caa a22 4500 463156242 CHVBK 20180406164735.0 cr unu---uuuuu 170326e20070901xx s 000 0 eng 10.1007/s00217-006-0493-8 doi (NATIONALLICENCE)springer-10.1007/s00217-006-0493-8 Partial characterization of peroxidase from the leaves of thymbra plant ( Thymbra spicata L. var. spicata ) [Elektronische Daten] [Serap Doğan, Pınar Turan, Mehmet Doğan, Oktay Arslan, Mahir Alkan] Peroxidase (EC 1.11.1.7; donor: hydrogen-peroxide oxidoreductase) catalyses the oxidation of various electron donor substrates (e.g. phenols, aromatic amines). In this study, the peroxidase was extracted from Thymbra spicata L. var. spicata and, then partially purified with (NH4)2SO4 precipitation and dialysis. The substrate specificity of peroxidase was investigated using 2,2′-azino-bis(3-ethylbenz-thiazoline-6-sulfonic acid) (ABTS), o-dianisidine, o-phenylenediamine, catechol and guaiacol as substrates. Furthermore, the effects of buffer concentration, pH, temperature and thermal inactivation on enzyme activity were also studied. The results obtained have shown that (i) the best substrate is o-dianisidine, followed by ABTS, catechol, guaiacol and o-phenylenediamine, respectively; (ii) the best buffer concentration is 40mM for o-dianisidine and catechol, 10mM for ABTS and guaiacol, and 100mM for o-phenylenediamine; (iii) optimum pH is 2.5 for ABTS and o-phenylenediamine, 6.0 for o-dianisidine, and 7.0 for catechol and guaiacol; (iv) optimum temperature is 20°C for catechol, 40°C for ABTS, guaiacol and o-dianisidine, and 50°C for o-phenylenediamine; and (v) the enzyme activity in the thermal inactivation experiments was enhanced with increase in temperature with o-dianisidine as a substrate while its activity decreased with o-phenylenediamine. Springer-Verlag, 2006 Thymbra spicata L. var. spicata nationallicence Peroxidase nationallicence Thymbra leaves nationallicence pH nationallicence Thermal inactivation nationallicence Substrate specificity nationallicence Doğan Serap Department of Biology, Faculty of Science and Literature, Balikesir University, 10145, Balikesir, Turkey aut Turan Pınar Department of Chemistry, Faculty of Science and Literature, Balikesir University, 10145, Balikesir, Turkey aut Doğan Mehmet Department of Chemistry, Faculty of Science and Literature, Balikesir University, 10145, Balikesir, Turkey aut Arslan Oktay Department of Chemistry, Faculty of Science and Literature, Balikesir University, 10145, Balikesir, Turkey aut Alkan Mahir Department of Chemistry, Faculty of Science and Literature, Balikesir University, 10145, Balikesir, Turkey aut European Food Research and Technology Springer-Verlag 225/5-6(2007-09-01), 865-871 1438-2377 225:5-6<865 2007 225 217 https://doi.org/10.1007/s00217-006-0493-8 text/html Onlinezugriff via DOI 1 research-article jats NATIONALLICENCE 856 40 https://doi.org/10.1007/s00217-006-0493-8 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Doğan Serap Department of Biology, Faculty of Science and Literature, Balikesir University, 10145, Balikesir, Turkey aut NATIONALLICENCE 700 1- Turan Pınar Department of Chemistry, Faculty of Science and Literature, Balikesir University, 10145, Balikesir, Turkey aut NATIONALLICENCE 700 1- Doğan Mehmet Department of Chemistry, Faculty of Science and Literature, Balikesir University, 10145, Balikesir, Turkey aut NATIONALLICENCE 700 1- Arslan Oktay Department of Chemistry, Faculty of Science and Literature, Balikesir University, 10145, Balikesir, Turkey aut NATIONALLICENCE 700 1- Alkan Mahir Department of Chemistry, Faculty of Science and Literature, Balikesir University, 10145, Balikesir, Turkey aut NATIONALLICENCE 773 0- European Food Research and Technology Springer-Verlag 225/5-6(2007-09-01), 865-871 1438-2377 225:5-6<865 2007 225 217 Metadata rights reserved Springer special CC-BY-NC licence nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-springer