Kinetics of reextraction of Penicillin G from the organic phase after reactive extraction

1988 ◽  
Vol 3 (2) ◽  
pp. 79-82 ◽  
Author(s):  
Z. Likidis ◽  
K. Sch�gerl
2010 ◽  
Vol 7 (2) ◽  
pp. 185-189
Author(s):  
Imam Santoso ◽  
Buchari Buchari ◽  
M. Bachri Amran ◽  
Aminudin Sulaeman

The aim of this research is to study the effect of concentration carrier, pH and time of extraction on separation's factor of penicillin g - phenyl acetate by reactive extraction technique. The 10 mL  aqueous  solution with variation of  pH : 5, 6 contains 0.001 M penicillin G and 0.001 M phenyl acetate has been extracted with 10 mL n-butyl acetate contains dioctylamine as carrier. Variation concentration  of carrier were 0.000; 0.002; 0.004; 0.006 and 0.008 M. Variation time of extraction were 1, 5, 10, 15 and 20 min. The penicillin G and phenyl acetate that dissolved in organic phase ha been  reextracted with 10 mL aqueous with variation of pH : 7, 8. The optimum condition obtained as follow : concentration dioctylamine was 0.002M ; pH the first phase water was 5 and the second phase water was 8 ; and the time of extraction was 10 min.   Keywords: Separation factor, Reactive extraction


1993 ◽  
Vol 291 (3) ◽  
pp. 907-914 ◽  
Author(s):  
J Martín ◽  
J M Mancheño ◽  
R Arche

Penicillin acylase (PA) from Kluyvera citrophila was inhibited by N-ethoxycarbonyl-2-ethoxy-1,2-dihydroquinoline (EEDQ), a specific carboxy-group-reactive reagent. Enzyme activity progressively decreased to a residual value depending on EEDQ concentration. Neither enzymic nor non-enzymic decomposition of EEDQ is concomitant with PA inactivation. Moreover, enzyme re-activation is achieved by chromatographic removal of EEDQ, pH increase or displacement of the reagent with penicillin G. It was then concluded that PA inactivation is due to an equilibrium reaction. The kinetics of enzyme inactivation was analysed by fitting data to theoretical equations derived in accordance with this mechanism. Corrections for re-activation during the enzyme assay were a necessary introduction. The pH-dependence of the rate constant for EEDQ hydrolysis either alone or in the presence of enzyme was studied by u.v. spectroscopy. It turned out to be coincident with the pH-dependence of the forward and reverse rate constants for the inactivation process. It is suggested that previous protonation of the EEDQ molecule is required for these reactions to occur. The thermodynamic values associated with the overall reaction showed little change. Finally it is proposed that the inactivation of PA by EEDQ proceeds through a two-step reaction. The initial and rapid reversible binding is followed by a slow, time-dependent, non-covalent, reversible inactivating step. The expected behaviour in the case of enzyme modification by covalent activation of carboxy residues is also reviewed.


1996 ◽  
Vol 25 (8) ◽  
pp. 605-606
Author(s):  
Tadashi Mizutani ◽  
Akihiko Tobisawa ◽  
Hisanobu Ogoshi

2016 ◽  
Vol 169 ◽  
pp. 1-8 ◽  
Author(s):  
Jannick Gorden ◽  
Tim Zeiner ◽  
Gabriele Sadowski ◽  
Christoph Brandenbusch

Sign in / Sign up

Export Citation Format

Share Document