{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Yu S"],"funding":["National Key Research &amp; Development Program of China","National Natural Foundation of China","National First-Class Discipline Program of Light Industry Technology and Engineering","National Key Research & Development Program of China"],"pagination":["25"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC11772468"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["109(1)"],"pubmed_abstract":["The enzyme D-sorbitol dehydrogenase (SLDH) facilitates the conversion of D-sorbitol to L-sorbose. While current knowledge of this enzyme class predominantly centers on Gluconobacter oxydans, the catalytic properties of enzymes from alternative sources, particularly their substrate specificity and coenzyme dependency, remain ambiguous. In this investigation, we conducted BLASTp analysis and screened out a novel SLDH (Fpsldh) from Faunimonas pinastri A52C2. The SLDH was then identified and characterized. Analysis of the purified enzyme revealed its dependence on NAD<sup>+</sup>/NADP<sup>+</sup> and its specificity for L-sorbose production. Fpsldh demonstrated sustained catalytic activity over temperatures ranging from 27 to 37 ℃, with optimal performance observed at pH 8.0-10.0, and it exhib"],"journal":["Applied microbiology and biotechnology"],"pubmed_title":["Characterization of a novel D-sorbitol dehydrogenase from Faunimonas pinastri A52C2."],"pmcid":["PMC11772468"],"funding_grant_id":["(2020YFA0907700","2018YFA0900300)","(LITE2018-22","(32172174","31401674)","2018YFA0900504"],"pubmed_authors":["Li Y","Yu S","Shi G","Xu S","Zhang L","Ding Z"],"additional_accession":[]},"is_claimable":false,"name":"Characterization of a novel D-sorbitol dehydrogenase from Faunimonas pinastri A52C2.","description":"The enzyme D-sorbitol dehydrogenase (SLDH) facilitates the conversion of D-sorbitol to L-sorbose. While current knowledge of this enzyme class predominantly centers on Gluconobacter oxydans, the catalytic properties of enzymes from alternative sources, particularly their substrate specificity and coenzyme dependency, remain ambiguous. In this investigation, we conducted BLASTp analysis and screened out a novel SLDH (Fpsldh) from Faunimonas pinastri A52C2. The SLDH was then identified and characterized. Analysis of the purified enzyme revealed its dependence on NAD<sup>+</sup>/NADP<sup>+</sup> and its specificity for L-sorbose production. Fpsldh demonstrated sustained catalytic activity over temperatures ranging from 27 to 37 ℃, with optimal performance observed at pH 8.0-10.0, and it exhib","dates":{"release":"2025-01-01T00:00:00Z","publication":"2025 Jan","modification":"2026-07-15T08:48:47.717Z","creation":"2025-04-04T22:24:03.797Z"},"accession":"S-EPMC11772468","cross_references":{"pubmed":["39869196"],"doi":["10.1007/s00253-024-13381-2"]}}