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Volumn 123, Issue 4, 2006, Pages 434-442

Thermostabilization of Bacillus amyloliquefaciens α-amylase by chemical cross-linking

Author keywords

Amylase; Aggregation; Chemical cross linking; Deamidation; Hydrophobicity; Thermostability

Indexed keywords

AGGLOMERATION; CROSSLINKING; ESTERS; HYDROPHOBICITY; MOLECULAR DYNAMICS; PROTEINS; THERMODYNAMIC STABILITY;

EID: 33646518109     PISSN: 01681656     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jbiotec.2005.12.017     Document Type: Article
Times cited : (11)

References (44)
  • 1
    • 33748037939 scopus 로고
    • α-and β-amylases
    • Bernfeld P. α-and β-amylases. Methods Enzymol. 1 (1955) 149-154
    • (1955) Methods Enzymol. , vol.1 , pp. 149-154
    • Bernfeld, P.1
  • 2
    • 0024677047 scopus 로고
    • Stabilization of enzymes by multipoint attachment to agarose-aldehyde gels. Borohydride reduction of trypsin-agarose derivatives
    • Blanco R.M., and Guisán J.M. Stabilization of enzymes by multipoint attachment to agarose-aldehyde gels. Borohydride reduction of trypsin-agarose derivatives. Enzyme Microb. Technol. 11 (1989) 360-366
    • (1989) Enzyme Microb. Technol. , vol.11 , pp. 360-366
    • Blanco, R.M.1    Guisán, J.M.2
  • 3
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein dye-binding
    • Bradford M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein dye-binding. Anal. Biochem. 72 (1976) 248-254
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 5
    • 0023661282 scopus 로고
    • Three dimensional structure of porcine pancreatic alpha-amylase at 2.9 A resolution. Role of calcium in structure and activity
    • Buisson G., Duee E., Haser R., and Payan F. Three dimensional structure of porcine pancreatic alpha-amylase at 2.9 A resolution. Role of calcium in structure and activity. EMBO J. 6 (1987) 3909-3916
    • (1987) EMBO J. , vol.6 , pp. 3909-3916
    • Buisson, G.1    Duee, E.2    Haser, R.3    Payan, F.4
  • 6
    • 0031194458 scopus 로고    scopus 로고
    • The quantification of protein amino groups by the trinitrobenzenesulfonic acid method: a reexamination
    • Cayot P., and Tainturier G. The quantification of protein amino groups by the trinitrobenzenesulfonic acid method: a reexamination. Anal. Biochem. 249 (1997) 184-200
    • (1997) Anal. Biochem. , vol.249 , pp. 184-200
    • Cayot, P.1    Tainturier, G.2
  • 7
    • 0037424370 scopus 로고    scopus 로고
    • Activity-stability relationships in extremophilic enzymes
    • D'Amico S., Marx J.-C., Gerday C., and Feller G. Activity-stability relationships in extremophilic enzymes. J. Biol. Chem. 278 (2003) 7891-7896
    • (2003) J. Biol. Chem. , vol.278 , pp. 7891-7896
    • D'Amico, S.1    Marx, J.-C.2    Gerday, C.3    Feller, G.4
  • 8
    • 0019321850 scopus 로고
    • Chemical crosslinking stabilizes the enzymic activity and quaternary structure of formyltetrahydrofolate synthetase
    • De Renobales M., and Welch W. Chemical crosslinking stabilizes the enzymic activity and quaternary structure of formyltetrahydrofolate synthetase. J. Biol. Chem. 255 (1980) 10460-10463
    • (1980) J. Biol. Chem. , vol.255 , pp. 10460-10463
    • De Renobales, M.1    Welch, W.2
  • 9
    • 13544272805 scopus 로고    scopus 로고
    • Chemical modification of lysine residues in Bacillus licheniformis α-amylase: conversion of an endo- to an exo-type enzyme
    • Ebrahim Habibi A., Khajeh K., and Nemat-Gorgani M. Chemical modification of lysine residues in Bacillus licheniformis α-amylase: conversion of an endo- to an exo-type enzyme. J. Biochem. Mol. Biol. 37 (2004) 462-467
    • (2004) J. Biochem. Mol. Biol. , vol.37 , pp. 462-467
    • Ebrahim Habibi, A.1    Khajeh, K.2    Nemat-Gorgani, M.3
  • 10
    • 0033528657 scopus 로고    scopus 로고
    • Thermodynamic stability of a cold-active α-amylase from the antarctic bacterium Alteromonas haloplanctis
    • Feller G., D'Amico D., and Gerday C. Thermodynamic stability of a cold-active α-amylase from the antarctic bacterium Alteromonas haloplanctis. Biochemistry 38 (1999) 4613-4619
    • (1999) Biochemistry , vol.38 , pp. 4613-4619
    • Feller, G.1    D'Amico, D.2    Gerday, C.3
  • 11
    • 0015115320 scopus 로고
    • The measurement of amino groups in proteins and peptides
    • Fields R. The measurement of amino groups in proteins and peptides. Biochem. J. 124 (1971) 581-590
    • (1971) Biochem. J. , vol.124 , pp. 581-590
    • Fields, R.1
  • 12
    • 0035807038 scopus 로고    scopus 로고
    • Activity and stability of a thermostable α-amylase compared to its mesophilic homologue: mechanisms of thermal adaptation
    • Fitter J., Herrmann R., Dencher N.A., Blume A., and Hauss T. Activity and stability of a thermostable α-amylase compared to its mesophilic homologue: mechanisms of thermal adaptation. Biochemistry 40 (2001) 10723-10731
    • (2001) Biochemistry , vol.40 , pp. 10723-10731
    • Fitter, J.1    Herrmann, R.2    Dencher, N.A.3    Blume, A.4    Hauss, T.5
  • 13
    • 3343015685 scopus 로고    scopus 로고
    • Structural stability and unfolding properties of thermostable bacterial α-amylases: a comparative study of homologous enzymes
    • Fitter J., and Haber-Pohlmeier S. Structural stability and unfolding properties of thermostable bacterial α-amylases: a comparative study of homologous enzymes. Biochemistry 43 (2004) 9589-9599
    • (2004) Biochemistry , vol.43 , pp. 9589-9599
    • Fitter, J.1    Haber-Pohlmeier, S.2
  • 14
    • 24344438293 scopus 로고    scopus 로고
    • Structural and dynamical features contributing to thermostability in α-amylases
    • Fitter J. Structural and dynamical features contributing to thermostability in α-amylases. Cell. Mol. Life Sci. 62 (2005) 1925-1937
    • (2005) Cell. Mol. Life Sci. , vol.62 , pp. 1925-1937
    • Fitter, J.1
  • 15
    • 0020454937 scopus 로고
    • Mechanism of action of human pancreatic and salivary α-amylase on α-4-nitrophenyl maltoheptaoside substrate
    • Hägele E.-O., Schalch E., Rauscher E., Lehmann P., Bürk H., and Wahlefeld A.-W. Mechanism of action of human pancreatic and salivary α-amylase on α-4-nitrophenyl maltoheptaoside substrate. Clin. Chem. 28 (1982) 2201-2205
    • (1982) Clin. Chem. , vol.28 , pp. 2201-2205
    • Hägele, E.-O.1    Schalch, E.2    Rauscher, E.3    Lehmann, P.4    Bürk, H.5    Wahlefeld, A.-W.6
  • 16
    • 0026055308 scopus 로고
    • A classification of glycosyl hydrolases based on amino acid sequence similarities
    • Henrissat B. A classification of glycosyl hydrolases based on amino acid sequence similarities. Biochem. J. 280 (1991) 309-316
    • (1991) Biochem. J. , vol.280 , pp. 309-316
    • Henrissat, B.1
  • 17
    • 0142012120 scopus 로고    scopus 로고
    • Partial unfolding of carbonic anhydrase provides a method for its immobilization on hydrophobic adsorbents and protects it against irreversible thermoinactivation
    • Hosseinkhani S., and Nemat-Gorgani M. Partial unfolding of carbonic anhydrase provides a method for its immobilization on hydrophobic adsorbents and protects it against irreversible thermoinactivation. Enzyme Microb. Technol. 33 (2003) 179-184
    • (2003) Enzyme Microb. Technol. , vol.33 , pp. 179-184
    • Hosseinkhani, S.1    Nemat-Gorgani, M.2
  • 19
    • 0020652626 scopus 로고
    • Bifunctional reagents
    • Ji T.H. Bifunctional reagents. Methods Enzymol. 91 (1983) 580-609
    • (1983) Methods Enzymol. , vol.91 , pp. 580-609
    • Ji, T.H.1
  • 20
    • 2942731686 scopus 로고    scopus 로고
    • Interaction of an intermediate structure of Bacillus subtilis α-amylase with alkyl-substituted Sepharose 4B: a model of membrane translocation
    • Karbalaei-Heidari H.R., Ebrahim Habibi A., Khajeh K., Ranjbar B., and Nemat-Gorgani M. Interaction of an intermediate structure of Bacillus subtilis α-amylase with alkyl-substituted Sepharose 4B: a model of membrane translocation. Appl. Biochem. Biotechnol. 117 (2004) 123-132
    • (2004) Appl. Biochem. Biotechnol. , vol.117 , pp. 123-132
    • Karbalaei-Heidari, H.R.1    Ebrahim Habibi, A.2    Khajeh, K.3    Ranjbar, B.4    Nemat-Gorgani, M.5
  • 21
    • 0031004544 scopus 로고    scopus 로고
    • The application of circular dichroism to studies of protein folding and unfolding
    • Kelly S.M., and Price N.C. The application of circular dichroism to studies of protein folding and unfolding. Biochim. Biophys. Acta 1338 (1997) 161-185
    • (1997) Biochim. Biophys. Acta , vol.1338 , pp. 161-185
    • Kelly, S.M.1    Price, N.C.2
  • 22
    • 0035810275 scopus 로고    scopus 로고
    • Chemical modification of bacterial α-amylases: changes in tertiary structures and the effect of additional calcium
    • Khajeh K., Ranjbar B., Naderi-Manesh H., Ebrahim Habibi A., and Nemat-Gorgani M. Chemical modification of bacterial α-amylases: changes in tertiary structures and the effect of additional calcium. Biochim. Biophys. Acta 28 (2001) 543-549
    • (2001) Biochim. Biophys. Acta , vol.28 , pp. 543-549
    • Khajeh, K.1    Ranjbar, B.2    Naderi-Manesh, H.3    Ebrahim Habibi, A.4    Nemat-Gorgani, M.5
  • 23
    • 0035106604 scopus 로고    scopus 로고
    • Comparative studies on a mesophilic and a thermophilic α-amylase
    • Khajeh K., and Nemat-Gorgani M. Comparative studies on a mesophilic and a thermophilic α-amylase. Appl. Biochem. Biotechnol. 90 (2001) 47-55
    • (2001) Appl. Biochem. Biotechnol. , vol.90 , pp. 47-55
    • Khajeh, K.1    Nemat-Gorgani, M.2
  • 24
    • 0020999167 scopus 로고
    • Stabilization of enzymes against thermal inactivation
    • Klibanov A.M. Stabilization of enzymes against thermal inactivation. Adv. Appl. Microb. 29 (1983) 1-28
    • (1983) Adv. Appl. Microb. , vol.29 , pp. 1-28
    • Klibanov, A.M.1
  • 25
    • 0035831255 scopus 로고    scopus 로고
    • Relationship of sequence and structure to specificity in the α-amylase family of enzymes
    • MacGregor E.A., Janeček S., and Svensson B. Relationship of sequence and structure to specificity in the α-amylase family of enzymes. Biochim. Biophys. Acta 1546 (2001) 1-20
    • (2001) Biochim. Biophys. Acta , vol.1546 , pp. 1-20
    • MacGregor, E.A.1    Janeček, S.2    Svensson, B.3
  • 26
    • 0028933531 scopus 로고
    • Crystal structure of calcium-depleted Bacillus licheniformis alpha-amylase at 2.2 A resolution
    • Machius M., Wiegand G., and Huber R. Crystal structure of calcium-depleted Bacillus licheniformis alpha-amylase at 2.2 A resolution. J. Mol. Biol. 246 (1995) 545-559
    • (1995) J. Mol. Biol. , vol.246 , pp. 545-559
    • Machius, M.1    Wiegand, G.2    Huber, R.3
  • 27
    • 13144305048 scopus 로고    scopus 로고
    • Activation of Bacillus licheniformis alpha-amylase through a disorder→order transition of the substrate-binding site mediated by a calcium-sodium-calcium metal triad
    • Machius M., Declerck N., Huber R., and Wiegand G. Activation of Bacillus licheniformis alpha-amylase through a disorder→order transition of the substrate-binding site mediated by a calcium-sodium-calcium metal triad. Structure 6 (1998) 281-292
    • (1998) Structure , vol.6 , pp. 281-292
    • Machius, M.1    Declerck, N.2    Huber, R.3    Wiegand, G.4
  • 28
    • 0019876640 scopus 로고
    • Affinity labeling of multiplication stimulating activity receptors in membranes from rat and human tissues
    • Massague J., Guillette B.J., and Czech M.P. Affinity labeling of multiplication stimulating activity receptors in membranes from rat and human tissues. J. Biol. Chem. 256 (1981) 2122-2125
    • (1981) J. Biol. Chem. , vol.256 , pp. 2122-2125
    • Massague, J.1    Guillette, B.J.2    Czech, M.P.3
  • 29
    • 0023656828 scopus 로고
    • Variable selection method improves the prediction of protein secondary structure from circular dichroism spectra
    • Marthasarathy P., and Johnson Jr. W.C. Variable selection method improves the prediction of protein secondary structure from circular dichroism spectra. Anal. Biochem. 167 (1987) 76-85
    • (1987) Anal. Biochem. , vol.167 , pp. 76-85
    • Marthasarathy, P.1    Johnson Jr., W.C.2
  • 30
    • 0020121751 scopus 로고
    • Non-ionic adsorptive immobilization of proteins to palmityl-substituted Sepharose 4B
    • Nemat-Gorgani M., and Karimian K. Non-ionic adsorptive immobilization of proteins to palmityl-substituted Sepharose 4B. Eur. J. Biochem. 123 3 (1982) 601-610
    • (1982) Eur. J. Biochem. , vol.123 , Issue.3 , pp. 601-610
    • Nemat-Gorgani, M.1    Karimian, K.2
  • 31
    • 0034731354 scopus 로고    scopus 로고
    • Protein engineering of bacterial α-amylases
    • Nielsen J.E., and Borchert T.V. Protein engineering of bacterial α-amylases. Biochim. Biophys. Acta 1543 (2000) 253-374
    • (2000) Biochim. Biophys. Acta , vol.1543 , pp. 253-374
    • Nielsen, J.E.1    Borchert, T.V.2
  • 33
    • 0028363563 scopus 로고
    • Thermostabilized chemical derivatives of horseradish peroxidase
    • Ryan O., Smyth M.R., and O'Fagain C. Thermostabilized chemical derivatives of horseradish peroxidase. Enzyme Microb. Technol. 16 (1994) 501-505
    • (1994) Enzyme Microb. Technol. , vol.16 , pp. 501-505
    • Ryan, O.1    Smyth, M.R.2    O'Fagain, C.3
  • 34
    • 0000311409 scopus 로고
    • Stabilization of pyranose 2-oxidase and catalase by chemical modification
    • Shaked Z., and Wolfe S. Stabilization of pyranose 2-oxidase and catalase by chemical modification. Methods Enzymol. 137 (1988) 599-615
    • (1988) Methods Enzymol. , vol.137 , pp. 599-615
    • Shaked, Z.1    Wolfe, S.2
  • 35
    • 0037097003 scopus 로고    scopus 로고
    • Calcium-binding parameter of Bacillus amyloliquefaciens alpha-amylase determined by inactivation kinetics
    • Tanaka A., and Hoshino E. Calcium-binding parameter of Bacillus amyloliquefaciens alpha-amylase determined by inactivation kinetics. Biochem. J. 364 (2002) 635-639
    • (2002) Biochem. J. , vol.364 , pp. 635-639
    • Tanaka, A.1    Hoshino, E.2
  • 36
    • 0023834870 scopus 로고
    • Mechanisms of irreversible thermal inactivation of Bacillus α-amylases
    • Tomazic S.J., and Klibanov A.M. Mechanisms of irreversible thermal inactivation of Bacillus α-amylases. J. Biol. Chem. 263 (1988) 3086-3091
    • (1988) J. Biol. Chem. , vol.263 , pp. 3086-3091
    • Tomazic, S.J.1    Klibanov, A.M.2
  • 37
    • 0017872783 scopus 로고
    • The principles of enzyme stabilization. III. The effect of the length of intra-molecular cross-linkages on thermostability of enzymes
    • Torchilin V.P., Maksimenko A.V., Smienov V.S., Berezin I.V., Klibanov A.M., and Martinek K. The principles of enzyme stabilization. III. The effect of the length of intra-molecular cross-linkages on thermostability of enzymes. Biochim. Biophys. Acta 522 (1978) 277-283
    • (1978) Biochim. Biophys. Acta , vol.522 , pp. 277-283
    • Torchilin, V.P.1    Maksimenko, A.V.2    Smienov, V.S.3    Berezin, I.V.4    Klibanov, A.M.5    Martinek, K.6
  • 38
    • 0025822794 scopus 로고
    • Relation between stability, dynamics and enzyme activity in 3-phosphoglycerate kinases from yeast and Thermus thermophilus
    • Varley P., and Pain R.H. Relation between stability, dynamics and enzyme activity in 3-phosphoglycerate kinases from yeast and Thermus thermophilus. J. Mol. Biol. 220 (1991) 532-538
    • (1991) J. Mol. Biol. , vol.220 , pp. 532-538
    • Varley, P.1    Pain, R.H.2
  • 39
    • 0024469173 scopus 로고
    • Kinetic study of the irreversible thermal denaturation of Bacillus licheniformis α-amylase
    • Violet M., and Meunier J.-C. Kinetic study of the irreversible thermal denaturation of Bacillus licheniformis α-amylase. Biochem. J. 263 (1989) 665-670
    • (1989) Biochem. J. , vol.263 , pp. 665-670
    • Violet, M.1    Meunier, J.-C.2
  • 40
    • 0032782071 scopus 로고    scopus 로고
    • Instability, stabilization, and formulation of liquid pharmaceuticals
    • Wang W. Instability, stabilization, and formulation of liquid pharmaceuticals. Int. J. Pharm. 185 (1999) 129-188
    • (1999) Int. J. Pharm. , vol.185 , pp. 129-188
    • Wang, W.1
  • 41
    • 0022870712 scopus 로고
    • Urinary protein as measured with a pyrogallol red-molybdate complex, manually and in a Hitachi 726 automated analyzer
    • Watanabe N., Kamei S., Ohkubo A., Yamanaka M., Ohsawa S., Makino K., and Tokuda K. Urinary protein as measured with a pyrogallol red-molybdate complex, manually and in a Hitachi 726 automated analyzer. Clin. Chem. 32 (1986) 1551-1554
    • (1986) Clin. Chem. , vol.32 , pp. 1551-1554
    • Watanabe, N.1    Kamei, S.2    Ohkubo, A.3    Yamanaka, M.4    Ohsawa, S.5    Makino, K.6    Tokuda, K.7
  • 42
    • 0026955799 scopus 로고
    • Chemical cross-linking and the stabilization of proteins and enzymes
    • Wong S.S., and Wong L.-J. Chemical cross-linking and the stabilization of proteins and enzymes. Enzyme Microb. Technol. 14 (1992) 866-874
    • (1992) Enzyme Microb. Technol. , vol.14 , pp. 866-874
    • Wong, S.S.1    Wong, L.-J.2
  • 43
    • 0026065533 scopus 로고
    • Sequence and structure determinants of the non-enzymatic deamidation of asparagine and glutamine residues in proteins
    • Wright H.T. Sequence and structure determinants of the non-enzymatic deamidation of asparagine and glutamine residues in proteins. Protein Eng. 4 (1991) 283-294
    • (1991) Protein Eng. , vol.4 , pp. 283-294
    • Wright, H.T.1
  • 44
    • 0022503457 scopus 로고
    • Calculation of protein conformation from circular dichroism
    • Yang J.T., Wu C.S.C., and Martinez H.M. Calculation of protein conformation from circular dichroism. Methods Enzymol. 130 (1986) 208-278
    • (1986) Methods Enzymol. , vol.130 , pp. 208-278
    • Yang, J.T.1    Wu, C.S.C.2    Martinez, H.M.3


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