{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["9"],"submitter":["Zhao Y"],"pubmed_abstract":["Previously, a new copper-zinc SOD (CuZnSOD) isolated from chestnut rose (<i>Rosa roxburghii</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 <i>E. coli</i> BL21 and <i>P. pastoris</i> GS115. For characterization, the enzyme was isolated in two steps in <i>E. coli</i> and one step in <i>P. pastoris</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"],"journal":["Frontiers in nutrition"],"pagination":["850824"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC8959677"],"repository":["biostudies-literature"],"pubmed_title":["Production of a Novel Superoxide Dismutase by <i>Escherichia coli</i> and <i>Pichia pastoris</i> and Analysis of the Thermal Stability of the Enzyme."],"pmcid":["PMC8959677"],"pubmed_authors":["Zhang W","Zhao L","Liao X","Wang Y","Rao L","Zhao Y"],"additional_accession":[]},"is_claimable":false,"name":"Production of a Novel Superoxide Dismutase by <i>Escherichia coli</i> and <i>Pichia pastoris</i> and Analysis of the Thermal Stability of the Enzyme.","description":"Previously, a new copper-zinc SOD (CuZnSOD) isolated from chestnut rose (<i>Rosa roxburghii</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 <i>E. coli</i> BL21 and <i>P. pastoris</i> GS115. For characterization, the enzyme was isolated in two steps in <i>E. coli</i> and one step in <i>P. pastoris</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","dates":{"release":"2022-01-01T00:00:00Z","publication":"2022","modification":"2026-05-30T20:57:41.494Z","creation":"2025-04-04T10:02:21.661Z"},"accession":"S-EPMC8959677","cross_references":{"pubmed":["35356736"],"doi":["10.3389/fnut.2022.850824"]}}