{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Skowron PM"],"funding":["Barentzymes AS, Norway"],"pagination":["135"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC7313183"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["19(1)"],"pubmed_abstract":["<h4>Background</h4>A neutral, heat-sensitive serine protease (NHSSP) originating from the feather-degrading fungus Onygena corvina (O. corvina) was described and defined as an alkaline serine protease of the subtilisin type S8 family, exhibiting an enzymatic activity at neutral pH. Generally, broad specificity proteases, such as proteinase K or trypsin, have found numerous applications in research and biotechnology.<h4>Results</h4>We report the cloning and expression in the yeast PichiaPink™ system, as well as purification, and characterization of the NHSSP. Recombinant, His<sub>6</sub>-tagged NHSSP was efficiently expressed from an optimized, synthetic gene and purified using a simple protocol based on ammonium sulfate fractionation and hydrophobic interaction chromatography. The enzyme s"],"journal":["Microbial cell factories"],"pubmed_title":["An alternative for proteinase K-heat-sensitive protease from fungus Onygena corvina for biotechnology: cloning, engineering, expression, characterization and special application for protein sequencing."],"pmcid":["PMC7313183"],"funding_grant_id":["company funds"],"pubmed_authors":["Brodzik R","Skowron PM","Kasperkiewicz P","Koller KP","Drag M","Krefft D"],"additional_accession":[]},"is_claimable":false,"name":"An alternative for proteinase K-heat-sensitive protease from fungus Onygena corvina for biotechnology: cloning, engineering, expression, characterization and special application for protein sequencing.","description":"<h4>Background</h4>A neutral, heat-sensitive serine protease (NHSSP) originating from the feather-degrading fungus Onygena corvina (O. corvina) was described and defined as an alkaline serine protease of the subtilisin type S8 family, exhibiting an enzymatic activity at neutral pH. Generally, broad specificity proteases, such as proteinase K or trypsin, have found numerous applications in research and biotechnology.<h4>Results</h4>We report the cloning and expression in the yeast PichiaPink™ system, as well as purification, and characterization of the NHSSP. Recombinant, His<sub>6</sub>-tagged NHSSP was efficiently expressed from an optimized, synthetic gene and purified using a simple protocol based on ammonium sulfate fractionation and hydrophobic interaction chromatography. The enzyme s","dates":{"release":"2020-01-01T00:00:00Z","publication":"2020 Jun","modification":"2026-04-30T07:08:49.671Z","creation":"2020-07-01T07:09:45Z"},"accession":"S-EPMC7313183","cross_references":{"pubmed":["32580707"],"doi":["10.1186/s12934-020-01392-3"]}}