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Volumn 39, Issue 7, 2006, Pages 1417-1422

Immobilization of thermostable β-glucosidase from Sulfolobus shibatae by cross-linking with transglutaminase

Author keywords

Glucosidase; Enzyme immobilization; Sulfolobus shibatae; Transglutaminase

Indexed keywords

CROSSLINKING; ENZYMES; HYDROLYSIS; PH EFFECTS; SILICA GEL; THERMODYNAMIC STABILITY;

EID: 33748751885     PISSN: 01410229     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.enzmictec.2006.03.028     Document Type: Article
Times cited : (29)

References (27)
  • 1
    • 0025157985 scopus 로고
    • Economic evaluation of hydrolysis of lactose using immobilized β-galactosidase
    • Axelsson A., and Zacchi G. Economic evaluation of hydrolysis of lactose using immobilized β-galactosidase. Appl Biochem Biotechnol 24/25 (1990) 679-693
    • (1990) Appl Biochem Biotechnol , vol.24-25 , pp. 679-693
    • Axelsson, A.1    Zacchi, G.2
  • 3
    • 33748754227 scopus 로고    scopus 로고
    • Kinetic model of lactose hydrolysis in a hollow-fiber bioreactor
    • Jurado E., Camacho F., Luzon G., and Vicaria J.M. Kinetic model of lactose hydrolysis in a hollow-fiber bioreactor. Chem Eng Sci 59 (2004) 97-405
    • (2004) Chem Eng Sci , vol.59 , pp. 97-405
    • Jurado, E.1    Camacho, F.2    Luzon, G.3    Vicaria, J.M.4
  • 4
    • 0037454636 scopus 로고    scopus 로고
    • Hydrolysis of lactose by free and immobilized β-galactosidase from Thermus sp. strain T2
    • Ladero M., Perez M.T., Santos A., and Garcia-Ochoa F. Hydrolysis of lactose by free and immobilized β-galactosidase from Thermus sp. strain T2. Biotechnol Bioeng 81 (2002) 241-252
    • (2002) Biotechnol Bioeng , vol.81 , pp. 241-252
    • Ladero, M.1    Perez, M.T.2    Santos, A.3    Garcia-Ochoa, F.4
  • 5
    • 0003206797 scopus 로고
    • Immobilization of lactase for use in dairy processing
    • Greenberg N.A., and Mahoney R.R. Immobilization of lactase for use in dairy processing. Process Biochem (1981) 2-8
    • (1981) Process Biochem , pp. 2-8
    • Greenberg, N.A.1    Mahoney, R.R.2
  • 6
    • 0142107388 scopus 로고    scopus 로고
    • The immobilization of a thermophilic β-galactosidase on Sepabeads supports decreases products inhibition. Complete hydrolysis of lactose in dairy products
    • Pessela B.C., Mateo C., Fuentes M., Vian A., Garcia J.L., Carrascosa A.V., et al. The immobilization of a thermophilic β-galactosidase on Sepabeads supports decreases products inhibition. Complete hydrolysis of lactose in dairy products. Enzyme Microb Technol 33 (2003) 199-205
    • (2003) Enzyme Microb Technol , vol.33 , pp. 199-205
    • Pessela, B.C.1    Mateo, C.2    Fuentes, M.3    Vian, A.4    Garcia, J.L.5    Carrascosa, A.V.6
  • 7
    • 0037139753 scopus 로고    scopus 로고
    • Development of an ultrahigh-temperature process for the enzymatic hydrolysis of lactose. IV. Immobilization of two thermostable β-glycosidases and optimization of a packed-bed reactor for lactose conversion
    • Petzelbauer I., Kuhn B., Splechina B., Kulbe K.D., and Nidetzky B. Development of an ultrahigh-temperature process for the enzymatic hydrolysis of lactose. IV. Immobilization of two thermostable β-glycosidases and optimization of a packed-bed reactor for lactose conversion. Biotechnol Bioeng 77 (2002) 619-631
    • (2002) Biotechnol Bioeng , vol.77 , pp. 619-631
    • Petzelbauer, I.1    Kuhn, B.2    Splechina, B.3    Kulbe, K.D.4    Nidetzky, B.5
  • 8
    • 0033179684 scopus 로고    scopus 로고
    • Immobilized enzymes crystals or carriers
    • Tischer W., and Kasche V. Immobilized enzymes crystals or carriers. TIBTECH 17 (1999) 326-335
    • (1999) TIBTECH , vol.17 , pp. 326-335
    • Tischer, W.1    Kasche, V.2
  • 9
    • 0041430560 scopus 로고    scopus 로고
    • Immobilized enzymes: carrier-bound or carrier-free
    • Cao L., vanLangen L., and Sheldon R.A. Immobilized enzymes: carrier-bound or carrier-free. Curr Opin Biotechnol 14 (2003) 387-394
    • (2003) Curr Opin Biotechnol , vol.14 , pp. 387-394
    • Cao, L.1    vanLangen, L.2    Sheldon, R.A.3
  • 10
    • 0027619202 scopus 로고
    • Preparation of immobilized proteins covalently coupled through silane coupling agents to inorganic supports
    • Weetal H.H. Preparation of immobilized proteins covalently coupled through silane coupling agents to inorganic supports. Appl Biochem Biotechnol 41 (1993) 157-188
    • (1993) Appl Biochem Biotechnol , vol.41 , pp. 157-188
    • Weetal, H.H.1
  • 11
    • 0001785135 scopus 로고
    • Thermostabilization of proteins
    • Gupta M.N. Thermostabilization of proteins. Biotechnol Appl Biochem 14 (1991) 1-11
    • (1991) Biotechnol Appl Biochem , vol.14 , pp. 1-11
    • Gupta, M.N.1
  • 13
    • 0344267676 scopus 로고    scopus 로고
    • Isolation and some properties of β-galactosidase from thermophilic bacterium Thermus thermophilus
    • Maciuńska J., Czyż B., and Synowiecki J. Isolation and some properties of β-galactosidase from thermophilic bacterium Thermus thermophilus. Food Chem 63 (1998) 441-445
    • (1998) Food Chem , vol.63 , pp. 441-445
    • Maciuńska, J.1    Czyz, B.2    Synowiecki, J.3
  • 14
    • 0036002458 scopus 로고    scopus 로고
    • Isolation and some properties of the thermostable β-galactosidase of Pyrococcus woesei expressed in Escherichia coli
    • Synowiecki J., and Maciuńska J. Isolation and some properties of the thermostable β-galactosidase of Pyrococcus woesei expressed in Escherichia coli. J Food Biochem 26 (2002) 49-62
    • (2002) J Food Biochem , vol.26 , pp. 49-62
    • Synowiecki, J.1    Maciuńska, J.2
  • 15
    • 0035098779 scopus 로고    scopus 로고
    • Hyperthermophilic enzymes: sources, uses, and molecular mechanisms for thermostability
    • Vieille C., and Zeikus G.J. Hyperthermophilic enzymes: sources, uses, and molecular mechanisms for thermostability. Microbiol Mol Biol Rev 65 (2001) 1-43
    • (2001) Microbiol Mol Biol Rev , vol.65 , pp. 1-43
    • Vieille, C.1    Zeikus, G.J.2
  • 16
    • 0002454257 scopus 로고
    • An extremely thermostable β-glucosidase from the hyperthermphilic archaeon Pyrococcus furiosus; a comparison with other glycosidases
    • Kengen S.W., and Stams A.J. An extremely thermostable β-glucosidase from the hyperthermphilic archaeon Pyrococcus furiosus; a comparison with other glycosidases. Biocatalysis 11 (1994) 79-88
    • (1994) Biocatalysis , vol.11 , pp. 79-88
    • Kengen, S.W.1    Stams, A.J.2
  • 17
    • 0036240154 scopus 로고    scopus 로고
    • Hydrolysis of lactose by β-galactosidase CelB from hyperthermophilic archaeon Pyrococcus furiosus
    • Splechina B., Petzelbauer I., Kuhn B., Kulbe K.D., and Nidetzky B. Hydrolysis of lactose by β-galactosidase CelB from hyperthermophilic archaeon Pyrococcus furiosus. Appl Biochem Biotechnol 98 (2002) 473-488
    • (2002) Appl Biochem Biotechnol , vol.98 , pp. 473-488
    • Splechina, B.1    Petzelbauer, I.2    Kuhn, B.3    Kulbe, K.D.4    Nidetzky, B.5
  • 18
    • 0346849970 scopus 로고    scopus 로고
    • Thermostable β-glucosidase with a broad substrate specifity suitable for processing of lactose-containing products
    • Wołosowska S., and Synowiecki J. Thermostable β-glucosidase with a broad substrate specifity suitable for processing of lactose-containing products. Food Chem 85 (2004) 181-187
    • (2004) Food Chem , vol.85 , pp. 181-187
    • Wołosowska, S.1    Synowiecki, J.2
  • 19
    • 0015275944 scopus 로고
    • Sulfolobus a new genus of sulfur-oxidizing bacteria living at low pH and high temperature
    • Brock T.D., Brock K.M., Belly R.T., and Weis R.I. Sulfolobus a new genus of sulfur-oxidizing bacteria living at low pH and high temperature. Arch Microbiol 84 (1972) 54-68
    • (1972) Arch Microbiol , vol.84 , pp. 54-68
    • Brock, T.D.1    Brock, K.M.2    Belly, R.T.3    Weis, R.I.4
  • 20
    • 0031917122 scopus 로고    scopus 로고
    • Production of the thermostable amylolytic enzymes by Thermococcus hydrothermalis
    • Legin E., Copinet A., and Duchiron F. Production of the thermostable amylolytic enzymes by Thermococcus hydrothermalis. Biotechnol Lett 20 (1998) 363-367
    • (1998) Biotechnol Lett , vol.20 , pp. 363-367
    • Legin, E.1    Copinet, A.2    Duchiron, F.3
  • 21
    • 0001165802 scopus 로고
    • Purification, composition and molecular weight of the β-galactosidase of Escherichia coli K12
    • Craven G.R., Steers E., and Anfinsen C.B. Purification, composition and molecular weight of the β-galactosidase of Escherichia coli K12. J Biol Chem 240 (1965) 2468-2477
    • (1965) J Biol Chem , vol.240 , pp. 2468-2477
    • Craven, G.R.1    Steers, E.2    Anfinsen, C.B.3
  • 22
    • 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
  • 23
    • 67650352071 scopus 로고
    • Colorimetric estimation of lactose and its hydrolysis products
    • Nickerson T.A., Vujicic I.F., and Lin A.Y. Colorimetric estimation of lactose and its hydrolysis products. J Dairy Sci 59 (1976) 386-390
    • (1976) J Dairy Sci , vol.59 , pp. 386-390
    • Nickerson, T.A.1    Vujicic, I.F.2    Lin, A.Y.3
  • 24
    • 0032820434 scopus 로고    scopus 로고
    • Enzyme immobilization via microbial transglutaminase: a method for the generation of stable sensing surfaces
    • Josten A., Meusel M., Spener F., and Haalck L. Enzyme immobilization via microbial transglutaminase: a method for the generation of stable sensing surfaces. J Mol Catal B: Enzymat 7 (1999) 57-66
    • (1999) J Mol Catal B: Enzymat , vol.7 , pp. 57-66
    • Josten, A.1    Meusel, M.2    Spener, F.3    Haalck, L.4
  • 25
    • 0002270229 scopus 로고
    • Immobilization of lactase on chitosan coated gel particles
    • Muzzarelli R., Jeuniaux C., and Graham G.W. (Eds), Plenum Press, New York
    • Griethuysen E., Flashel E., and Renken A. Immobilization of lactase on chitosan coated gel particles. In: Muzzarelli R., Jeuniaux C., and Graham G.W. (Eds). Chitin in nature and technology (1986), Plenum Press, New York 422-427
    • (1986) Chitin in nature and technology , pp. 422-427
    • Griethuysen, E.1    Flashel, E.2    Renken, A.3
  • 26
    • 0021506933 scopus 로고
    • Some properties of β-galactosidase from an extremely thermophilic bacterium
    • Covan D.A., Daniel R.M., Marton A.M., and Morgan H.W. Some properties of β-galactosidase from an extremely thermophilic bacterium. Biotechnol Bioeng 26 (1984) 1141-1145
    • (1984) Biotechnol Bioeng , vol.26 , pp. 1141-1145
    • Covan, D.A.1    Daniel, R.M.2    Marton, A.M.3    Morgan, H.W.4
  • 27
    • 0000498034 scopus 로고    scopus 로고
    • Purification and characterization of β-galactosidase from Mucor pusillus
    • Ismail S.A., Mabrouk S.S., and Mahoney R.R. Purification and characterization of β-galactosidase from Mucor pusillus. J Food Biochem 21 (1997) 145-162
    • (1997) J Food Biochem , vol.21 , pp. 145-162
    • Ismail, S.A.1    Mabrouk, S.S.2    Mahoney, R.R.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.