Equilibrium sorption of amino acids by a cation-exchange resin

1990 ◽  
Vol 29 (5) ◽  
pp. 849-857 ◽  
Author(s):  
Susan R. Dye ◽  
Joseph P. DeCarli ◽  
Giorgio Carta
Keyword(s):  
Amino Acids ◽  
Cation Exchange ◽  
Exchange Resin ◽  
Cation Exchange Resin ◽  
Equilibrium Sorption

Kinetics of LIS-100 Cation Exchange Resin to Remove Reaction Substrate of Non-Enzymatic Browning in Clarified Apple Juice

2013 ◽  
Vol 699 ◽  
pp. 770-774
Author(s):  
Jian Hua Yi ◽  
Mei Li Li ◽  
Zhen Bao Zhu
Keyword(s):  
Amino Acids ◽  
Cation Exchange ◽  
Apple Juice ◽  
Exchange Resin ◽  
Cation Exchange Resin ◽  
Enzymatic Browning ◽  
Adsorption Parameters ◽  
Cation Exchange Resins ◽  
Exchange Resins ◽  
Dynamic Exchange

In order to inhibit non-enzymatic browning in clarified Fuji apple juice during storage, four kinds of cation exchange resins were compared for their abilities to exchange and remove amino acids, the reaction substrates of non-enzymatic browning in apple juice. The favorite resin, LSI-100, was screened to carry out static and dynamic adsorption experiments. The results showed that LSI-100 cation exchange resin had the best capacity for adsorption and removal amino acids. The equilibrium time of LSI-100 resin for amino acids was 3.5h.And the isotherm of LSI-100 resin could be described by Freundlich at 20°C. Additionally, the flow rates, temperature and concentrations of amino acids in apple juice affected the dynamic kinetic curves of LSI-100 cation exchange resin and the better dynamic exchange and adsorption parameters were as follows: flow rate 4BV/h, temperature 50°C,and amino acid concentration 30mg/100g apple juice.

scholarly journals A Semi-Automated Bone Pretreatment System and the Pretreatment of Older and Contaminated Samples

Radiocarbon ◽  
1989 ◽  
Vol 31 (03) ◽  
pp. 247-253 ◽  
Author(s):  
I A Law ◽  
R E M Hedges
Keyword(s):  
Amino Acids ◽  
Cation Exchange ◽  
Continuous Flow ◽  
Exchange Resin ◽  
Flow System ◽  
Cation Exchange Resin ◽  
Flow Cells ◽  
Continuous Flow System ◽  
New Process ◽  
Degree Of Purification

A semi-automated continuous-flow system used to process archaeological bone to purified gelatin or amino acids for 14C dating is described. Powdered bone is retained in flow cells specifically designed to permit the sequential leaching of the bone with acid, alkali and water. Crude collagen obtained by this process is gelatinized, and than either purified directly using a macroporous cation exchange resin (BioRad AGMP-50), or hydrolyzed and the amino acids desalted on BioRad 50W-X8 resin. When compared with previous methods used by the laboratory, the new method allows more samples to be treated to a higher degree of purification. Examples of dates obtained on “standard” bones are presented, and confirm that no contamination is introduced from the components used in the new process.

scholarly journals Isolation of bacilysin and a new amino acid from culture filtrates of Bacillus subtilis

1970 ◽  
Vol 118 (4) ◽  
pp. 557-561 ◽  
Author(s):  
J. E. Walker ◽  
E. P. Abraham
Keyword(s):  
Amino Acids ◽  
Bacillus Subtilis ◽  
Amino Acid ◽  
Glutamic Acid ◽  
Cation Exchange ◽  
Exchange Resin ◽  
Cation Exchange Resin ◽  
Neutral Amino Acids ◽  
Peptide Fraction ◽  
Neutral Peptide

1. Bacilysin, a labile dipeptide antibiotic that lyses growing staphylococci, was isolated from culture fluids of Bacillus subtilis by a process giving higher yields than those previously obtained. 2. The process involves adsorption on a cation-exchange resin and elution with aqueous trimethylamine, separation from neutral amino acids and glutamic acid by chromatography on DEAE-Sephadex at pH8.7 and separation from other neutral peptides by chromatography in aqueous propan-2-ol on Sephadex G-25. 3. A new amino acid, which is chemically related to bacilysin, was isolated from the fraction containing neutral amino acids. 4. Two substances that yield alanine on hydrolysis, in addition to bacilysin, were obtained from the neutral peptide fraction.

Chromatographic behaviour of amino acids on cation-exchange resin-coated chromatosheets in the H+ form

1974 ◽  
Vol 102 ◽  
pp. 245-249 ◽  
Author(s):  
I. Hazai ◽  
S. Zoltán ◽  
J. Salát ◽  
S. Ferenczi ◽  
T. Dévényi
Keyword(s):  
Amino Acids ◽  
Cation Exchange ◽  
Exchange Resin ◽  
Cation Exchange Resin ◽  
Chromatographic Behaviour

The non-protein nitrogen composition of grass silages: I. The estimation of the basic amino acids and non-volatile amines by chromatography on a weak cation exchange resin

1969 ◽  
Vol 72 (3) ◽  
pp. 459-466 ◽  
Author(s):  
A. D. Hughes
Keyword(s):  
Amino Acids ◽  
Ion Exchange ◽  
Cation Exchange ◽  
Exchange Resin ◽  
Cation Exchange Resin ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Protein Nitrogen ◽  
Weak Cation Exchange

SUMMARYInvestigations into the non-protein nitrogen composition of grass silages using the 50 cm strong cation-exchange column of Spackman, Stein & Moore (1958) to determine the basic amino acids led to difficulties in the determination of ethanolamine in the presence of high concentrations of ammonia, and of histidine in the presence of δ amino-n-valeric acid. An alternative technique for the ion exchange chromatography and estimation of histidine, lysine, ornithine, ethanolamine, arginine and ammonia on a weak cation-exchange resin has been developed. This method enables small amounts of ethanolamine to be determined in the presence of large amounts of ammonia and values for the ethanolamine content of a number of silage samples are presented. When used in conjunction with the technique of Spackman et al. (1958) the δ-amino-n-valeric acid content of grass silages could also be determined in the presence of histidine.The estimation of amines produced by the microbial decomposition of herbage proteins during ensiling has previously involved their initial separation from the amino acids followed by quantitative partition chromatography. An alternative method for the estimation of these amines by ion-exchange chromatography on a weak cation-exchange resin is described. This method permits the colorimetric determination of β-phenylethylamine, tyramine, tryptamine, 5-hydroxytryptamine, putrescine, cadaverine and histamine without interference from the amino acids. The efficiency of this technique has been investigated using standard solutions of the naturally occurring amines and samples of good quality and of high pH spoilt silages.

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