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Cross-linked stabilization of Escherichia coli penicillin G acylase against pH by dextran-dialdehyde polymers

dc.contributor.authorErarslan, A
dc.contributor.authorErtan, H
dc.contributor.authorKazan, D
dc.date.accessioned2021-03-03T16:55:18Z
dc.date.available2021-03-03T16:55:18Z
dc.date.issued1997
dc.identifier.citationErtan H., Kazan D., Erarslan A., "Cross-linked stabilization of Escherichia coli penicillin G acylase against pH by dextran-dialdehyde polymers", BIOTECHNOLOGY TECHNIQUES, cilt.11, sa.4, ss.225-229, 1997
dc.identifier.issn0951-208X
dc.identifier.othervv_1032021
dc.identifier.otherav_46f4e605-5303-4bf8-9384-db2f44047148
dc.identifier.urihttp://hdl.handle.net/20.500.12627/51266
dc.identifier.urihttps://doi.org/10.1023/a:1018478103143
dc.description.abstractThe inactivation kinetics of Escherichia coli penicillin G acylase (PGA), and cross-linked stabilization of the enzyme by dextran-dialdehyde derivatives of molecular weights of 11500, 37000 and 71000, were similar from pH 2 to pH 10. Inactivation of the native and modified PGA obeyed first order kinetics. The lowest inactivation rate constants for native and dextran-11500-dialdehyde modified PGA were 9.0 x 10(-4) and 1.5 x 10(-4) min(-1) respectively at pH 7.0. The highest pH stabilization (nearly ten-fold) was obtained at pH 7.0.
dc.language.isoeng
dc.subjectSitogenetik
dc.subjectBİYOKİMYASAL ARAŞTIRMA YÖNTEMLERİ
dc.subjectBiyoloji ve Biyokimya
dc.subjectYaşam Bilimleri (LIFE)
dc.subjectBİYOTEKNOLOJİ VE UYGULAMALI MİKROBİYOLOJİ
dc.subjectMikrobiyoloji
dc.subjectBİYOKİMYA VE MOLEKÜLER BİYOLOJİ
dc.subjectMoleküler Biyoloji ve Genetik
dc.subjectTıp
dc.subjectSağlık Bilimleri
dc.subjectTemel Tıp Bilimleri
dc.subjectBiyokimya
dc.subjectYaşam Bilimleri
dc.subjectBiyoteknoloji
dc.subjectMoleküler Biyoloji ve Genetik
dc.subjectTemel Bilimler
dc.titleCross-linked stabilization of Escherichia coli penicillin G acylase against pH by dextran-dialdehyde polymers
dc.typeMakale
dc.relation.journalBIOTECHNOLOGY TECHNIQUES
dc.contributor.department, ,
dc.identifier.volume11
dc.identifier.issue4
dc.identifier.startpage225
dc.identifier.endpage229
dc.contributor.firstauthorID118696


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