scholarly journals The Biosynthesis of UDP-Galacturonic Acid in Plants. Functional Cloning and Characterization of Arabidopsis UDP-d-Glucuronic Acid 4-Epimerase

2004 ◽  
Vol 136 (4) ◽  
pp. 4256-4264 ◽  
Author(s):  
Xiaogang Gu ◽  
Maor Bar-Peled
Keyword(s):  
Galacturonic Acid ◽  
Glucuronic Acid

A uronic acid isomerase in Flavobacterium heparinum

1970 ◽  
Vol 48 (2) ◽  
pp. 164-169 ◽  
Author(s):  
James C. Karapally ◽  
Carl P. Dietrich
Keyword(s):  
Hyaluronic Acid ◽  
Equilibrium Point ◽  
Galacturonic Acid ◽  
Uronic Acid ◽  
Glucuronic Acid ◽  
Chondroitin Sulfates ◽  
Isolation And Characterization ◽  
Flavobacterium Heparinum

The isolation and characterization of a uronic acid isomerase from F. heparinum is described. The enzyme converts glucuronic acid and galacturonic acid to fructuronic acid and tagaturonic acid. The equilibrium point of the reaction is affected by buffers. In the presence of borate, 75% of glucuronic acid is converted to fructuronic acid. In the presence of phosphate, the equilibrium is reached when 31% of glucuronic acid is converted to fructuronic acid. Conversely, fructuronic acid and tagaturonic acid are converted to glucuronic acid and galacturonic acid, respectively. Monosaccharides derived from heparin and chondroitin sulfates do not affect the activity of the isomerase, in contrast to the monosaccharides from hyaluronic acid which have marked inhibitory (or diluting) activity upon the enzyme. The role of this enzyme in the metabolism of mucopolysaccharides is discussed.

scholarly journals Enzymatic Extraction and Characterization of Pectin from Cocoa Pod Husks (Theobroma cacao L.) Using Celluclast® 1.5 L

Molecules ◽  
2021 ◽  
Vol 26 (5) ◽  
pp. 1473
Author(s):  
Licelander Hennessey-Ramos ◽  
Walter Murillo-Arango ◽  
Juliana Vasco-Correa ◽  
Isabel Cristina Paz Astudillo
Keyword(s):  
Acid Content ◽  
Galacturonic Acid ◽  
Extraction Process ◽  
Chemical Extraction ◽  
Enzymatic Extraction ◽  
Acid Yield ◽  
Physicochemical Features ◽  
Enzyme Dosage ◽  
Cocoa Pod Husks

Cocoa pod husks are a waste generated during the processing of cocoa beans. We aimed to explore the enzymatic extraction of pectin using cellulases. The extraction process was optimized using a central composite design (CCD) and analyzed by response surface methodology (RSM). The parameters optimized were feedstock concentration (%), enzyme dosage (µL/g), and time (h). Three dependent variables were studied: pectin yield (g/100 g dry husk) (R2 = 97.02), galacturonic acid content (g/100 g pectin) (R2 = 96.90), and galacturonic acid yield (g/100 g feedstock) (R2 = 95.35). The optimal parameters were 6.0% feedstock concentration, 40 µL g−1 of enzyme, and 18.54 h, conditions that produced experimentally a pectin yield of 10.20 g/100 g feedstock, 52.06 g galacturonic acid/100 g pectin, and a yield 5.31 g galacturonic acid/100 g feedstock. Using the chemical extraction method, a yield of 8.08 g pectin/100 g feedstock and a galacturonic acid content of 60.97 g/100 g pectin were obtained. Using assisted sonication, a pectin yield of 8.28 g/100 g feedstock and a galacturonic acid content of 42.77 g/100 g pectin were obtained. Enzymatically optimized pectin has rheological and physicochemical features typical of this biomaterial, which provides an interesting alternative for the valorization of cocoa husks.

scholarly journals cDNA Isolation and Functional Characterization of UDP-d-glucuronic Acid 4-Epimerase Family from Ornithogalum caudatum

Molecules ◽  
2016 ◽  
Vol 21 (11) ◽  
pp. 1505 ◽  
Author(s):  
Sen Yin ◽  
Yu-Jia Sun ◽  
Ming Liu ◽  
Li-Na Li ◽  
Jian-Qiang Kong
Keyword(s):  
Glucuronic Acid ◽  
Functional Characterization ◽  
Cdna Isolation ◽  
Ornithogalum Caudatum

scholarly journals Functional Cloning and Expression of the Schizophyllum commune Glucuronoyl Esterase Gene and Characterization of the Recombinant Enzyme

2012 ◽  
Vol 2012 ◽  
pp. 1-7 ◽  
Author(s):  
Dominic W. S. Wong ◽  
Victor J. Chan ◽  
Amanda A. McCormack ◽  
Ján Hirsch ◽  
Peter Biely
Keyword(s):  
Glucuronic Acid ◽  
Active Form ◽  
Schizophyllum Commune ◽  
Constitutive Expression ◽  
Recombinant Enzyme ◽  
Cloning And Expression ◽  
Gene Encoding ◽  
Glucuronoyl Esterase ◽  
Esterase Gene

The gene encoding Schizophyllum commune glucuronoyl esterase was identified in the scaffold 17 of the genome, containing two introns of 50 bp and 48 bp, with a transcript sequence of 1179 bp. The gene was synthesized and cloned into Pichia pastoris expression vector pGAPZα to achieve constitutive expression and secretion of the recombinant enzyme in soluble active form. The purified protein was 53 kD with glycosylation and had an acidic pI of 3.7. Activity analysis on several uronic acids and their derivatives suggests that the enzyme recognized only esters of 4-O-methyl-D-glucuronic acid derivatives, even with a 4-nitrophenyl aglycon but did not hydrolyze the ester of D-galacturonic acid. The kinetic values were Km 0.25 mM, Vmax 16.3 μM⋅min−1, and kcat 9.27 s−1 with 4-nitrophenyl 2-O-(methyl 4-O-methyl-α-D-glucopyranosyluronate)-β-D-xylopyranoside as the substrate.

Characterization of glucuronic acid containing glycolipid in Aspergillus fumigatus mycelium

2009 ◽  
Vol 344 (15) ◽  
pp. 1960-1967 ◽  
Author(s):  
Thierry Fontaine ◽  
Claude Lamarre ◽  
Catherine Simenel ◽  
Karine Lambou ◽  
Bernadette Coddeville ◽  
...  
Keyword(s):  
Aspergillus Fumigatus ◽  
Glucuronic Acid

Characterization of a mucoid Escherichia coli K12 strain, and chemical analysis of the exopolysaccharide

1972 ◽  
Vol 18 (7) ◽  
pp. 969-973 ◽  
Author(s):  
Stephen Shugar ◽  
Kenneth E. Sanderson
Keyword(s):  
Escherichia Coli ◽  
Chemical Analysis ◽  
Glucuronic Acid ◽  
Extracellular Polysaccharide ◽  
Spontaneous Mutant ◽  
Escherichia Coli K12 ◽  
Molar Ratios ◽  
Genetic Lesion ◽  
Long Form

A spontaneous mutant of Escherichia coli K12 C600 was isolated which is mucoid as a result of overproduction of an extracellular polysaccharide. This strain also forms filaments, is sensitive to ultraviolet irradiation, and has its genetic lesion closely linked to the lac gene. Its phenotype and map position are analogous to the lon mutation (long form). The exopolysaccharide contains fucose, glucose, galactose, and may contain glucuronic acid, but the molar ratios of these sugars differ from those previously reported.

Isolation and Characterization of Glucuronic Acid Conjugates of Chlorpromazine in Human Urine

1959 ◽  
Vol 102 (3) ◽  
pp. 602-605 ◽  
Author(s):  
T. H. Lin ◽  
L. W. Reynolds ◽  
I. M. Rondish ◽  
E. J. Van Loon
Keyword(s):  
Human Urine ◽  
Glucuronic Acid ◽  
Isolation And Characterization

scholarly journals The glycosylation of Bowes melanoma tissue plasminogen activator: lectin mapping, reaction with anti-L2/HNK-1 antibodies and the presence of sulphated/glucuronic acid containing glycans

1996 ◽  
Vol 316 (2) ◽  
pp. 427-437 ◽  
Author(s):  
A. J. JAQUES ◽  
G. OPDENAKKER ◽  
T. W. RADEMACHER ◽  
R. A. DWEK ◽  
S. E. ZAMZE
Keyword(s):  
Cell Line ◽  
Plasminogen Activator ◽  
Tissue Plasminogen Activator ◽  
Glucuronic Acid ◽  
Gel Filtration ◽  
Lectin Affinity Chromatography ◽  
Tissue Plasminogen ◽  
A Cell ◽  
Neuroectodermal Origin

The glycosylation of tissue plasminogen activator (t-PA) obtained from the Bowes melanoma cell line was re-examined using methods of serial lectin affinity chromatography coupled with Bio-Gel P-4 gel filtration chromatography and exoglycosidase sequencing. This study clarified an earlier discrepancy in the literature and confirmed that the major complex N-linked glycans on Bowes t-PA that carry sialic acid as their sole charged group are bi-antennary, core fucosylated, with terminal N-acetylgalactosamine residues. We also report the characterization of a series of related and previously unidentified sialylated glycans. Further we show that Bowes t-PA expresses glucuronic acid/sulphate containing N-linked glycans and is recognized by anti-carbohydrate L2/HNK-1 monoclonal antibodies. The presence on Bowes t-PA of glycans associated primarily with the nervous system is consistent with its expression in a cell line of neuroectodermal origin.

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