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However, the enzyme that is involved in the biodegradation process is the key information to be revealed.<\/jats:p>\n                  <\/jats:sec>\n                  <jats:sec>\n                    <jats:title>Results<\/jats:title>\n                    <jats:p>\n                      In this study, the beta-lactamase from\n                      <jats:italic>Ochrobactrum<\/jats:italic>\n                      <jats:italic>tritici<\/jats:italic>\n                      that mediates the biodegradation of penicillin V was identified and characterized. When searching the proteins of\n                      <jats:italic>Ochrobactrum<\/jats:italic>\n                      <jats:italic>tritici<\/jats:italic>\n                      , the \u03b2-lactamase (OtLac) was identified. OtLac consists of 347 amino acids, and predicted isoelectric point is 7.0. It is a class C \u03b2-lactamase according to BLAST analysis. The coding gene of OtLac was amplified from the genomic DNA of\n                      <jats:italic>Ochrobactrum<\/jats:italic>\n                      <jats:italic>tritici<\/jats:italic>\n                      . The OtLac was overexpressed in\n                      <jats:italic>E. coli<\/jats:italic>\n                      BL21 (DE3) and purified with Ni\n                      <jats:sup>2+<\/jats:sup>\n                      column affinity chromatography. The biodegradation ability of penicillin V by OtLac was identified in an in vitro study and analyzed by HPLC. The optimal temperature for OtLac is 32\u00a0\u2103 and the optimal pH is 7.0. Steady-state kinetics showed that OtLac was highly active against penicillin V with a Km value of 17.86\u00a0\u03bcM and a kcat value of 25.28 s\n                      <jats:sup>\u22121<\/jats:sup>\n                      respectively.\n                    <\/jats:p>\n                  <\/jats:sec>\n                  <jats:sec>\n                    <jats:title>Conclusions<\/jats:title>\n                    <jats:p>OtLac demonstrated biodegradation activity towards penicillin V potassium, indicating that OtLac is expected to degrade penicillin V in the future.<\/jats:p>\n                  <\/jats:sec>","DOI":"10.1186\/s12934-021-01606-2","type":"journal-article","created":{"date-parts":[[2021,6,13]],"date-time":"2021-06-13T17:02:27Z","timestamp":1623603747000},"update-policy":"https:\/\/doi.org\/10.1007\/springer_crossmark_policy","source":"Crossref","is-referenced-by-count":21,"title":["Enzyme-catalyzed biodegradation of penicillin fermentation residues by \u03b2-lactamase OtLac from Ochrobactrum tritici"],"prefix":"10.1186","volume":"20","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-1148-3015","authenticated-orcid":false,"given":"Peng","family":"Wang","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Chen","family":"Shen","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Qinqin","family":"Cong","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Kaili","family":"Xu","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jialin","family":"Lu","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"297","published-online":{"date-parts":[[2021,6,13]]},"reference":[{"key":"1606_CR1","doi-asserted-by":"publisher","first-page":"122012","DOI":"10.1016\/j.biortech.2019.122012","volume":"292","author":"G Yang","year":"2019","unstructured":"Yang G, Wang J, Shen Y. 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