期刊
INTERNATIONAL JOURNAL OF FOOD SCIENCE AND TECHNOLOGY
卷 47, 期 9, 页码 1872-1881出版社
WILEY
DOI: 10.1111/j.1365-2621.2012.03044.x
关键词
Bambusa oldhamii; characterisation; peroxidase isoforms; purification
资金
- National Science Council of the Republic of China (Taiwan) [NSC-94-2321-B-126-001]
Three isoforms of peroxidase (POD) were isolated from the sheaths of bamboo shoots by chromatofocusing on Polybuffer exchanger PBE 94. POD-A was partially purified, and POD-B and POD-C were purified and characterised. POD-A was a basic peroxidase, whereas POD-B and POD-C were acidic peroxidases with different isoelectric points. Using o-phenylenediamine (OPD) as a hydrogen-donor, the optimum temperatures for function of POD-B and POD-C were 55 and 45-55 degrees C, respectively, while both had the same optimum pH of 4.5. Both isoforms were stable between 30 and 60 degrees C and between pH 4.5 and 10. The activities of the POD isoforms towards hydrogen-donors were both pH and concentration dependent. Under optimal conditions, POD-B and POD-C catalysed the oxidation of catechol, pyrogallol, and OPD at higher rates than guaiacol, o-dianisidine and 2, 2-azino-bis- (3-ethylbenzothiazoline-6-sulphonic acid). Both isoforms were almost completely inhibited by chemical modification reagent diethyl pyrocarbonate (4.5 mM).
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