Enzyme-catalyzed biodegradation of penicillin fermentation residues by β-lactamase OtLac from Ochrobactrum tritici
Abstract Background Biodegradation of antibiotics is a promising method for the large-scale removal of antibiotic residues in the environment. However, the enzyme that is involved in the biodegradation process is the key information to be revealed. Results In this study, the beta-lactamase from Ochr...
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Published in | Microbial cell factories Vol. 20; no. 1; pp. 1 - 9 |
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Main Authors | , , , , |
Format | Journal Article |
Language | English |
Published |
London
BioMed Central
13.06.2021
BMC |
Subjects | |
Online Access | Get full text |
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Summary: | Abstract
Background
Biodegradation of antibiotics is a promising method for the large-scale removal of antibiotic residues in the environment. However, the enzyme that is involved in the biodegradation process is the key information to be revealed.
Results
In this study, the beta-lactamase from
Ochrobactrum
tritici
that mediates the biodegradation of penicillin V was identified and characterized. When searching the proteins of
Ochrobactrum
tritici
, the β-lactamase (OtLac) was identified. OtLac consists of 347 amino acids, and predicted isoelectric point is 7.0. It is a class C β-lactamase according to BLAST analysis. The coding gene of OtLac was amplified from the genomic DNA of
Ochrobactrum
tritici
. The OtLac was overexpressed in
E. coli
BL21 (DE3) and purified with Ni
2+
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 ℃ 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 μM and a kcat value of 25.28 s
−1
respectively.
Conclusions
OtLac demonstrated biodegradation activity towards penicillin V potassium, indicating that OtLac is expected to degrade penicillin V in the future. |
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ISSN: | 1475-2859 1475-2859 |
DOI: | 10.1186/s12934-021-01606-2 |