PHOTOSYNTHESIS AND METABOLISM OF MARINE ALGAE: II. A SURVEY OF RATES AND PRODUCTS OF PHOTOSYNTHESIS IN C14O2

1958 ◽  
Vol 36 (3) ◽  
pp. 337-349 ◽  
Author(s):  
R. G. S. Bidwell
Keyword(s):  
Amino Acids ◽  
Paper Chromatography ◽  
Brown Algae ◽  
Marine Algae ◽  
Main Product ◽  
Fresh Plant ◽  
Continuous Record ◽  
Special Apparatus ◽  
Hydrolysis Of

The rates and products of photosynthesis of 14 species of brown, red, and green marine algae have been determined. C14O2 was supplied in a special apparatus which gave a continuous record of uptake. This apparatus is described in detail. The products of photosynthesis were extracted, separated by paper chromatography, and their radioactivity was determined. The main product was invariably mannitol in the brown algae, floridoside or a glycerol-mannoside in the reds, and sucrose in the greens. Hydrolysis of the insoluble residues released radioactive amino acids, glucose, galactose, and other carbohydrates. Although the soluble products were characteristic of each group, the insoluble products were much the same in all three groups. The rates of CO2 assimilation ranged from [Formula: see text] to 4 mg. of CO2 per hour per gram of fresh plant. No correlation of the rate of CO2 uptake was observed with either the morphology or the taxonomy of the algae.

D-Mannitol Interferes with Amino Acid Analysis of Marine Organisms

1979 ◽  
Vol 36 (9) ◽  
pp. 1134-1137 ◽  
Author(s):  
W. Fong ◽  
R. K. O'dor
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Acid Hydrolysis ◽  
Key Words ◽  
Amino Acid Analysis ◽  
Chromatographic Analysis ◽  
Marine Algae ◽  
Protein S ◽  
New Compounds ◽  
Hydrolysis Of

Acid hydrolysis of a protein in the presence of D-mannitol, a common constituent of marine algae, can cause significant reductions in the recovery of a number of amino acids. The new compounds formed by the interactions of D-mannitol and these amino acids may interfere in the chromatographic analysis of other amino acids. The recoveries of most of the amino acids appear to be either directly or inversely proportional to the amount of D-mannitol added to a protein sample before acid hydrolysis. These results suggest that it is necessary to determine the effects of contaminants in a sample of protein(s) on the recoveries of amino acids during routine acid hydrolysis. Key words: kelp, amino acids, carbohydrates, D-mannitol

Chemo-Enzymatic Syntheses of Both Enantiomers of Neodictyoprolenol and Neodictyoprolene; Possible Biosynthetic Intermediates of Sex Pheromones in Brown Algae

1999 ◽  
Vol 54 (12) ◽  
pp. 1027-1032 ◽  
Author(s):  
Yuuko Yamamoto ◽  
Yoshihiko Akakabe ◽  
Kenji Matsui ◽  
Hiroshi Shimidzu ◽  
Tadahiko Kajiwara
Keyword(s):  
Brown Algae ◽  
Sex Pheromones ◽  
Marine Algae ◽  
Enantiomeric Excess ◽  
Optical Resolution ◽  
Novozym 435 ◽  
Candida Sp ◽  
Hydrolysis Of ◽  
Enzymatic Methods

Neodictyoprolenol [(-)-(S)-(1,5Z,8Z)-undecatrien-3-ol], dictyoprolenol [(-)-(S )-(1,5Z)- undecadien-3-ol] and their acetates neodictyoprolene [(+)-(5)-3-acetoxy-(1,5Z,8Z)-undecatriene] and dictyoprolene [(+)-(S)-3-acetoxy-(1,5Z)-undecadiene], which are interesting as possible biosynthetic intermediates of the sex pheromones (dictyopterene B, C′ and D′) of brown algae, were synthesized by chemo-enzymatic methods through optical resolution of racemic neodictyoprolenol and dictyoprolenol using two lipases; Amano PS (Pseudom onas sp.) and Novozym 435® (Candida sp.). A combination of acylation of the alcohols and hydrolysis of the acetates by Novozym 435® produced neodictyoprolenol, neodictyoprolene, dictyoprolenol and dictyoprolene with high optical purities over 99% enantiomeric excess (e.e.). This snythetic methods will make it easier to search these compounds in marine algae and to study their biosynthesis.

Deinking of recycled paper by coupling of the enzyme endo-β-1,4-D-glucanasa and the cellulose, and by using a laboratory flotation column

MRS Advances ◽  
2020 ◽  
Vol 5 (52-53) ◽  
pp. 2669-2678
Author(s):  
Jeovani González P. ◽  
Ramiro Escudero G
Keyword(s):  
Amino Acids ◽  
Sodium Hydroxide ◽  
Paper Industry ◽  
Computational Simulation ◽  
Cellulose Fibers ◽  
Residual Water ◽  
Chemical Reagent ◽  
Recycled Paper ◽  
Flotation Column ◽  
Hydrolysis Of

AbstractDeinking of recycled office (MOW) paper was carried out by using a flotation column and adding separately sodium hydroxide, and the enzyme Cellulase Thricodema Sp., as defibrillators.The de-inked cellulose fibers were characterized according to the standards of the paper industry, to compare the efficiency of the deinking of each chemical reagent used to hydrolyze the fibers and defibrillate them.The computational simulation of the molecular coupling between the enzyme and cellulose was performed, to establish the enzyme-cellulose molecular complex and then to identify the principal amino-acids of endo-β-1,4-D-glucanase in this molecular link, which are responsible for the hydrolysis of the cellulose.Experimental results show the feasibility to replace sodium hydroxide with the enzyme Cellulase Thricodema Sp., by obtaining deinked cellulose with similar optical and physical properties.The use of the enzyme instead of sodium hydroxide avoids the contamination of the residual water; in addition to that, the column is operated more easily, taking into consideration that the pH of the system goes from alkaline to neutral.

Studies on Chromatographic Fractioning by Cations Exchangers of a Bovine Hemoglobin Hydrolysate

2018 ◽  
Vol 69 (10) ◽  
pp. 2794-2798
Author(s):  
Alina Diana Panainte ◽  
Ionela Daniela Morariu ◽  
Nela Bibire ◽  
Madalina Vieriu ◽  
Gladiola Tantaru ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Amino Acids ◽  
Retention Time ◽  
Chromatographic Separation ◽  
Bovine Hemoglobin ◽  
Reverse Phase ◽  
Hplc System ◽  
Fast Flow ◽  
Hydrolysis Of ◽  
Phase Column

A peptidic hydrolysate has been obtained through hydrolysis of bovine hemoglobin using pepsin. The fractioning of the hydrolysate was performed on a column packed with CM-Sepharose Fast Flow. The hydrolysate and each fraction was filtered and then injected into a HPLC system equipped with a Vydak C4 reverse phase column (0.46 x 25 cm), suitable for the chromatographic separation of large peptides with 20 to 30 amino acids. The detection was done using mass spectrometry, and the retention time, size and distribution of the peptides were determined.

scholarly journals The α-Chymotrypsin-catalyzed Hydrolysis of Esters of α-Amino Acids

1972 ◽  
Vol 247 (18) ◽  
pp. 5746-5752
Author(s):  
Ferenc J. Kézdy ◽  
Satya P. Jindal ◽  
Myron L. Bender
Keyword(s):  
Amino Acids ◽  
Hydrolysis Of Esters ◽  
Hydrolysis Of

Availability of amino acids supplied by constant intravenous infusion of synthetic dipeptides in healthy man

1989 ◽  
Vol 76 (6) ◽  
pp. 643-648 ◽  
Author(s):  
S. Albers ◽  
J. Wernerman ◽  
P. Stehle ◽  
E. Vinnars ◽  
P. Fürst
Keyword(s):  
Amino Acids ◽  
Free Amino Acids ◽  
Free Amino ◽  
Metabolic Clearance ◽  
Amino Acid Solution ◽  
Appreciable Change ◽  
Total Body ◽  
Hydrolysis Of ◽  
Firm Evidence ◽  
Apparently Healthy

1. A commercial amino acid solution supplemented with two synthetic dipeptides, l-alanyl-l-glutamine (Ala-Gln) and glycyl-l-tyrosine (Gly-Tyr), or alternatively with isonitrogenous amounts of free alanine and glycine has been continuously infused over 4 h in six apparently healthy volunteers. 2. The infusion of the solutions was not accompanied by any side effects and the volunteers reported no complaints. 3. Infusion of the alanine- and glycine-supplemented control solution resulted in an increase of the concentration of these amino acids, while no appreciable change in free glutamine concentration was observed and free tyrosine revealed a steady decrease throughout the infusion. 4. Infusion of the peptide-supplemented solution resulted in a prompt equimolar liberation of the constituent free amino acids (glutamine, alanine, tyrosine and glycine), approaching steady state after about 30 min infusion, while only trace but stable concentrations of the two dipeptides were measured throughout the infusion. No peptides were detectable in urine. The findings suggest a nearly quantitative extracellular hydrolysis of the infused dipeptides and indicate a subsequent utilization of the liberated free amino acids. 5. The estimated metabolic clearance rates and total body plasma clearances were very similar for the two dipeptides (Ala-Gln 35.9 ± 9.5 ml min−1 kg−1 and 2.9 ± 0.9 1/min, respectively; Gly-Tyr 33.7 ± 9.5 ml min−1 kg−1 and 2.7 ± 0.9 1/min, respectively); thus there is little difference in the metabolic handling of these dipeptides. 6. The study provides firm evidence that the synthetic dipeptides Ala-Gln and Gly-Tyr are quantitatively hydrolysed and that these peptides can be used as a safe and efficient source of free glutamine and tyrosine as part of a commercial solution.

PAPER CHROMATOGRAPHY OF COMPLEX BIOLOGICAL MATERIALS BY SOLVENT REDEVELOPMENT WITHOUT PRIOR REMOVAL OF SALTS OR PROTEINS

1960 ◽  
Vol 38 (10) ◽  
pp. 1137-1147 ◽  
Author(s):  
Arthur E. Pasieka
Keyword(s):  
Amino Acids ◽  
Paper Chromatography ◽  
Filter Paper ◽  
Complex Mixtures ◽  
Two Dimensional ◽  
One Dimensional ◽  
Equivalent Time ◽  
Biological Compounds ◽  
High Concentrations ◽  
Subsequent Staining

A solvent redeveloping technique has been devised by which amino acids, peptides, and sugars can be separated from complex mixtures in the presence of high concentrations of salts and proteins. The separations are effected by two to four successive 18-hour solvent developments with drying between each 18-hour period before subsequent staining of the chromatograms. Better separations and resolutions are obtained by such successive 18-hour solvent developments than by one continuous solvent development for an equivalent time. The effect of these redevelopments on the separations and resolutions of biological compounds is illustrated at various stages by photographs of one- and two-dimensional chromatograms. The redevelopment technique requires filter paper sheets up to 4 ft in length for one-dimensional analytical and preparative types of chromatograms.

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