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

Date

2002-12-01

Author

Çalık, Pınar
Calik, G
Ozdamar, TH

Metadata

Show full item record

This work is licensed under a Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International License.

Item Usage Stats

91
views

0
downloads

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.

Subject Keywords

Serine alkaline protease, Separation, Ion exchange, Enzyme-ion-exchanger interactions, Theory, Equilibrium, Kinetics, Fermentation

URI

https://hdl.handle.net/11511/38651

Journal

BIOCHEMICAL ENGINEERING JOURNAL

DOI

https://doi.org/10.1016/s1369-703x(02)00069-4

Collections

Department of Chemical Engineering, Article

Suggestions

OpenMETU
Core

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...
Purification and characterization of an intracellular chymotrypsin-like serine protease from Thermoplasma volcanium Kocabıyık, Semra (2006-01-01) An intracellular serine protease produced by Thermoplasma (Tp.) voleanium was purified using a combination of ammonium sulfate fractionation, ion exchange, and et-casein agarose affinity chromatography. This enzyme exhibited the highest activity and stability at pH 7.0, and at 50 degrees C. The purifed enzyme hydrolyzed synthetic peptides preferentially at the carboxy terminus of phenylalanine or leucine and was almost completely inhibited by PMSF, TPCK, and chymostatin, similarly to a chymotrypsin-like ser...
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...
Enzyme-catalyzed resolution of aromatic ring fused cyclic tertiary alcohols Ozdemirhan, Devrim; Sezer, Serdar; Sonmez, Yasemin (Elsevier BV, 2008-12-01) An efficient chemoenzymatic route for the synthesis of optically active aromatic ring fused cyclic tertiary alcohols (S)-(-)-1-methyl-1,2,3,4-tetrahydronaphthalen-1-ol (-)-1b and (S)-(+)-1-methyl-2,3-dihydro-1H-inden-1-ol (+)-1a has been developed. Different lipases have been tested in the transesterification of these tertiary alcohols; CAL-A (Candida antarctica Lipase A) was found to be the best biocatalyst for 1b and CAL-A-CLEA (Lipase A, C. antarctica, cross-linked enzyme aggregate) for la, obtained with...

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.