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Purification of peroxidase enzyme from radish species in fast and high yield with affinity chromatography technique
Ist Teil von
Journal of chromatography. B, Analytical technologies in the biomedical and life sciences, 2019-05, Vol.1114-1115, p.86-92
Ort / Verlag
Netherlands: Elsevier B.V
Erscheinungsjahr
2019
Link zum Volltext
Quelle
Alma/SFX Local Collection
Beschreibungen/Notizen
In this study, an effective single step affinity method is presented for purifying plant peroxidase (POD) enzymes from radish species. This method make possible to purify the enzymes in high yield and purity. Briefly, 10 different 4-amino benzohydrazide derivatives were synthesized and identified as new competitive POD inhibitors. Then, these derivatives were coupled to Sepharose 4B-L-Tyrosine support matrix by diazotization to form the affinity gels. Purification factors were recorded as 54.8% yield - 665-fold, 33.8% yield - 613-fold, 22.7% yield - 595-fold, 34.4% yield - 781-fold, 40.9% yield - 282-fold for turnip (T-POD), black radish (BR-POD), daikon (D-POD), sweet radish (SR-POD) and kohlrabi radish, (KR-POD), respectively. It has also been shown that the affinity gels, which prepared using the 4-amino 3-bromo benzohydrazide and 4-amino 2-nitro benzohydrazide molecules, capable to purify all radish species POD enzymes in high purity and yield.
•10 different 4-amino benzohydrazide derivatives were synthesized and identified as new POD inhibitors.•These derivatives were coupled to Sepharose 4B-L-Tyrosine support matrix to form affinity gels.•The binding patterns for Sepharose-4B-L-Tyrosine-(1a-10a) affinity gels were controlled by FT-IR.•The radish peroxidases were purified in a single step with the prepared affinity gels.