scholarly journals Decomposition of Oxalic Acid in Ginger Juice by Adding the Roots of Barley Seedlings Containing Oxalate Oxidase.

1999 ◽  
Vol 46 (5) ◽  
pp. 346-351 ◽  
Author(s):  
Sumitaka YAMASHITA ◽  
Akira KUBOTA ◽  
Naoko FUKAHORI
Keyword(s):  
2016 ◽  
Vol 63 (3) ◽  
Author(s):  
Marcin Grąz ◽  
Kamila Rachwał ◽  
Radosław Zan ◽  
Anna Jarosz-Wilkołazka

Oxalate oxidase was identified in mycelial extracts of a basidiomycete Abortiporus biennis strain. Intracellular enzyme activity was detected only after prior lowering of the pH value of the fungal cultures by using oxalic or hydrochloric acids. This enzyme was purified using size exclusion chromatography (Sephadex G-25) and ion-exchange chromatography (DEAE-Sepharose). This enzyme exhibited optimum activity at pH 2 when incubated at 40°C, and the optimum temperature was established at 60°C. Among the tested organic acids, this enzyme exhibited specificity only towards oxalic acid. Molecular mass was calculated as 58 kDa. The values of Km for oxalate and Vmax for the enzyme reaction were 0.015 M and 30 mmol min-1, respectively.


Euphytica ◽  
1995 ◽  
Vol 85 (1-3) ◽  
pp. 169-172 ◽  
Author(s):  
C. Thompson ◽  
J. M. Dunwell ◽  
C. E. Johnstone ◽  
V. Lay ◽  
J. Ray ◽  
...  

2013 ◽  
Vol 72 ◽  
pp. 96-101 ◽  
Author(s):  
Sandra Winestrand ◽  
Kristin Johansson ◽  
Lars Järnström ◽  
Leif J. Jönsson
Keyword(s):  

1980 ◽  
Vol 26 (7) ◽  
pp. 827-830 ◽  
Author(s):  
M F Laker ◽  
A F Hofmann ◽  
B J Meeuse

Abstract A novel spectrophotometric enzymic procedure for estimating oxalic acid in urine is described. Oxalate oxidase, prepared from moss species, converts oxalic acid to hydrogen peroxide and carbon dioxide. Hydrogen peroxide is determined enzymatically with horseradish peroxidase, by oxidative coupling of 3-methyl-2-benzothiazolinone hydrazone with N,N-dimethylaniline; the resulting indamine due is determined spectrophotometrically at 595 nm. Interfering substances are removed by adsorption to ion-exchange resins and oxidation with charcoal, thus avoiding oxalate recovery problems accompanying oxalate isolation. The procedure is rapid, sensitive, linear, and precise. Results agreed well with those obtained with a widely used chemical technique.


Author(s):  
Satabdi Ghosh ◽  
Debapriya Das ◽  
Piyali Nandy ◽  
Ankita Ray

Oxalate oxidase enzyme in monocotyledonous plants, act as a scavenger to breakdown oxalic acid into carbon dioxide and hydrogen peroxide. They perform several important functions in early plant defence responses, including induction of PR protein synthesis and systemic resistance. In the present study oxalic acid, the virulence factor of fungi, was applied to monocotyledonous plants and it was observed that it activates the innate host immune system, along with secretion of oxalate oxidase. The enzymatic activities of other host defence related enzymes like catalase, superoxide dismutase, ascorbic acid oxidase, phenolic content, phenylalanine ammonia lyase were compared between the control and oxalic acid treated (2mM) plants.


1980 ◽  
Vol 26 (7) ◽  
pp. 827-830 ◽  
Author(s):  
M F Laker ◽  
A F Hofmann ◽  
B J Meeuse

Abstract A novel spectrophotometric enzymic procedure for estimating oxalic acid in urine is described. Oxalate oxidase, prepared from moss species, converts oxalic acid to hydrogen peroxide and carbon dioxide. Hydrogen peroxide is determined enzymatically with horseradish peroxidase, by oxidative coupling of 3-methyl-2-benzothiazolinone hydrazone with N,N-dimethylaniline; the resulting indamine due is determined spectrophotometrically at 595 nm. Interfering substances are removed by adsorption to ion-exchange resins and oxidation with charcoal, thus avoiding oxalate recovery problems accompanying oxalate isolation. The procedure is rapid, sensitive, linear, and precise. Results agreed well with those obtained with a widely used chemical technique.


2000 ◽  
Vol 83 (5) ◽  
pp. 1212-1217 ◽  
Author(s):  
Stjepan Milardović ◽  
Zorana Grabarić ◽  
Mihael Tkalčec ◽  
Vlatko Rumenjak

Abstract A novel enzymatic amperometric method is described for the determination of oxalic acid in urine. An amperometric biosensor was made by immobilizing oxalate oxidase on the surface of a chromium(III) hexacyanoferrate-modified graphite electrode by using a bovine serum albumin and glutaraldehyde cross-linking procedure. The enzyme biocatalyzes oxalate decomposition in the presence of oxygen into carbon dioxide and hydrogen peroxide. The oxalate concentration, which is proportional to the amount of hydrogen peroxide, was determined amperometrically by measuring the current resulting in the reduction of hydrogen peroxide at a very low working potential (0.05 V versus the Hg | Hg2Cl2 | 3M KCl electrode), which minimized the influence of the possible interferences present in human urine. All experiments were performed with succinic buffer, pH 3.8, containing 0.1M KCl and 5.4mM ethylenediaminetetraacetic acid. In an aqueous solution of pure oxalic acid, the biosensor showed good linearity in a concentration range of 2.5–100μM without the use of a dialysis membrane. For untreated urine samples, a high correlation (R2 = 0.9949) was obtained between oxalate concentrations added to urine samples and oxalate recoveries calculated for determinations with the described oxalate biosensor.


Plant Science ◽  
2007 ◽  
Vol 172 (3) ◽  
pp. 488-496 ◽  
Author(s):  
Andreanna Jo Welch ◽  
Arthur John Stipanovic ◽  
Charles Alvin Maynard ◽  
William Allen Powell

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