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

Ertan H., Kazan D. , Erarslan A.

BIOTECHNOLOGY TECHNIQUES, cilt.11, sa.4, ss.225-229, 1997 (SCI İndekslerine Giren Dergi) identifier identifier

  • Cilt numarası: 11 Konu: 4
  • Basım Tarihi: 1997
  • Doi Numarası: 10.1023/a:1018478103143
  • Sayfa Sayıları: ss.225-229


The 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.