<HashMap><database>biostudies-literature</database><scores/><additional><omics_type>Unknown</omics_type><volume>9</volume><submitter>Zhao Y</submitter><pubmed_abstract>Previously, a new copper-zinc SOD (CuZnSOD) isolated from chestnut rose (&lt;i>Rosa roxburghii&lt;/i>) with good stability was described. In this study, the biosynthetic approach was used to create recombinant CuZnSOD. RACE PCR was also used to amplify the full-length CuZnSOD gene from chestnut rose, and the ORF segment was expressed in &lt;i>E. coli&lt;/i> BL21 and &lt;i>P. pastoris&lt;/i> GS115. For characterization, the enzyme was isolated in two steps in &lt;i>E. coli&lt;/i> and one step in &lt;i>P. pastoris&lt;/i>. The biochemical properties of the two recombinant enzymes were similar, and their optimal reaction pH and temperature were 6.0 and 50°C, respectively. According to molecular dynamics simulation, the CuZnSOD showed high stability from 70 to 90°C, and eight amino acids are important for enzyme thermal sta</pubmed_abstract><journal>Frontiers in nutrition</journal><pagination>850824</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC8959677</full_dataset_link><repository>biostudies-literature</repository><pubmed_title>Production of a Novel Superoxide Dismutase by &lt;i>Escherichia coli&lt;/i> and &lt;i>Pichia pastoris&lt;/i> and Analysis of the Thermal Stability of the Enzyme.</pubmed_title><pmcid>PMC8959677</pmcid><pubmed_authors>Zhang W</pubmed_authors><pubmed_authors>Zhao L</pubmed_authors><pubmed_authors>Liao X</pubmed_authors><pubmed_authors>Wang Y</pubmed_authors><pubmed_authors>Rao L</pubmed_authors><pubmed_authors>Zhao Y</pubmed_authors></additional><is_claimable>false</is_claimable><name>Production of a Novel Superoxide Dismutase by &lt;i>Escherichia coli&lt;/i> and &lt;i>Pichia pastoris&lt;/i> and Analysis of the Thermal Stability of the Enzyme.</name><description>Previously, a new copper-zinc SOD (CuZnSOD) isolated from chestnut rose (&lt;i>Rosa roxburghii&lt;/i>) with good stability was described. In this study, the biosynthetic approach was used to create recombinant CuZnSOD. RACE PCR was also used to amplify the full-length CuZnSOD gene from chestnut rose, and the ORF segment was expressed in &lt;i>E. coli&lt;/i> BL21 and &lt;i>P. pastoris&lt;/i> GS115. For characterization, the enzyme was isolated in two steps in &lt;i>E. coli&lt;/i> and one step in &lt;i>P. pastoris&lt;/i>. The biochemical properties of the two recombinant enzymes were similar, and their optimal reaction pH and temperature were 6.0 and 50°C, respectively. According to molecular dynamics simulation, the CuZnSOD showed high stability from 70 to 90°C, and eight amino acids are important for enzyme thermal sta</description><dates><release>2022-01-01T00:00:00Z</release><publication>2022</publication><modification>2026-05-30T20:57:41.494Z</modification><creation>2025-04-04T10:02:21.661Z</creation></dates><accession>S-EPMC8959677</accession><cross_references><pubmed>35356736</pubmed><doi>10.3389/fnut.2022.850824</doi></cross_references></HashMap>