Biotransformation of penicillin V to 6-aminopenicillanic acid using immobilized whole cells of <i>E. coli</i> expressing a highly active penicillin V acylase

Avinash, Vellore Sunder; Chauhan, Palna Dinesh; Gaikwad, Shraddha; Pundle, Archana

doi:10.1080/10826068.2016.1163580

Cited by 11 publications

(7 citation statements)

References 28 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Penicillin G acylase (PGA) has been used widely in production of semi‐synthetic β‐lactam antibiotics, which has attracted extensive interesting all over the world. In actual applications, PGA was presented in an immobilized form in order to improve the recyclability and reusability.…”

Section: Introductionmentioning

confidence: 99%

The engineering and immobilization of penicillin G acylase onto thermo‐sensitive tri‐block copolymer system

Liu

Zhang

et al. 2018

Polymers for Advanced Techs

View full text Add to dashboard Cite

In this work, the relationships between catalytic performances of penicillin G acylase (PGA) and the molar ratio of carrier, thermo‐sensitive tri‐block polymer, poly (N,N‐diethylacrylamide‐b‐ β‐hydroxyethyl methacrylate‐b‐glycidyl methacrylate) (PDEA‐b‐PHEMA‐b‐PGMA) were studied firstly, and result documented the optimal molar ratio was nDEA:nHEMA:nGMA = 100:47:24, which presented a suitable lower critical solution temperature (LCST) of 35°C and the activity retention ratio of 80.62% (±0.50%). Based on the suitable carrier, immobilization conditions were investigated and optimized. When pH of solution, concentration of PGA, immobilized time, and immobilization temperature were 8.0, 1/10 (m/v), 16 hours, and 36°C, respectively, enzyme loading capacity (L), enzyme activity (Ea), and activity retention ratio (Ar) of PGA arrived at the highest value of 21 223 U, 16 199 U/g, and 93.50% (±0.50%), respectively. Besides, the response rate (Rr) of immobilized PGA was the same as free PGA, the reusable stability (Rs) was 77.00% (±1.00%) after using for 11 times, which indicated that the carrier has better compatibility with L, Ar, Rs, and Rr.

show abstract

Section: Introductionmentioning

confidence: 99%

The engineering and immobilization of penicillin G acylase onto thermo‐sensitive tri‐block copolymer system

Liu

Zhang

et al. 2018

Polymers for Advanced Techs

View full text Add to dashboard Cite

show abstract

“…Furthermore, the immobilization of whole-cells can facilitate product purification and allows for the recycling of the biocatalysts, thus lowering the cost of production. However, this method also suffers from lower activity compared to using free enzymes because of the limited diffusion of the reaction substrates or products through the cell membrane [ 33 ]. Treatment of the cell with chemical agents will permeabilize the membrane, thereby alleviating this problem.…”

Section: Resultsmentioning

confidence: 99%

Biosynthesis of S-Adenosylmethionine by Magnetically Immobilized Escherichia coli Cells Highly Expressing a Methionine Adenosyltransferase Variant

2017

View full text Add to dashboard Cite

S-Adenosylmethionine (SAM) is a natural metabolite having important uses in the treatment of various diseases. To develop a simple and effective way to produce SAM, immobilized Escherichia coli cells highly expressing an engineered variant of methionine adenosyltransferase (MAT) were employed to synthesize SAM. The recombinant I303V MAT variant was successfully produced at approximately 900 mg/L in a 10-L bioreactor and exhibited significantly less product inhibition and had a four-fold higher specific activity (14.2 U/mg) than the wild-type MAT (3.6 U/mg). To reduce the mass transfer resistance, the free whole-cells were permeabilized and immobilized using gellan gum gel as support in the presence of 100 mg/L Fe3O4 nanoparticles, and the highest activity (4152.4 U/L support) was obtained, with 78.2% of the activity recovery. The immobilized cells were more stable than the free cells under non-reactive conditions, with a half-life of 9.1 h at 50 °C. Furthermore, the magnetically immobilized cells were employed to produce SAM at a 40-mM scale. The residual activity of the immobilized cells was 67% of its initial activity after 10 reuses, and the conversion rate of ATP was ≥95% in all 10 batches. These results indicated that magnetically immobilized cells should be a promising biocatalyst for the biosynthesis of SAM.

show abstract

“…Then, this product was further hydrolyzed to form penicilloic acid or penicilloic acid potassium and phenoxyacetic acid. This step was probably catalyzed by penicillin V acylase (32).…”

Section: Discussionmentioning

confidence: 99%

Isolation and Characterization of Ochrobactrum tritici for Penicillin V Potassium Degradation

Wang

Shen

et al. 2020

mSphere

View full text Add to dashboard Cite

Substantial concentrations of penicillin V potassium (PVK) have been found in livestock manure, soil, and wastewater effluents, which may pose potential threats to human health and contribute to the emergence of penicillin-resistant bacterial strains. In this study, bacterial strains capable of degrading PVK were isolated from sludge and characterized. Strain X-2 was selected for biodegradation of PVK. Based on morphological observations and 16S rRNA gene sequencing, strain X-2 was identified as an Ochrobactrum tritici strain. To enhance the PVK degradation ability of PVK, a whole-cell biodegradation process of Ochrobactrum tritici X-2 was established and optimized. In the whole-cell biodegradation process, the optimal temperature and pH were 30°C and 7.0, respectively. Under the optimized conditions, the degradation rate using 0.5 mg/ml PVK reached 100% within 3 h. During biodegradation, two major metabolites were detected: penicilloic acid and phenolic acid. The present study provides a novel method for the biodegradation of PVK using Ochrobactrum tritici strains, which represent promising candidates for the industrial biodegradation of PVK. IMPORTANCE Substantial concentrations of penicillin V potassium (PVK) have been found in the environment, which may pose potential threats to human health and contribute to the emergence of penicillin-resistant bacterial strains. In this study, antibiotic-degrading bacterial strains for PVK were isolated from sludge and characterized. Ochrobactrum tritici was selected for the biodegradation of PVK with high efficiency. To enhance its PVK degradation ability, a whole-cell biodegradation process was established and optimized using Ochrobactrum tritici. The degradation rate with 0.5 mg/ml PVK reached 100% within 3 h. The potential biodegradation pathway was also investigated. To the best of our knowledge, the present study provides new insights into the biodegradation of PVK using an Ochrobactrum tritici strain, a promising candidate strain for the industrial biodegradation of β-lactam antibiotics.

show abstract

Biotransformation of penicillin V to 6-aminopenicillanic acid using immobilized whole cells of E. coli expressing a highly active penicillin V acylase

Cited by 11 publications

References 28 publications

The engineering and immobilization of penicillin G acylase onto thermo‐sensitive tri‐block copolymer system

The engineering and immobilization of penicillin G acylase onto thermo‐sensitive tri‐block copolymer system

Biosynthesis of S-Adenosylmethionine by Magnetically Immobilized Escherichia coli Cells Highly Expressing a Methionine Adenosyltransferase Variant

Isolation and Characterization of Ochrobactrum tritici for Penicillin V Potassium Degradation

Contact Info

Product

Resources

About