Exploitation of E. coli for the production of penicillin G amidase: a tool for the synthesis of semisynthetic β-lactam antibiotics

Sambyal, Krishika; Singh, Rahul Vikram

doi:10.1186/s43141-021-00263-7

Cited by 10 publications

(4 citation statements)

References 86 publications

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“…Numerous microbial strains, including E. coli, Pseudomonas melanogenum, Bacillus megaterium, Kluyvera sp., and Proteus rettgeri, possess the natural capability to produce PGA. Notably, according to to Vélez et al, (2014) & Sambyal & Singh, (2021, the PGA enzymes that is in great demand in both research and industry settings originate from E. coli and B. megaterium due to their exceptional efficiency.…”

Section: Early Discovery Of Pgamentioning

confidence: 99%

“…Structural changes in enzymes exert a stronger influence on amidase than synthetase activity due to the complex mechanism involved in amide hydrolysis (Buchholz, 2016;Sambyal & Singh, 2021). Organic solvents contribute to increasing substrate solubility, influencing reaction pK values for the formation of non-reactive ions, and aiding synthesis by reducing water activity (Deng et al, 2015).…”

Section: Volume 35 Issue 1 (2024)mentioning

confidence: 99%

“…Penicillin G acylase (PGA) is one of the most extensively employed commercial enzymes globally worldwide (Sambyal & Singh, 2021). Initially, penicillin G, a β-lactam antibiotic, was discovered for its efficacy in combating grampositive bacteria.…”

Section: Introductionmentioning

confidence: 99%

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Manipulation Strategy to Increase Expression Level of Soluble Recombinant Protein Penicillin G Acylase (PGA) in Bacterial Host Escherichia coli: A Review Article

Amin,

Sismindari,

Aniqah

et al. 2024

Indonesian J Pharm

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The strategy of producing PGA on a massive scale with high levels of soluble protein can be through recombinant genetic techniques and expressed in a certain host. E. coli is still a popular bacterial host to produce a recombinant protein which has advantages such as fast growth, low production cost, and high expression rate. Apart from its advantages, E. coli as a production host also has disadvantages including the expression of recombinant proteins often failing to form the proper folding conformation which makes the protein biologically inactive. Many strategies can be developed to overcome these problems, such as the selection of the host strain (E. coli HB101 & JM109), fusion protein to enhance the recovery of soluble protein (MBP & NusA), optimization of fermentation (low-temperature incubation), and optimization of the protein isolation process for the recovery of active PGA (Freeze-thawing method).

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Section: Early Discovery Of Pgamentioning

confidence: 99%

Section: Volume 35 Issue 1 (2024)mentioning

confidence: 99%

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Manipulation Strategy to Increase Expression Level of Soluble Recombinant Protein Penicillin G Acylase (PGA) in Bacterial Host Escherichia coli: A Review Article

Amin,

Sismindari,

Aniqah

et al. 2024

Indonesian J Pharm

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“…Extraction of DNA from the different environments is followed by a metagenomic approach. Usually, there are two commonly applied methods to screen the con-struction of the metagenomic library, sequence-based screening, and function-based screening [38][39][40]. Sequence-based screening has the advantage of conserved sequence similarity assessment and functional gene annotation through online databases [41,42].…”

Section: Trends and Strategies In Enzyme Engineering For Enzymatic Sy...mentioning

confidence: 99%

Enzymatic Catalysts for Hydroxamic Acid Formation: A Mini‐Review

Singh

2023

ChemBioEng Reviews

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In recent years, biocatalysts have emerged as crucial tool in organic synthesis, particularly for the production of drug intermediates and precursors, e.g., the synthesis of hydroxamic acids. Traditionally, hydroxamic acids were synthesized using organic chemistry methods. However, with the growing emphasis on sustainable and environment‐friendly practices, the chemical industry has increasingly turned towards green synthesis approaches. The significance of hydroxamic acids in medicinal chemistry has also contributed to the changing trends. Following the approval of certain hydroxamic acids as histone deacetylase (HDAC) inhibitors for cancer treatment by the Food and Drug Administration (US‐FDA), there has been a renewed focus on their synthesis and the development of derivatives with improved properties. As an alternative route, amidases have emerged as promising biocatalysts for hydroxamic acid synthesis through their acyltransferase activity. Recent advancements in the synthesis approaches for hydroxamic acids are reviewed. The biocatalytic routes are explored, emphasizing the use of amidases and their acyltransferase activity. The scope and potential applications of this chemoenzymatic approach in synthesizing various hydroxamic acids and their derivatives are discussed. Such advancements have the potential to revolutionize the production of these important compounds, making the synthesis process more sustainable, efficient, and economically viable.

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