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Volumn 81, Issue 2, 2003, Pages 241-252

Hydrolysis of lactose by free and immobilized β-galactosidase from thermus sp. strain T2

Author keywords

galactosidase; Activity; Hydrolysis; Immobilization; Kinetic model; Lactose; Thermus

Indexed keywords

ALUMINA; ENZYME IMMOBILIZATION; ENZYME KINETICS; GENES; GLUCOSE; HYDROLYSIS; MICROORGANISMS; PH EFFECTS; SILICA; SOLUTIONS; THERMAL EFFECTS;

EID: 0037454636     PISSN: 00063592     EISSN: None     Source Type: Journal    
DOI: 10.1002/bit.10466     Document Type: Article
Times cited : (43)

References (31)
  • 1
    • 0001460969 scopus 로고
    • Use of novel immobilized β-galactosidase reactor to hydrolyze the lactose constituent of skim milk
    • Bakken AP, Hill CG, Amundson CH. 1991. Use of novel immobilized β-galactosidase reactor to hydrolyze the lactose constituent of skim milk. Appl Biochem Biotech 28/29:741-756.
    • (1991) Appl Biochem Biotech , vol.28-29 , pp. 741-756
    • Bakken, A.P.1    Hill, C.G.2    Amundson, C.H.3
  • 2
    • 0031057219 scopus 로고    scopus 로고
    • Purification, properties and characterization of a high -molecular-mass β-galactosidase isoenzyme from Thermus aquaticus YT-1
    • Berger J-L, Lee BH, Lacroix C. 1997. Purification, properties and characterization of a high -molecular-mass β-galactosidase isoenzyme from Thermus aquaticus YT-1. Biotech Appl Biochem 25:29-41.
    • (1997) Biotech Appl Biochem , vol.25 , pp. 29-41
    • Berger, J.-L.1    Lee, B.H.2    Lacroix, C.3
  • 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 MM. 1976. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72:248-254.
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 4
    • 0029176775 scopus 로고    scopus 로고
    • Determination of kinetics parameters for free and immobilized β-galactosidase
    • Carrara CR, Rubiolo AC. 1996. Determination of kinetics parameters for free and immobilized β-galactosidase. Process Biochem 31:243-248.
    • (1996) Process Biochem , vol.31 , pp. 243-248
    • Carrara, C.R.1    Rubiolo, A.C.2
  • 5
    • 0026469488 scopus 로고
    • The enzymes from extreme thermophiles: Bacterial sources, thermostabilities and industrial relevance
    • Coolbear T, Daniel RM, Morgan HW. 1992. The enzymes from extreme thermophiles: bacterial sources, thermostabilities and industrial relevance. Adv Biochem Eng 45:57-97.
    • (1992) Adv Biochem Eng , vol.45 , pp. 57-97
    • Coolbear, T.1    Daniel, R.M.2    Morgan, H.W.3
  • 6
    • 0022145283 scopus 로고
    • Product inhibition of the enzymatic hydrolysis of lactose
    • Chen K-C, Houng J-Y, Alvin CL. 1985. Product inhibition of the enzymatic hydrolysis of lactose. Enz Microb Technol 7:510-514.
    • (1985) Enz Microb Technol , vol.7 , pp. 510-514
    • Chen, K.-C.1    Houng, J.-Y.2    Alvin, C.L.3
  • 7
    • 0020211575 scopus 로고
    • The kinetics of lactose hydrolysis by the β-galactosidase from Aspergillus niger
    • Flaschel E, Raetz E, Renken A. 1982. The kinetics of lactose hydrolysis by the β-galactosidase from Aspergillus niger. Biotechnol Bioeng 24:2499-2518.
    • (1982) Biotechnol Bioeng , vol.24 , pp. 2499-2518
    • Flaschel, E.1    Raetz, E.2    Renken, A.3
  • 8
    • 0025505864 scopus 로고
    • Modeling of the liquid phase n-octane oxidation catalyzed by cobalt
    • Garcia-Ochoa F, Querol J, Romero A. 1990. Modeling of the liquid phase n-octane oxidation catalyzed by cobalt. Ind Eng Chem Res 29:1989-1994.
    • (1990) Ind Eng Chem Res , vol.29 , pp. 1989-1994
    • Garcia-Ochoa, F.1    Querol, J.2    Romero, A.3
  • 9
    • 84987441218 scopus 로고
    • Isomerization of 1-butene on silica alumina: Kinetic modeling and catalyst deactivation
    • Garcia-Ochoa F, Santos A. 1995. Isomerization of 1-butene on silica alumina: kinetic modeling and catalyst deactivation. AIChE J 41:286-300.
    • (1995) AIChE J , vol.41 , pp. 286-300
    • Garcia-Ochoa, F.1    Santos, A.2
  • 10
    • 0002976888 scopus 로고
    • Hydrolysis of lactose: A literature review
    • Gekas V, Lopez-Leiva M. 1985. Hydrolysis of lactose: a literature review. Process Biochem 20:2-12.
    • (1985) Process Biochem , vol.20 , pp. 2-12
    • Gekas, V.1    Lopez-Leiva, M.2
  • 12
    • 0344492722 scopus 로고    scopus 로고
    • Modification of purified lipases from Candida rugosa with polyethylene glycol: A systematic study
    • Hernaiz MJ. Sanchez-Montero JM, Sinisterra JV. 1999. Modification of purified lipases from Candida rugosa with polyethylene glycol: a systematic study. Enz Microb Technol 24:181-190.
    • (1999) Enz Microb Technol , vol.24 , pp. 181-190
    • Hernaiz, M.J.1    Sanchez-Montero, J.M.2    Sinisterra, J.V.3
  • 13
    • 0034333338 scopus 로고    scopus 로고
    • Kinetic modelling of lactose hydrolysis by an immobilized β-galactosidase from Kluyveromyces fragilis
    • Ladero M, Santos A, Garcia-Ochoa F. 2000. Kinetic modelling of lactose hydrolysis by an immobilized β-galactosidase from Kluyveromyces fragilis. Enz Microb Technol 27:583-592.
    • (2000) Enz Microb Technol , vol.27 , pp. 583-592
    • Ladero, M.1    Santos, A.2    Garcia-Ochoa, F.3
  • 14
    • 0035822773 scopus 로고    scopus 로고
    • Activity over lactose and ONPG of a genetically engineered β-galactosidase from Escherichia coli in solution and immobilized: Kinetic modelling
    • Ladero M, Santos A, Garcia JL, Garcia-Ochoa F. 2001. Activity over lactose and ONPG of a genetically engineered β-galactosidase from Escherichia coli in solution and immobilized: kinetic modelling. Enz Microb Technol 29:181-193.
    • (2001) Enz Microb Technol , vol.29 , pp. 181-193
    • Ladero, M.1    Santos, A.2    Garcia, J.L.3    Garcia-Ochoa, F.4
  • 15
    • 0001581992 scopus 로고
    • Immobilization of lactase on silica gel: Study of lactose hydrolysis using the immobilized material
    • Lartillot S. 1993. Immobilization of lactase on silica gel: study of lactose hydrolysis using the immobilized material. Biochem Ed 21:157-159.
    • (1993) Biochem Ed , vol.21 , pp. 157-159
    • Lartillot, S.1
  • 16
    • 0032189244 scopus 로고    scopus 로고
    • Galactosyl-oligosaccharide formation during lactose hydrolysis: A review
    • Mahoney RR. 1998. Galactosyl-oligosaccharide formation during lactose hydrolysis: a review. Food Chem 63:147-154.
    • (1998) Food Chem , vol.63 , pp. 147-154
    • Mahoney, R.R.1
  • 17
    • 77956922394 scopus 로고
    • Glycosidases and glycosyltransferases
    • Boyer PD, editor. New York: Academic Press
    • Mooser G. 1992. Glycosidases and glycosyltransferases. In: Boyer PD, editor. The enzymes. New York: Academic Press. p 187-233.
    • (1992) The Enzymes , pp. 187-233
    • Mooser, G.1
  • 19
    • 0032126001 scopus 로고    scopus 로고
    • Properties of a thermostable β-glucosidase immobilized using tris(hydroxymethyl)phosphine as a highly effective coupling agent
    • Oswald PR, Evans RA, Henderson W, Daniel RM, Fee CJ. 1998. Properties of a thermostable β-glucosidase immobilized using tris(hydroxymethyl)phosphine as a highly effective coupling agent. Enz Microb Technol 23:14-19.
    • (1998) Enz Microb Technol , vol.23 , pp. 14-19
    • Oswald, P.R.1    Evans, R.A.2    Henderson, W.3    Daniel, R.M.4    Fee, C.J.5
  • 20
    • 0027639561 scopus 로고
    • Studies on modelling and simulation of lactose hydrolysis by free and immobilized β-galactosidase from Aspergillus niger
    • Papayannakos N, Markas G, Kekos D. 1993. Studies on modelling and simulation of lactose hydrolysis by free and immobilized β-galactosidase from Aspergillus niger. Chem Eng J 52:B1-B12.
    • (1993) Chem Eng J , vol.52
    • Papayannakos, N.1    Markas, G.2    Kekos, D.3
  • 21
    • 0033527096 scopus 로고    scopus 로고
    • Development of an ultra-high-temperature process for the enzymatic hydrolysis of lactose. I. The properties of two thermostable β-glycosidases
    • Petzelbauer I, Nidetzky B, Haltrich D, Kulbe KD. 1999. Development of an ultra-high-temperature process for the enzymatic hydrolysis of lactose. I. The properties of two thermostable β-glycosidases. Biotechnol Bioeng 64:322-332.
    • (1999) Biotechnol Bioeng , vol.64 , pp. 322-332
    • Petzelbauer, I.1    Nidetzky, B.2    Haltrich, D.3    Kulbe, K.D.4
  • 22
  • 24
    • 85023286783 scopus 로고
    • β-galactosidase: Review of recent research related to technological application, nutritional concerns and immobilization
    • Richmond M, Gray J, Stine C. 1981. β-Galactosidase: review of recent research related to technological application, nutritional concerns and immobilization. J Dairy Sci 64:1759-1771.
    • (1981) J Dairy Sci , vol.64 , pp. 1759-1771
    • Richmond, M.1    Gray, J.2    Stine, C.3
  • 25
    • 0032524182 scopus 로고    scopus 로고
    • Kinetic modeling of lactose hydrolysis by a β-galactosidase from Kluyveromycesfragilis
    • Santos A, Ladero M, Garcia-Ochoa F. 1998. Kinetic modeling of lactose hydrolysis by a β-galactosidase from Kluyveromycesfragilis. Enz Microb Technol 22:558-567.
    • (1998) Enz Microb Technol , vol.22 , pp. 558-567
    • Santos, A.1    Ladero, M.2    Garcia-Ochoa, F.3
  • 26
    • 0033199021 scopus 로고    scopus 로고
    • Biocatalysis in organic media using enzymes from extremophiles
    • Sellek GA, Chaudhuri JB. 1999. Biocatalysis in organic media using enzymes from extremophiles. Enz Microb Technol 25:471-482.
    • (1999) Enz Microb Technol , vol.25 , pp. 471-482
    • Sellek, G.A.1    Chaudhuri, J.B.2
  • 27
    • 0031777568 scopus 로고    scopus 로고
    • Structure of the β-galactosidase gene from Thermus sp. strain T2: Expression in Escherichia coli and purification in a single step of an active fusion protein
    • Vian A, Carrascosa AV, Garcia JL, Cortes E. 1998. Structure of the β-galactosidase gene from Thermus sp. strain T2: expression in Escherichia coli and purification in a single step of an active fusion protein. Appl Environ Microb 64:2187-2191.
    • (1998) Appl Environ Microb , vol.64 , pp. 2187-2191
    • Vian, A.1    Carrascosa, A.V.2    Garcia, J.L.3    Cortes, E.4
  • 28
    • 0016764964 scopus 로고
    • Kinetic behavior of microencapsulated β-galactosidase
    • Wadiak DT, Carbonell RG. 1975. Kinetic behavior of microencapsulated β-galactosidase. Biotechnol Bioeng 17:1157-1181.
    • (1975) Biotechnol Bioeng , vol.17 , pp. 1157-1181
    • Wadiak, D.T.1    Carbonell, R.G.2
  • 29
    • 0001722763 scopus 로고
    • β-galactosidase
    • Boyer PD, editor. New York: Academic Press
    • Wallenfelds K, Weil R. 1972. β-Galactosidase. In: Boyer PD, editor. The enzymes, Vol 7. New York: Academic Press. p 619-660.
    • (1972) The Enzymes , vol.7 , pp. 619-660
    • Wallenfelds, K.1    Weil, R.2
  • 30
    • 0027619202 scopus 로고
    • Preparation of immobilized proteins covalently coupled through silane coupling agents to inorganic supports
    • Weetall HH. 1993. Preparation of immobilized proteins covalently coupled through silane coupling agents to inorganic supports. Appl Biochem Biotech 41:157-188.
    • (1993) Appl Biochem Biotech , vol.41 , pp. 157-188
    • Weetall, H.H.1
  • 31
    • 0024574012 scopus 로고
    • Effects of temperature on lactose hydrolysis by immobilized β-galactosidase in plug-flow reactor
    • Yang S-T, Okos MR. 1989. Effects of temperature on lactose hydrolysis by immobilized β-galactosidase in plug-flow reactor. Biotechnol Bioeng 33:873-885.
    • (1989) Biotechnol Bioeng , vol.33 , pp. 873-885
    • Yang, S.-T.1    Okos, M.R.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.