Published February 28, 2022
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Fig. 3. A in Structure and activity of a novel robust peroxidase from Alkanna frigida cell culture
Authors/Creators
- 1. , Ali Asghar Karkhane & , Javad Zamani Amirzakaria & , & , Jaleh Ghashghaie & * & National Institute for Genetic Engineering and Biotechnology, Tehran, Iran
Description
Fig. 3. A) The 2-D gel IEF of POXalf. B) Optimal pH of activity, C) optimal temperature of activity, and D) the thermal stability of POXalf in the presence of phenol (●) and guaiacol (▴). The average of triple assays of POXsolution (stored at 4 ◦ C) activity in the presence of phenol on E) day 1 and F) day 720. All the phenol (8.6 mM) alf and guaiacol (5 mM) reactions were carried out in PBS (10 mM) in the presence of constant amounts of POXalf (65.35 nM) and H2O2 (6.76 mM). Constant pH of 7 and 6 (for phenol and guaiacol, respectively) and constant temperature (20 ± 1 ◦ C) were applied when needed. POXwas maintained 10 min at the desired pH and alf temperature prior to the assays for the stability examinations.
Notes
Published as part of Asl, Saeed Soleimani, Karkhane, Ali Asghar, Amirzakaria, Javad Zamani, Noghabi, Kambiz Akbari, Ghashghaie, Jaleh & haghbeen, Kamahldin, 2022, Structure and activity of a novel robust peroxidase from Alkanna frigida cell culture, pp. 113022 in Phytochemistry (113022) 194 on page 4, DOI: 10.1016/j.phytochem.2021.113022, http://zenodo.org/record/8160531
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- Journal article: 10.1016/j.phytochem.2021.113022 (DOI)
- Journal article: urn:lsid:plazi.org:pub:FFFFFFB01A1CFF87FF96FFFBFFB9FF90 (LSID)
- Journal article: https://zenodo.org/record/8160531 (URL)