 scopus 로고
    • Laser Raman spectroscopy of aqueous denaturation of lysozyme
    • Chen M.C., and Lord R.C. Laser Raman spectroscopy of aqueous denaturation of lysozyme. Biochim. Biophys. Acta 328 (1974) 252-260
    • (1974) Biochim. Biophys. Acta , vol.328 , pp. 252-260
    • Chen, M.C.1    Lord, R.C.2
  • 9
    • 0018473089 scopus 로고
    • Lysozyme film hydration events: an IR and gravimetric study
    • Careri G., Giansanti A., Gratton E., and Namprogetti S. Lysozyme film hydration events: an IR and gravimetric study. Biopolymers 18 (1979) 1187-1203
    • (1979) Biopolymers , vol.18 , pp. 1187-1203
    • Careri, G.1    Giansanti, A.2    Gratton, E.3    Namprogetti, S.4
  • 10
    • 0026459045 scopus 로고
    • Effects of cyclodextrins on the stability of globular proteins
    • Cooper A. Effects of cyclodextrins on the stability of globular proteins. J. Am. Chem. Soc. 114 (1992) 9208-9209
    • (1992) J. Am. Chem. Soc. , vol.114 , pp. 9208-9209
    • Cooper, A.1
  • 11
    • 0029820371 scopus 로고    scopus 로고
    • Is trehalose special for preserving dry biomaterials?
    • Crowe L.M., and Reid D.S. Is trehalose special for preserving dry biomaterials?. Biophys. J. 71 4 (1996) 2087-2093
    • (1996) Biophys. J. , vol.71 , Issue.4 , pp. 2087-2093
    • Crowe, L.M.1    Reid, D.S.2
  • 13
    • 0021630171 scopus 로고
    • Modifications of the crystalline structure of sorbitol and its effects on tabletting characteristics
    • Du Ross J.W. Modifications of the crystalline structure of sorbitol and its effects on tabletting characteristics. Pharm. Technol. 8 (1984) 42-53
    • (1984) Pharm. Technol. , vol.8 , pp. 42-53
    • Du Ross, J.W.1
  • 14
    • 39649115475 scopus 로고    scopus 로고
    • Integrity of crystalline lysozyme exceeds that of spray-dried
    • Elkordy A.A., Forbes R.T., and Barry B.W. Integrity of crystalline lysozyme exceeds that of spray-dried. Int. J. Pharm. 00 (2002) 1-12
    • (2002) Int. J. Pharm. , vol.0 , pp. 1-12
    • Elkordy, A.A.1    Forbes, R.T.2    Barry, B.W.3
  • 16
    • 0000946996 scopus 로고
    • The effect of polyhydric alcohols on the thermal denaturation of lysozyme measured using differential scanning calorimetry
    • Fujita Y., Iwasa Y., and Noda Y. The effect of polyhydric alcohols on the thermal denaturation of lysozyme measured using differential scanning calorimetry. Bull. Chem. Soc. Jpn. 55 (1982) 1896-1900
    • (1982) Bull. Chem. Soc. Jpn. , vol.55 , pp. 1896-1900
    • Fujita, Y.1    Iwasa, Y.2    Noda, Y.3
  • 17
    • 0020123955 scopus 로고
    • Calorimetric study on thermal denaturation of lysozyme in polyol-water mixtures
    • Gekko K. Calorimetric study on thermal denaturation of lysozyme in polyol-water mixtures. J. Biochem. 91 (1982) 1197-1204
    • (1982) J. Biochem. , vol.91 , pp. 1197-1204
    • Gekko, K.1
  • 18
    • 0015457797 scopus 로고
    • The effect of polyhydric and monohydric alcohols on the heat induced reversible denaturation of lysozyme and ribonuclease
    • Gerlsma S.Y., and Stuur E.R. The effect of polyhydric and monohydric alcohols on the heat induced reversible denaturation of lysozyme and ribonuclease. Int. J. Pept. Prot. Res. 4 (1972) 377-383
    • (1972) Int. J. Pept. Prot. Res. , vol.4 , pp. 377-383
    • Gerlsma, S.Y.1    Stuur, E.R.2
  • 19
    • 0033105151 scopus 로고    scopus 로고
    • Cyclodextrins in peptide and protein delivery
    • Irie T., and Uekama K. Cyclodextrins in peptide and protein delivery. Adv. Drug Deliv. Rev. 36 1 (1999) 101-123
    • (1999) Adv. Drug Deliv. Rev. , vol.36 , Issue.1 , pp. 101-123
    • Irie, T.1    Uekama, K.2
  • 20
    • 39649122688 scopus 로고
    • Decreased protein-stabilizing effects of cryoprotectants due to crystallisation
    • Izutsu K.-I., Yoshioka S., and Terao T. Decreased protein-stabilizing effects of cryoprotectants due to crystallisation. Chem. Pharm. Bull. 42 (1993) 5-8
    • (1993) Chem. Pharm. Bull. , vol.42 , pp. 5-8
    • Izutsu, K.-I.1    Yoshioka, S.2    Terao, T.3
  • 22
    • 1542295067 scopus 로고    scopus 로고
    • Thermal stability of proteins in aqueous polyol solutions: role of the surface tension of water in the stabilisation effect of polyols
    • Kaushik J.K., and Bhat R. Thermal stability of proteins in aqueous polyol solutions: role of the surface tension of water in the stabilisation effect of polyols. J. Phys. Chem. B. 102 (1998) 7058-7066
    • (1998) J. Phys. Chem. B. , vol.102 , pp. 7058-7066
    • Kaushik, J.K.1    Bhat, R.2
  • 24
    • 2942685201 scopus 로고    scopus 로고
    • Investigation of the stabilisation of freeze-dried lysozyme and the physical properties of the formulations
    • Liao Y.-H., Brown M.B., and Martin G.P. Investigation of the stabilisation of freeze-dried lysozyme and the physical properties of the formulations. Eur. J. Pharm. Biopharm. 58 1 (2004) 15-24
    • (2004) Eur. J. Pharm. Biopharm. , vol.58 , Issue.1 , pp. 15-24
    • Liao, Y.-H.1    Brown, M.B.2    Martin, G.P.3
  • 25
    • 0037151469 scopus 로고    scopus 로고
    • Influence of some formulation parameters on lysozyme adsorption and on its stability in solution
    • Malzert A., Boury F., Robert P., Proust J.E., and Benoit J.P. Influence of some formulation parameters on lysozyme adsorption and on its stability in solution. Int. J. Pharm. 242 1-2 (2002) 405-409
    • (2002) Int. J. Pharm. , vol.242 , Issue.1-2 , pp. 405-409
    • Malzert, A.1    Boury, F.2    Robert, P.3    Proust, J.E.4    Benoit, J.P.5
  • 26
    • 0030265222 scopus 로고    scopus 로고
    • Thermal inactivation of lysozyme as influenced by pH, sucrose and sodium chloride and inactivation and preservative effect in beer
    • Makki F., and Durance T.D. Thermal inactivation of lysozyme as influenced by pH, sucrose and sodium chloride and inactivation and preservative effect in beer. Food Res. Int. 29 7 (1996) 635-645
    • (1996) Food Res. Int. , vol.29 , Issue.7 , pp. 635-645
    • Makki, F.1    Durance, T.D.2
  • 27
    • 0038379784 scopus 로고    scopus 로고
    • An investigation into the crystallization of α,α-trehalose from the amorphous state
    • McGarvey O.S., Kett V.L., and Craig D.Q.M. An investigation into the crystallization of α,α-trehalose from the amorphous state. J. Phys. Chem. B 107 27 (2003) 6614-6620
    • (2003) J. Phys. Chem. B , vol.107 , Issue.27 , pp. 6614-6620
    • McGarvey, O.S.1    Kett, V.L.2    Craig, D.Q.M.3
  • 28
    • 0030940336 scopus 로고    scopus 로고
    • Thermophysical properties of trehalose and its concentrated aqueous solutions
    • Miller D.P., Pablo J.J., and Corti H. Thermophysical properties of trehalose and its concentrated aqueous solutions. Pharm. Res. 14 (1997) 578-590
    • (1997) Pharm. Res. , vol.14 , pp. 578-590
    • Miller, D.P.1    Pablo, J.J.2    Corti, H.3
  • 29
    • 0242353397 scopus 로고    scopus 로고
    • Solute crystallization in mannitol-glycine systems-implications on protein stabilization in freeze-dried formulations
    • Pyne A., Chatterjee K., and Suryanarayanan R. Solute crystallization in mannitol-glycine systems-implications on protein stabilization in freeze-dried formulations. J. Pharm. Sci. 92 11 (2003) 2272-2283
    • (2003) J. Pharm. Sci. , vol.92 , Issue.11 , pp. 2272-2283
    • Pyne, A.1    Chatterjee, K.2    Suryanarayanan, R.3
  • 31
    • 39649116510 scopus 로고
    • Laser Raman spectroscopy of denatured lysozyme
    • Randolph S., and Porubcans S. Laser Raman spectroscopy of denatured lysozyme. Arch. Biochem. Biophys. 186 2 (1978) 256-264
    • (1978) Arch. Biochem. Biophys. , vol.186 , Issue.2 , pp. 256-264
    • Randolph, S.1    Porubcans, S.2
  • 32
    • 0015247070 scopus 로고
    • Hydrogen ion titration curve of lysozyme in 6 molar guanidine hydrochloride
    • Roxby R., and Tanford C. Hydrogen ion titration curve of lysozyme in 6 molar guanidine hydrochloride. Biochemistry 10 (1971) 3348
    • (1971) Biochemistry , vol.10 , pp. 3348
    • Roxby, R.1    Tanford, C.2
  • 33
    • 36649033018 scopus 로고    scopus 로고
    • Conformational analysis of protein secondary structure during spray-drying of antibody/mannitol formulations
    • Schule S., Frieb W., Bechtold-Peters K., and Garidel P. Conformational analysis of protein secondary structure during spray-drying of antibody/mannitol formulations. Eur. J. Pharm. Biopharm. 65 1 (2007) 1-9
    • (2007) Eur. J. Pharm. Biopharm. , vol.65 , Issue.1 , pp. 1-9
    • Schule, S.1    Frieb, W.2    Bechtold-Peters, K.3    Garidel, P.4
  • 34
    • 34247124903 scopus 로고
    • Measurement of lysozyme activity and UV inactivation
    • Shugar D. Measurement of lysozyme activity and UV inactivation. Biochim. Biophys. Acta 8 (1952) 302-309
    • (1952) Biochim. Biophys. Acta , vol.8 , pp. 302-309
    • Shugar, D.1
  • 35
    • 0037139368 scopus 로고    scopus 로고
    • Investigation of protein/carbohydrate interactions in the dried state. 2. Diffuse reflectance FTIR studies
    • Souilliac P.O., Middaugh C.R., and Rytting J.H. Investigation of protein/carbohydrate interactions in the dried state. 2. Diffuse reflectance FTIR studies. Int. J. Pharm. 235 (2002) 207-218
    • (2002) Int. J. Pharm. , vol.235 , pp. 207-218
    • Souilliac, P.O.1    Middaugh, C.R.2    Rytting, J.H.3
  • 36
    • 0025817772 scopus 로고
    • Cryoprotective effect of saccharides on denaturation of catalase by freeze drying
    • Tanaka K., Takeda T., and Miyajima K. Cryoprotective effect of saccharides on denaturation of catalase by freeze drying. Chem. Pharm. Bull. 39 (1991) 1091-1094
    • (1991) Chem. Pharm. Bull. , vol.39 , pp. 1091-1094
    • Tanaka, K.1    Takeda, T.2    Miyajima, K.3
  • 37
    • 0028924665 scopus 로고
    • Stabilization of lysozyme against irreversible inactivation by suppression of chemical reactions
    • Tomizawa H., Hidenori Y., Katsutoshi W., and Imoto T. Stabilization of lysozyme against irreversible inactivation by suppression of chemical reactions. J. Biochem. 117 (1995) 635-640
    • (1995) J. Biochem. , vol.117 , pp. 635-640
    • Tomizawa, H.1    Hidenori, Y.2    Katsutoshi, W.3    Imoto, T.4
  • 38
    • 0000342133 scopus 로고
    • The effects of sugars on the thermal denaturation of lysozyme
    • Uedaira H., and Uedaira H. The effects of sugars on the thermal denaturation of lysozyme. Bull. Chem. Soc. Jpn. 53 (1980) 2451-2455
    • (1980) Bull. Chem. Soc. Jpn. , vol.53 , pp. 2451-2455
    • Uedaira, H.1    Uedaira, H.2
  • 39
    • 0018780588 scopus 로고
    • Thermodynamics of the denaturation of lysozyme in alcohol-water mixtures
    • Velicelebi G., and Sturtevant J.M. Thermodynamics of the denaturation of lysozyme in alcohol-water mixtures. Biochemistry 18 7 (1979) 1180-1186
    • (1979) Biochemistry , vol.18 , Issue.7 , pp. 1180-1186
    • Velicelebi, G.1    Sturtevant, J.M.2
  • 40
    • 0342981451 scopus 로고    scopus 로고
    • Towards a molecular level understanding of protein stabilisation. The interaction between lysozyme and sorbitol.
    • Wimmer R., Olsson M., Petersen M.T.N., Hatti-kaul R., Petersen S.B., and Muller N. Towards a molecular level understanding of protein stabilisation. The interaction between lysozyme and sorbitol. J. Biotech. 55 (1997) 85-100
    • (1997) J. Biotech. , vol.55 , pp. 85-100
    • Wimmer, R.1    Olsson, M.2    Petersen, M.T.N.3    Hatti-kaul, R.4    Petersen, S.B.5    Muller, N.6
  • 41
    • 0031807826 scopus 로고    scopus 로고
    • Determination of the glass properties of d-mannitol using sorbitol as an impurity
    • Yu L., Mishra S., and Rigsbee D.R. Determination of the glass properties of d-mannitol using sorbitol as an impurity. J. Pharm. Sci. 87 6 (1998) 774-777
    • (1998) J. Pharm. Sci. , vol.87 , Issue.6 , pp. 774-777
    • Yu, L.1    Mishra, S.2    Rigsbee, D.R.3


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