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Amino acids precipitation

Novozymes, a subtilisin produced by Bacillus licheniformis, was used by Chen et al ° to carry out a dynamic kinetic resolution of benzyl, butyl, or propyl esters of DL-phenylalanine, tyrosine, and leucine. The hydrolysis was performed at pH 8.5 in 2-methyl-2-propanol/water (19 1) and the freed L-amino acids precipitated. The key feature bringing about continual racemization of the remaining D-amino acid esters was the inclusion of 20 mmol 1 pyridoxal phosphate. [Pg.84]

A series of a-aminoesters has been hydrolyzed to a-amino acids using alcalase in the presence of pyridoxal 5-phosphate[40). During the course of these reactions, the amino acids precipitated from the reaction mixture, thereby protecting them from racemisation. The method was used to prepare enantiomerically enriched phenylalanine, leucine, tryptophan and norvaline with high selectivity (Fig. 9-19). [Pg.301]

Pre-formed imino-esters have also been used as substrates for dynamic kinetic resolution reactions[42). The free amino acid precipitated from the reaction mixture as the reaction proceeded. [Pg.301]

Cal Kulis passed a renal stone shortly after admission, with immediate relief of flank pain. Stone analysis showed its major component to be cystine. Normally, amino acids are filtered by the renal glomerular capillaries into the tubular urine but are almost entirely reabsorbed from this fluid back into the blood via transport proteins in the proximal tubular cells of the kidney. Cal Kulis has cystinuria, a genetically inherited amino acid substitution in the transport protein that normally reabsorbs cystine, arginine, and lysine from the kidney lumen back into the renal tubular cells. Therefore, his urine contained high amounts of these amino acids. Cystine, which is less soluble than other amino acids, precipitates in the urine to form renal stones (calculi). [Pg.78]

The amino acid 3 has low solubility in water, although the compoimd itself binds water tightly. Elemental analysis of the amino acid fits the composition of the monohydrate, C5H4N4O2 H2O. If the acid hydrolysis reaction is neutralized with sodium bicarbonate, the sodium salt of the amino acid precipitates as a white solid. The analysis for this product fits that calculated for the hemihydrate. [Pg.102]

The enzyme-catalysed hydrolysis of SchifiF bases derived from racemic amino acid esters and aromatic aldehydes was studied by Parmar et al. The L-amino acid precipitated out from the solution as the reaction progressed and the liberated aldehyde and unhydrolysed o-ester remained in solution. [Pg.165]

B) Benzoyl derivatives. Most amino-acids can be benzoyl-ated when their solutions in 10% aqueous sodium hydroxide are shaken with a small excess of benzoyl chloride until a clear solution is obtained (Schotten-Baumann reaction, p. 243). Acidification of the solution then precipitates the benzoyl derivative and the excess of benzoic acid, and the mixture must be filtered off, washed with water, and recrystallised (usually from ethanol) to obtain the pure derivative. (M.ps., p. 555 )... [Pg.382]

An amino-acid, although insoluble in water (e.g., anthranilic acid), is usually soluble in excess of mineral acid in such a case it is important to make the solution only very slightly acid. This applies also to a mixture of a neutral and a basic substance, from which dil. HCl will extract an amino-acid the solution must then be carefully treated with NaOH to precipitate the amino-acid. [Pg.399]

To 5 ml. of water add 1-2 drops of the amine if the amine does not dissolve, add a drop or two of concentrated hydrochloric acid. Add 0-5-1 ml. of this amine solution to 2-3 ml. of the reagent an almost immediate precipitate indicates the presence of a primary amine. A slight turbidity indicates the presence of a primary amine as an impurity. (Primary aromatic amines generally require 2-3 minutes for the test. Urea and other amides, as well as amino acids, do not react.)... [Pg.421]

Amino acids react in alkaline solution with a-naphthyl isocyanate to yield the sodium salts of the corresponding a-naphthylureido acids, which remain in solution upon addition of a mineral acid, the ureido acid is precipitated. [Pg.437]

Dissolve 0 01 g. equivalent of the amino acid in 0 03 g. equivalent of N sodium hydroxide solution and cool to 5° in a bath of ice. Add, with rapid stirring, 0 -01 g. equivalent of 2 4-dichlorophenoxyacetyl chloride dissolved in 5 ml. of dry benzene at such a rate (5-10 minutes) that the temperature of the mixture does not rise above 15° if the reaction mixture gels after the addition of the acid chloride, add water to thin it. Remove the ice bath and stir for 2-3 hours. Extract the resulting mixture with ether, and acidify the aqueous solution to Congo red with dilute hydrochloric acid. Collect the precipitate by filtration and recrystallise it from dilute alcohol. [Pg.438]

The history of the discovery of amino acids is closely related to advances ia analytical methods. Initially, quantitative and qualitative analysis depended exclusively upon crystallization from proteia hydrolysates. The quantitative precipitation of several basic amino acids including phosphotungstates, the separation of amino acid esters by vacuum distillation, and precipitation by sulfonic acid derivatives were developed successively duriag the last century. [Pg.271]

Soybean Protein Isolates. Soybean protein isolates, having a protein content of >90 wt%, are the only vegetable proteins that are widely used in imitation dairy products (1). Most isolates are derived from isoelectric precipitation, so that the soybean protein isolates have properties that are similar to those of casein. They are insoluble at thek isoelectric point, have a relatively high proportion of hydrophobic amino acid residues, and are calcium-sensitive. They differ from casein in that they are heat-denaturable and thus heat-labile. The proteins have relatively good nutritional properties and have been increasingly used as a principal source of protein. A main deterrent to use has been the beany flavor associated with the product. Use is expected to increase in part because of lower cost as compared to caseinates. There has been much research to develop improved soybean protein isolates. [Pg.442]

Other immobilization methods are based on chemical and physical binding to soHd supports, eg, polysaccharides, polymers, glass, and other chemically and physically stable materials, which are usually modified with functional groups such as amine, carboxy, epoxy, phenyl, or alkane to enable covalent coupling to amino acid side chains on the enzyme surface. These supports may be macroporous, with pore diameters in the range 30—300 nm, to facihtate accommodation of enzyme within a support particle. Ionic and nonionic adsorption to macroporous supports is a gentle, simple, and often efficient method. Use of powdered enzyme, or enzyme precipitated on inert supports, may be adequate for use in nonaqueous media. Entrapment in polysaccharide/polymer gels is used for both cells and isolated enzymes. [Pg.291]

The alcoholic filtrate is evaporated to 50 cc., and 50 g. of barium hydroxide and 150 cc. of distilled water are added (Note 4). The mixture is refluxed for two hours and the excess barium hydroxide is precipitated with carbon dioxide. The barium carbonate is removed by filtration and washed with hot distilled water. A slight excess of sulfuric acid is added to the filtrate to liberate the amino acid from its barium salt, and an excess of barium carbonate is added to remove sulfate ion. The mixture is digested on the steam bath until effervescence ceases, and it is then filtered and the precipitate is washed with hot distilled water. The filtrate and washings are concentrated on the steam bath to a volume of 100 cc., decolorized with i g. of active carbon, filtered, and concentrated to the point of crystallization (about 25 cc.). The amino acid is precipitated by the addition of 150 cc. of absolute alcohol and the product is collected and washed with absolute alcohol. [Pg.5]

After the complete removal of halogen and metallic ions, the solution is concentrated to a volume of about 100 cc., and 300 cc. of absolute alcohol is added. Then the amino acid is precipitated by slowly adding 500 cc. of ether with stirring and cooling. [Pg.7]

The mixture is then cooled and sodium bisulfite added to decolorize. Recrystallization of the product from methanol gives about 8 g, MP 147° to 150°C. The /3-(3-amino-2,4,6-triiodophenyl)-0 -ethylpropionic acid may be purified further by precipitation of the morpholine salt from ether solution and regeneration of the free amino acid by treatment of a methanol solution of the morpholine salt with sulfur dioxide. The pure amino acid has the MP 155° to 156.5°C. [Pg.831]

A solution of 5.0 g of a-ethyl-(3-(aminophenyl)propionic acid in 100 ml of water containing 5 ml of concentrated hydrochloric acid was added over a period of h hour to a stirred solution of 3.2 ml of Iodine monochioride in 25 ml of water and 25 ml of concentrated hydrochloric acid heated to 60°C. After addition was complete, the heating was continued for h hour longer at 60° to 70°C. A black oil separated which gradually solidified. The mixture was then cooled and sodium bisulfite was added to decolorize. Recrystallization of the product from methanol gave about 8 g of a-ethyl-(3-(2,4,6-triiodo-3-aminophenyl-pro-pionic acid, MP 147° to 150°C. The product could be further purified by precipitation of its morpholine salt from ether solution and regeneration of the free amino acid by treatment of a methanol solution of the morpholine salt with sulfur dioxide. The pure amino acid had the MP 155° to 156.5°C (corr). [Pg.1564]

A solution of 257 g. (1.05 moles) of barium chloride dihydrate in about 500 cc. of hot water is added to the reaction mixture, with vigorous shaking, and the mixture is heated on a steam bath for one-half hour. A heavy precipitate of the barium salt of the amino acid separates at once. After cooling to room temperature, the barium salt is collected on a suction filter, transferred to a beaker, and washed with two 250-cc. portions of hot water (8o°). After drying at ioo°, the barium salt weighs 225-230 g. (80-82 per cent of the theoretical amount). [Pg.56]

Foods such as meat, fish, and some vegetables contain sulfur-bearing amino acids that form volatile sulfur compounds during processing and storage. When these compounds react with iron, a black precipitate forms on the container and in most instances darkens the food. A small piece of aluminum welded to the tinplate can has been used to prevent container corrosion and sulfide staining in commercially canned hams. In this case, the aluminum acts as a sacrificial anode and stops the reaction with tin and iron that otherwise could occur at the small exposed tinplate areas (14). [Pg.48]


See other pages where Amino acids precipitation is mentioned: [Pg.292]    [Pg.241]    [Pg.166]    [Pg.1702]    [Pg.292]    [Pg.241]    [Pg.166]    [Pg.1702]    [Pg.331]    [Pg.435]    [Pg.238]    [Pg.1284]    [Pg.528]    [Pg.206]    [Pg.433]    [Pg.303]    [Pg.359]    [Pg.203]    [Pg.20]    [Pg.99]    [Pg.178]    [Pg.503]    [Pg.5]    [Pg.338]    [Pg.1015]    [Pg.14]    [Pg.16]    [Pg.16]    [Pg.16]    [Pg.17]    [Pg.17]    [Pg.19]    [Pg.57]    [Pg.83]    [Pg.117]   
See also in sourсe #XX -- [ Pg.103 ]




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Acid precipitation

Acidic precipitation

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