Effect of pH and temperature on the ion-exchange isotherm of Cd(II) and Pb(II) on clinoptilolite

2006 ◽  
Vol 81 (6) ◽  
pp. 966-973 ◽  
Author(s):  
Maria Selene Berber-Mendoza ◽  
Roberto Leyva-Ramos ◽  
Pedro Alonso-Davila ◽  
Jovita Mendoza-Barron ◽  
Paola Elizabeth Diaz-Flores
Keyword(s):  
Ion Exchange ◽  
Effect Of Ph ◽  
Ion Exchange Isotherm

Synthesis, characterization and ion exchange isotherm of zeolite Y using Box–Behnken design

2016 ◽  
Vol 27 (2) ◽  
pp. 750-755 ◽  
Author(s):  
Adewolu Oyinade ◽  
Abdulsalami Sanni Kovo ◽  
Patrick Hill
Keyword(s):  
Ion Exchange ◽  
Zeolite Y ◽  
Box Behnken Design ◽  
Ion Exchange Isotherm

scholarly journals Potassium–Sodium Ion Exchange Isotherm of Crystalline Zirconium Arsenate

1978 ◽  
Vol 51 (2) ◽  
pp. 637-638 ◽  
Author(s):  
Junko Sugisawa ◽  
Takao Yonezawa ◽  
Kazunori Takaguchi ◽  
Isao Tomita
Keyword(s):  
Ion Exchange ◽  
Sodium Ion ◽  
Potassium Sodium ◽  
Ion Exchange Isotherm

Determination of the Competitive Ion Exchange Isotherms of Taurine and Glycine on D290 Resin by Inverse Method

2013 ◽  
Vol 800 ◽  
pp. 22-26
Author(s):  
Shu Juan Zhuang ◽  
Feng Song ◽  
Zhong Jun Fu
Keyword(s):  
Ion Exchange ◽  
Anion Exchange ◽  
Inverse Method ◽  
Exchange Resin ◽  
Anion Exchange Resin ◽  
Fixed Bed ◽  
Elution Curves ◽  
Ion Exchange Isotherm ◽  
Good Agreement

With the elution curves of glycine and taurine, the ion exchange isotherm parameters of glycine and taurine on D290 anion exchange resin are determined by the inverse method. In this work, with the multi-component competitive ion exchange isotherm and the equilibrium dispersion chromatographic model, the elution curves of glycine and taurine on D290 anionic fixed bed are fitted. The parameters of competitive isotherm are determined, Ktau is 2.55, Kgly is 1.65. The result s showed good agreement between the elute curves fitted by the model and the separation data which confirmed the validity of the model selected.Keywords-taurine; glycine;competitive isotherm;inverse method;

Purification and partial characterization of an exo-β-glucanase from the yeast Kluyveromyces aestuarii

1977 ◽  
Vol 55 (9) ◽  
pp. 1001-1006 ◽  
Author(s):  
Marc-André Lachance ◽  
Tomas G. Villa ◽  
Herman J. Phaff
Keyword(s):  
Molecular Weight ◽  
Ion Exchange ◽  
Polypeptide Chain ◽  
Activation Energies ◽  
Partial Characterization ◽  
Effect Of Ph ◽  
Single Polypeptide Chain ◽  
Exclusion Chromatography ◽  
Single Polypeptide

The intracellular–periplasmic exo-1,3-β-glucanase (EC 3.2.1.58) has been extracted from the yeast Kluyveromyces aestuarii and purified to immunoelectrophoretic homogeneity by ion-exchange and gel-exclusion chromatography. The kinetic constants and activation energies for laminarin, p-nitrophenyl-β-D-glucoside, and pustulan have been determined, along with the effect of pH. Evidence is presented indicating that the enzyme is composed of a single polypeptide chain, about 24% carbohydrates, and its molecular weight was estimated to be 43 000.

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