메뉴 건너뛰기




Volumn 74, Issue 12, 1999, Pages 1157-1164

Effect of dextran polymers on the stability of soluble Escherichia coli penicillin G acylase

Author keywords

Dextrans; Enzyme inactivation; Escherichia coli; Penicillin G acylase

Indexed keywords

CATALYST DEACTIVATION; ESCHERICHIA COLI; MOLECULAR WEIGHT; PH EFFECTS; POLYSACCHARIDES; RATE CONSTANTS;

EID: 0033406289     PISSN: 02682575     EISSN: None     Source Type: Journal    
DOI: 10.1002/(sici)1097-4660(199912)74:12<1157::aid-jctb165>3.0.co;2-x     Document Type: Article
Times cited : (10)

References (34)
  • 1
    • 0025868862 scopus 로고
    • Purification and kinetics of penicillin G acylase from a mutant strain of Escherichia coli ATCC 11105
    • Erarslan A, Terzi I, Güray A and Bermek E, Purification and kinetics of penicillin G acylase from a mutant strain of Escherichia coli ATCC 11105. J Chem Technol Biotechnol 51:27-40 (1991).
    • (1991) J Chem Technol Biotechnol , vol.51 , pp. 27-40
    • Erarslan, A.1    Terzi, I.2    Güray, A.3    Bermek, E.4
  • 2
    • 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, 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).
    • (1993) Process Biochem , vol.28 , pp. 311-318
    • Erarslan, A.1
  • 3
    • 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 and Güray A, 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).
    • (1991) J Chem Technol Biotechnol , vol.51 , pp. 181-195
    • Erarslan, A.1    Güray, A.2
  • 5
    • 0020999167 scopus 로고
    • Stabilization of enzymes against thermal inactivation
    • ed by Laskin AI, Academic Press, New York
    • Klibanov AM, Stabilization of enzymes against thermal inactivation, in Advances in Applied Microbiology, ed by Laskin AI, Academic Press, New York. Vol 29, pp 1-28 (1983).
    • (1983) Advances in Applied Microbiology , vol.29 , pp. 1-28
    • Klibanov, A.M.1
  • 6
    • 0002883588 scopus 로고
    • Stabilized soluble enzymes
    • Ed by Ghose TT, Fietcher A and Blakebrough N, Springer-Verlag, Berlin
    • Schmid R, Stabilized soluble enzymes, in Advances in Biochemical Engineering, Ed by Ghose TT, Fietcher A and Blakebrough N, Springer-Verlag, Berlin. pp 42-115 (1979).
    • (1979) Advances in Biochemical Engineering , pp. 42-115
    • Schmid, R.1
  • 8
    • 0024029957 scopus 로고    scopus 로고
    • Aldehyde-agarose gels activated supports for immobilization-stabilization of enzymes
    • Guisán JM, Aldehyde-agarose gels activated supports for immobilization-stabilization of enzymes. Enzyme Microb Technol 10:375-382 (1998).
    • (1998) Enzyme Microb Technol , vol.10 , pp. 375-382
    • Guisán, J.M.1
  • 9
    • 0026878360 scopus 로고
    • Additional stabilization of penicillin G acylase-agarose derivatives by controlled chemical modification with formaldehyde
    • Lafuente RF, Rosell CM, Alvaro G and Guisán JM, Additional stabilization of penicillin G acylase-agarose derivatives by controlled chemical modification with formaldehyde. Enzyme Microb Technol 14:489-495 (1992).
    • (1992) Enzyme Microb Technol , vol.14 , pp. 489-495
    • Lafuente, R.F.1    Rosell, C.M.2    Alvaro, G.3    Guisán, J.M.4
  • 10
    • 0029040546 scopus 로고
    • Thermostabilization of penicillin G acylase obtained from a mutant of Esherichia coli ATCC 11105 by bisimidoesters as homobifunctional crosslinking agents
    • Erarslan A and Ertan H, Thermostabilization of penicillin G acylase obtained from a mutant of Esherichia coli ATCC 11105 by bisimidoesters as homobifunctional crosslinking agents. Enzyme Microb Technol 17:629-635 (1995).
    • (1995) Enzyme Microb Technol , vol.17 , pp. 629-635
    • Erarslan, A.1    Ertan, H.2
  • 11
    • 0029176047 scopus 로고    scopus 로고
    • Stabilization of penicillin G acylase agents pH by chemical crosslinking
    • Kazan D, Ertan H and Erarslan A, Stabilization of penicillin G acylase agents pH by chemical crosslinking. Process Biochem 31:135-140 (1996).
    • (1996) Process Biochem , vol.31 , pp. 135-140
    • Kazan, D.1    Ertan, H.2    Erarslan, A.3
  • 12
    • 0023077097 scopus 로고
    • Penicillin acylase activity and stability in PEG solutions
    • Andersson E and Hahn-Hägerdal B, Penicillin acylase activity and stability in PEG solutions. Annals New York Acad Sci 501:85-87 (1987).
    • (1987) Annals New York Acad Sci , vol.501 , pp. 85-87
    • Andersson, E.1    Hahn-Hägerdal, B.2
  • 13
    • 0023274228 scopus 로고
    • I. Stability of penicillin acylase in poly(ethylene glycol) and potassium phosphate solutions in relation to the water activity
    • Andersson E and Hahn-Hägerdal B, I. Stability of penicillin acylase in poly(ethylene glycol) and potassium phosphate solutions in relation to the water activity. Biochim Biophysics Acta 912:317-324 (1987).
    • (1987) Biochim Biophysics Acta , vol.912 , pp. 317-324
    • Andersson, E.1    Hahn-Hägerdal, B.2
  • 15
    • 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, 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 (1994).
    • (1994) Process Biochem , vol.30 , pp. 133-139
    • Erarslan, A.1
  • 16
    • 0030484089 scopus 로고    scopus 로고
    • Influence of polyhydric compounds on the pH stability of penicillin G acylase obtained from a mutant of Esherichia coli ATCC 11105
    • Kazan D and Erarslan A, Influence of polyhydric compounds on the pH stability of penicillin G acylase obtained from a mutant of Esherichia coli ATCC 11105. Process Biochem 31:691-697 (1996).
    • (1996) Process Biochem , vol.31 , pp. 691-697
    • Kazan, D.1    Erarslan, A.2
  • 17
    • 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 and Erarslan A, Influence of polyethylene glycols on the thermostability of penicillin G acylase obtained from a mutant of Escherichia coli ATCC 11105. Appl Biochem Biotech 62:1-13 (1997).
    • (1997) Appl Biochem Biotech , vol.62 , pp. 1-13
    • Kazan, D.1    Erarslan, A.2
  • 18
    • 0028472579 scopus 로고
    • Storage stabilization and purification of enzyme by water-soluble synthetic polymers
    • Bryjak J and Noworyta A, Storage stabilization and purification of enzyme by water-soluble synthetic polymers. Enzyme Microb Technol 16:616-621 (1994).
    • (1994) Enzyme Microb Technol , vol.16 , pp. 616-621
    • Bryjak, J.1    Noworyta, A.2
  • 19
    • 0030586927 scopus 로고    scopus 로고
    • Membrane reactor with soluble forms of penicillin acylase
    • 1996
    • Bryjak J, Bryjak M and Noworyta A, 1996. Membrane reactor with soluble forms of penicillin acylase. Enzyme Microb Technol 19:196-201 (1996).
    • (1996) Enzyme Microb Technol , vol.19 , pp. 196-201
    • Bryjak, J.1    Bryjak, M.2    Noworyta, A.3
  • 20
    • 0000472709 scopus 로고
    • Fermentation of penicillin G acylase by a mutant strain of Escherichia coli ATCC 11105
    • Erarslan A and Güray A, Fermentation of penicillin G acylase by a mutant strain of Escherichia coli ATCC 11105. Doga-Tr J Biology 15:167-174 (1991).
    • (1991) Doga-Tr J Biology , vol.15 , pp. 167-174
    • Erarslan, A.1    Güray, A.2
  • 22
    • 0002083389 scopus 로고
    • Evaluation and determination of 6-aminopenicillanic acid by p-dimethylaminobenzaldehyde
    • Shewale GJ, Kumar KK and Ambekar GR, Evaluation and determination of 6-aminopenicillanic acid by p-dimethylaminobenzaldehyde. Biotechnol Techniques 1:69-72 (1987).
    • (1987) Biotechnol Techniques , vol.1 , pp. 69-72
    • Shewale, G.J.1    Kumar, K.K.2    Ambekar, G.R.3
  • 23
    • 0018121934 scopus 로고
    • Refinement of the coomassie blue method of protein quantitation
    • Spector T, Refinement of the coomassie blue method of protein quantitation. Anal Biochem 86:142-146 (1978).
    • (1978) Anal Biochem , vol.86 , pp. 142-146
    • Spector, T.1
  • 24
    • 0017390556 scopus 로고
    • A rapid, sensitive and versatile assay for protein using Coomassie Brilliant Blue G-250
    • Sedmak JJ and Grossberg SE, A rapid, sensitive and versatile assay for protein using Coomassie Brilliant Blue G-250. Anal Biochem 79:544-552 (1977).
    • (1977) Anal Biochem , vol.79 , pp. 544-552
    • Sedmak, J.J.1    Grossberg, S.E.2
  • 25
    • 0026700681 scopus 로고
    • Thermal inactivation kinetics of penicillin G acylase obtained from a mutant derivative of Escherichia coli ATCC 11105
    • Erarslan A and Koçer H, 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).
    • (1992) J Chem Technol Biotechnol , vol.55 , pp. 79-84
    • Erarslan, A.1    Koçer, H.2
  • 26
    • 0027255479 scopus 로고
    • Structural and genetic analysis of protein stability
    • Mathews BW, Structural and genetic analysis of protein stability. Annu Rev Biochem 62:139-160 (1993).
    • (1993) Annu Rev Biochem , vol.62 , pp. 139-160
    • Mathews, B.W.1
  • 27
    • 0021699812 scopus 로고
    • Effect of water activity on enzyme action and stability
    • Ed by Laskin AI, Tsao GT and Wingard LB Jr, Annals of the New York Academy of Science, New York
    • Monsan P and Combes D, Effect of water activity on enzyme action and stability, in Enzyme Engineering, Ed by Laskin AI, Tsao GT and Wingard LB Jr, Annals of the New York Academy of Science, New York, pp 48-61 (1984).
    • (1984) Enzyme Engineering , pp. 48-61
    • Monsan, P.1    Combes, D.2
  • 28
    • 0021675149 scopus 로고
    • Effect of polyhydric compounds on invertase stabilization
    • Ed by Laskin AI, Tsao GT and Wingard LB Jr, Annals of the New York Academy of Science, New York
    • Combes D and Monsan P, Effect of polyhydric compounds on invertase stabilization, in Enzyme Engineering, Ed by Laskin AI, Tsao GT and Wingard LB Jr, Annals of the New York Academy of Science, New York, pp 61-63 (1984).
    • (1984) Enzyme Engineering , pp. 61-63
    • Combes, D.1    Monsan, P.2
  • 29
    • 0020477017 scopus 로고
    • Stabilization of protein structure by sugars
    • Arakawa T and Timasheff SN, Stabilization of protein structure by sugars. Biochemistry 21:6536-6544 (1982).
    • (1982) Biochemistry , vol.21 , pp. 6536-6544
    • Arakawa, T.1    Timasheff, S.N.2
  • 30
    • 0028098166 scopus 로고
    • The influence of polyalcohols and carbohydrates on the thermo-stability of α-amylase
    • De Cordt S, Hendrickx M, Maesmans G and Tobback P, The influence of polyalcohols and carbohydrates on the thermo-stability of α-amylase. Biotechnol Bioeng 43:107-114 (1994).
    • (1994) Biotechnol Bioeng , vol.43 , pp. 107-114
    • De Cordt, S.1    Hendrickx, M.2    Maesmans, G.3    Tobback, P.4
  • 31
    • 0014408671 scopus 로고
    • Reversible denaturation of ribonuclease in aqueous solutions as influenced by polyhydric alcohol and some other additives
    • Gerlsma SY, Reversible denaturation of ribonuclease in aqueous solutions as influenced by polyhydric alcohol and some other additives. J Biol Chem 243:957-961 (1968).
    • (1968) J Biol Chem , vol.243 , pp. 957-961
    • Gerlsma, S.Y.1
  • 32
    • 0018789680 scopus 로고
    • Increased thermal stability of proteins in the presence of sugars and polyols
    • Back JF, Oakenfull D and Smith MB, Increased thermal stability of proteins in the presence of sugars and polyols. Biochemistry 18:5191-5196 (1979).
    • (1979) Biochemistry , vol.18 , pp. 5191-5196
    • Back, J.F.1    Oakenfull, D.2    Smith, M.B.3
  • 33
    • 0021371442 scopus 로고
    • Structure-stability relationships in proteins: New approaches to stabilizing enzyme
    • Mozhaev VV and Martinek K, Structure-stability relationships in proteins: new approaches to stabilizing enzyme. Enzyme Microb Technol 6:50-59 (1984).
    • (1984) Enzyme Microb Technol , vol.6 , pp. 50-59
    • Mozhaev, V.V.1    Martinek, K.2
  • 34
    • 0024640089 scopus 로고
    • Stabilization of restriction endonuclease Bam HI by cross-linking reagents
    • Dubey AK, Bisaria VS, Mukhopadhyay SN and Ghose TK, Stabilization of restriction endonuclease Bam HI by cross-linking reagents. Biotechnol Bioeng 33:1311-1316 (1989).
    • (1989) Biotechnol Bioeng , vol.33 , pp. 1311-1316
    • Dubey, A.K.1    Bisaria, V.S.2    Mukhopadhyay, S.N.3    Ghose, T.K.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.