메뉴 건너뛰기




Volumn 48, Issue 2, 1997, Pages 191-197

Stabilization of Escherichia coli penicillin G acylase against thermal inactivation by cross-linking with dextran dialdehyde polymers

Author keywords

[No Author keywords available]

Indexed keywords

AMIDASE; BACTERIAL ENZYME; DEXTRAN; PENICILLIN G; POLYMER;

EID: 0030773072     PISSN: 01757598     EISSN: None     Source Type: Journal    
DOI: 10.1007/s002530051037     Document Type: Article
Times cited : (56)

References (23)
  • 1
    • 0025644432 scopus 로고
    • Immobilization-stabilization of penicillin acylase from Escherichia coli
    • Alvaro G, Lafuente RF, Blanco RM, Guisán JM (1990) Immobilization-stabilization of penicillin acylase from Escherichia coli. Appl Biotechnol 26: 181-195
    • (1990) Appl Biotechnol , vol.26 , pp. 181-195
    • Alvaro, G.1    Lafuente, R.F.2    Blanco, R.M.3    Guisán, J.M.4
  • 3
    • 33749946901 scopus 로고
    • Colorimetric method for determination of sugars and related substances
    • Dubois M, Gilles KA, Hamilton JK, Rebers PA, Smith F (1956) Colorimetric method for determination of sugars and related substances. Anal Chem 28: 350-356
    • (1956) Anal Chem , vol.28 , pp. 350-356
    • Dubois, M.1    Gilles, K.A.2    Hamilton, J.K.3    Rebers, P.A.4    Smith, F.5
  • 4
    • 0000546680 scopus 로고
    • The hydrolysis of cephalosporin G by free and immobilized penicillin G acylase from a mutant of Escherichia coli ATCC 11105
    • Erarslan A (1993) The hydrolysis of cephalosporin G by free and immobilized penicillin G acylase from a mutant of Escherichia coli ATCC 11105. Process Biochem 28: 311-318
    • (1993) Process Biochem , vol.28 , pp. 311-318
    • Erarslan, A.1
  • 5
    • 0029134288 scopus 로고
    • The effect of polyol compounds on the thermostability of penicillin G acylase obtained from a mutant of Escherichia coli ATCC 11105
    • Erarslan A (1995) The effect of polyol compounds on the thermostability of penicillin G acylase obtained from a mutant of Escherichia coli ATCC 11105. Process Biochem 30: 133-139
    • (1995) Process Biochem , vol.30 , pp. 133-139
    • Erarslan, A.1
  • 6
    • 0029040546 scopus 로고
    • Thermo-stabilization of penicillin G acylase obtained from a mutant of Escherichia coli ATCC 11105 by bisimidoesters as homobifunctional cross-linking agents
    • Erarslan A, Ertan H (1995) Thermo-stabilization of penicillin G acylase obtained from a mutant of Escherichia coli ATCC 11105 by bisimidoesters as homobifunctional cross-linking agents. Enzyme Microb Technol 17: 629-35
    • (1995) Enzyme Microb Technol , vol.17 , pp. 629-635
    • Erarslan, A.1    Ertan, H.2
  • 7
    • 0025777930 scopus 로고
    • Kinetic investigation of penicillin G acylase from a mutant strain of Escherichia coli ATCC 11105 immobilized on oxirane-acrylic beads
    • Erarslan A, Güruy A (1991a) Kinetic investigation of penicillin G acylase from a mutant strain of Escherichia coli ATCC 11105 immobilized on oxirane-acrylic beads. J Chem Technol Biotechnol 51: 181-195
    • (1991) J Chem Technol Biotechnol , vol.51 , pp. 181-195
    • Erarslan, A.1    Güruy, A.2
  • 8
    • 0000472709 scopus 로고
    • Fermentation of penicillin G acylase by a mutant strain of Escherichia coli ATCC 11105
    • Erarslan A, Güray A (1991b) Fermentation of penicillin G acylase by a mutant strain of Escherichia coli ATCC 11105. Turk J Biol 15: 167-174
    • (1991) Turk J Biol , vol.15 , pp. 167-174
    • Erarslan, A.1    Güray, A.2
  • 9
    • 0026700681 scopus 로고
    • Thermal inactivation kinetics of penicillin G acylase obtained from a mutant derivative of Escherichia coli ATCC 11105
    • Erarslan A, Koçer H (1992) Thermal inactivation kinetics of penicillin G acylase obtained from a mutant derivative of Escherichia coli ATCC 11105. J Chem Technol Biotechnol 55: 79-84
    • (1992) J Chem Technol Biotechnol , vol.55 , pp. 79-84
    • Erarslan, A.1    Koçer, H.2
  • 10
    • 0025868862 scopus 로고
    • Purification and kinetics of penicillin G acylase from a mutant strain of Escherichia coli ATCC 11105
    • Erarslan A, Terzi İ, Güray A, Bermek E (1991) Purification and kinetics of penicillin G acylase from a mutant strain of Escherichia coli ATCC 11105. J Chem Tech Biotech 51: 27-40
    • (1991) J Chem Tech Biotech , vol.51 , pp. 27-40
    • Erarslan, A.1    Terzi, I.2    Güray, A.3    Bermek, E.4
  • 11
    • 0024029957 scopus 로고
    • Aldehyde-agarose gels activated supports for immobilization-stabilization of enzymes
    • Guisán JM (1988) Aldehyde-agarose gels activated supports for immobilization-stabilization of enzymes. Enzyme Microb Technol 10: 375-382
    • (1988) Enzyme Microb Technol , vol.10 , pp. 375-382
    • Guisán, J.M.1
  • 12
    • 0030484089 scopus 로고    scopus 로고
    • Influence of polyhydric compounds on the pH stability of penicillin G acylase obtained from a mutant of Escherichia coli ATCC 11105
    • Kazan D, Erarslan A (1996) Influence of polyhydric compounds on the pH stability of penicillin G acylase obtained from a mutant of Escherichia coli ATCC 11105. Process Biochem 31: 691-697
    • (1996) Process Biochem , vol.31 , pp. 691-697
    • Kazan, D.1    Erarslan, A.2
  • 13
    • 85044701779 scopus 로고    scopus 로고
    • Influence of polyethylene glycols on the thermostability of penicillin G acylase obtained from a mutant of Escherichia coli ATCC 11105
    • Kazan D, Erarslan A (1997) Influence of polyethylene glycols on the thermostability of penicillin G acylase obtained from a mutant of Escherichia coli ATCC 11105. Appl Biochem Biotechnol 62: 1-13
    • (1997) Appl Biochem Biotechnol , vol.62 , pp. 1-13
    • Kazan, D.1    Erarslan, A.2
  • 14
    • 85008079112 scopus 로고
    • Cross-linked stabilization of trypsin with dextran-dialdehyde
    • Kobayashi M, Takatsu K (1994) Cross-linked stabilization of trypsin with dextran-dialdehyde. Biosci Biotechnol Biochem 58: 275-278
    • (1994) Biosci Biotechnol Biochem , vol.58 , pp. 275-278
    • Kobayashi, M.1    Takatsu, K.2
  • 15
    • 0026262142 scopus 로고
    • Enzyme reaction engineering: Synthesis of antibiotics catalyzed by stabilized penicillin G acylase in the presence of organic cosolvents
    • Lafuente RF, Rosell CM, Guisán JM (1991) Enzyme reaction engineering: synthesis of antibiotics catalyzed by stabilized penicillin G acylase in the presence of organic cosolvents. Enzyme Microb Technol 13: 898-905
    • (1991) Enzyme Microb Technol , vol.13 , pp. 898-905
    • Lafuente, R.F.1    Rosell, C.M.2    Guisán, J.M.3
  • 16
    • 0026878360 scopus 로고
    • Additional stabilization of penicillin G acylase-agarose derivatives by controlled chemical modification with formaldehyde
    • Lafuente RF, Rosell CM, Alvaro G, Guisán JM (1992) Additional stabilization of penicillin G acylase-agarose derivatives by controlled chemical modification with formaldehyde. Enzyme Microb Technol 14: 489-495
    • (1992) Enzyme Microb Technol , vol.14 , pp. 489-495
    • Lafuente, R.F.1    Rosell, C.M.2    Alvaro, G.3    Guisán, J.M.4
  • 17
    • 0016636113 scopus 로고
    • Enzyme stabilization by covalent attachment of Carbohydrate
    • Marshall JJ, Rabinowitz ML (1975) Enzyme stabilization by covalent attachment of Carbohydrate. Arch Biochem Biophys 167: 777-779
    • (1975) Arch Biochem Biophys , vol.167 , pp. 777-779
    • Marshall, J.J.1    Rabinowitz, M.L.2
  • 18
    • 0017390556 scopus 로고
    • A rapid, sensitive and vertasile assay for protein using Coomassie brilliant blue G-250
    • Sedmak JJ, Grossberg SE (1977) A rapid, sensitive and vertasile assay for protein using Coomassie brilliant blue G-250. Anal Biochem 79: 544-552
    • (1977) Anal Biochem , vol.79 , pp. 544-552
    • Sedmak, J.J.1    Grossberg, S.E.2
  • 19
    • 0002083389 scopus 로고
    • Evaluation and determination of 6-aminopenicillanic acid by p-dimethyl-aminobenzaldehyde
    • Shewale GJ, Kumar KK, Ambekar GR (1987) Evaluation and determination of 6-aminopenicillanic acid by p-dimethyl-aminobenzaldehyde. Biotechnol Tech 1: 69-72
    • (1987) Biotechnol Tech , vol.1 , pp. 69-72
    • Shewale, G.J.1    Kumar, K.K.2    Ambekar, G.R.3
  • 21
    • 0018121934 scopus 로고
    • Refinement of the Coomassie blue method of protein quantitation
    • Spector T (1978) Refinement of the Coomassie blue method of protein quantitation. Anal. Biochem 86: 142-146
    • (1978) Anal. Biochem , vol.86 , pp. 142-146
    • Spector, T.1
  • 22
    • 0017248834 scopus 로고
    • Functional groups on enzymes suitable for binding to matrices
    • Srere PA, Uyeda K (1976) Functional groups on enzymes suitable for binding to matrices. Methods Enzymol. 44: 1-45
    • (1976) Methods Enzymol. , vol.44 , pp. 1-45
    • Srere, P.A.1    Uyeda, K.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.