期刊
PROTEIN AND PEPTIDE LETTERS
卷 15, 期 4, 页码 320-326出版社
BENTHAM SCIENCE PUBL LTD
DOI: 10.2174/092986608784246506
关键词
cauliflower; Brassica oleracea; peroxidase; enzyme purification; chromatography
Peroxidases (EC 1.11.1.7; donor: hydrogen peroxide oxidoreductase) are part of a large group of enzymes. In this study, peroxidase, a primer antioxidant enzyme, was purified with 19.3 fold and 0.2% efficiency from cauliflower (Brassica oleracea L.) by ammonium sulphate precipitation, dialysis, CM-Sephadex ion-exchange chromatography and Sephadex G-25 purification steps. The substrate specificity of peroxidase was investigated using 2,2'-azino-bis 3-ethylbenz-thiazoline-6-sulphonic acid) (ABTS), 2-methoxyphenol (guaiacol), 1,2-dihydroxybenzene (catechol), 1,2,3-trihyidroxybenzene (pyrogallol) and 4-methylcatechol. Also, optimum pH, optimum temperature, optimum ionic strength, stable pH, stable temperature, thermal inactivation conditions were determined for guaiacol/H2O2, pyrogallol/H2O2, ABTS/H2O2, catechol/H2O2 and 4-methyl catechol/ H2O2 substrate patterns. The molecular weight (M-w) of this enzyme was found to be 44 kDa by gel filtration chromatography method. Native polyacrylamide gel electrophoresis (PAGE) was performed for isoenzyme determination and a single band was observed. K-m and V-max values were calculated from Lineweaver-Burk graph for each substrate patterns.
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