Enzyme-ion exchanger interactions in serine alkaline protease separation: theory, equilibria and kinetics

Çalık, Pınar
Calik, G
Ozdamar, TH
Kinetics of ion exchange separation of serine alkaline protease (SAP) by cation- and anion-exchangers, respectively, for the SAP(+)/H+ and SAP(-)/OH- ion exchange reactions were studied with four different resins, i.e. low acidic Macro-prep CM, high acidic Macro-prep HighS, low basic Macro-prep DEAE, and high basic Macro-prep HighQ. The effects of pH on ion exchange equilibria were investigated within pH = 6.5-8.0 and pH = 9.5-11.0, respectively, for the SAP+/H+ cation exchange and SAP-/OH- anion exchange reactions at T = 10-25 degreesC, and the results were interpreted on the basis of the theory of exchange of enzyme-ions. Although Macro-prep CM showed the highest SAP binding capacity at pH = 7.0, maximum recovery of SAP activity was obtained at 15 degreesC and pH = 6.5. Effects of feed concentration and flow rate were investigated in differential-(DIC) and integral (IC) ion exchange columns and 0.025 mol dm(-3) and 1.0 x 10(-2) dm(3) min(-1) gave the highest enzyme recovery as 70%. The overall internal-external mass transfer coefficient which was found by differential analysis showed the importance of liquid phase mass transfer resistances on the process under the operation conditions applied.


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Kadaifci, Bijen; Yücel, Hayrettin; Department of Chemical Engineering (2011)
In this study binary and ternary ion exchange on Zeolite NaA using silver and cadmium ions were investigated. Ion exchange were conducted at constant temperature (25oC) and normality (0.1N) in a batch system for both binary and ternary experiments. Zeolite weights were varied between 0.1 and 1 g for binary experiments. Thermodynamic analysis of binary ion exchange between Cd2+-Na+ and Ag+-Na+ were examined and thermodynamic equilibrium constant and Gibbs free energy were calculated. Thermodynamic equilibriu...
Production of lactic acid esters catalyzed by heteropoly acid supported over ion-exchange resins
AYTURK, E; Hamamcı, Haluk; Karakaş, Gürkan (2003-01-01)
The heterogeneous liquid-phase esterification reaction of lactic acid with ethyl alcohol accompanied with lactoyllactic acid hydrolysis over heteropoly acid supported on ion exchange resin catalysts was investigated at 343 K with ethanol to lactic acid molar ratio of 1:1. The catalysts with 5-20% of tungstophosphoric (H(3)PW(12)O(40).xH(2)O) and molybdophosphoric (H(3)PMo(12)O(40).xH(2)O) acid type of heteropoly acids over Lewatit(R) S100 showed higher activities than the resin itself. DRIFTS and XRD analys...
Oxygen-transfer strategy and its regulation effects in serine alkaline protease production by Bacillus licheniformis
Çalık, Pınar; Özdamar, Tunçer H. (2000-08-01)
The effects of oxygen transfer on the production and product distribution in serine alkaline protease (SAP) fermentation by Bacillus licheniformis and oxygen-transfer strategy in relation to the physiology of the bacilli were investigated on a defined medium with citric acid as sole carbon source in 3.5-dm(3) batch bioreactor systems. By forming a 3 x 3 matrix with the parameters air-inlet rates of Q(O)/V-R = 0.2, 0.5, 1.0 vvm, and agitation rates of N = 150, 500, 750 min(-1), the effects of oxygen transfer...
Substrate interactions during the biodegradation of benzene, toluene and phenol mixtures
Abu Hamed, T; Bayraktar, E; Mehmetoglu, T; Mehmetoglu, U (Elsevier BV, 2003-09-30)
Benzene, toluene and phenol were degraded completely at high initial concentrations by Pseudomonas putida F I ATCC 700007. Two hundred and fifty milligram per litre benzene, 225 mg/l toluene and 200 mg/l phenol were degraded individually in 19, 14 and 3 5 h, respectively. The biodegradation times increased on increasing the substrate concentration. The maximum biodegradation rates were 149 mg benzene/g dry cell h for 60 mg/l benzene, 44 mg toluene/g dry cell h for 110 mg/l toluene and 102 mg phenol/g dry ce...
Enzyme Catalyzed Trans-Benzoin Condensation
BİLİR, Gökçil; AYHAN SITKI, Demir; Özçubukçu, Salih (2018-04-01)
Benzaldehyde lyase (BAL) is an enzyme that is used in the C-C bond cleavage and formation which was isolated first from Pseudomonas fluorescens Biovar I. It requires thiamine diphosphate (ThDP) and Mg(II) ions as cofactors. In this work, BAL was used as an enzymatic catalysis for the trans-benzoin condensation reaction between racemic benzoins and benzyloxyacetaldehyde to form unsymmetrical benzoin products with moderate enantiomeric excesses. (S)-benzoin derivatives remained unreacted at the end of the rea...
Citation Formats
P. Çalık, G. Calik, and T. Ozdamar, “Enzyme-ion exchanger interactions in serine alkaline protease separation: theory, equilibria and kinetics,” BIOCHEMICAL ENGINEERING JOURNAL, pp. 193–204, 2002, Accessed: 00, 2020. [Online]. Available: https://hdl.handle.net/11511/38651.