Abstract
BackgroundPenicillin G amidase/acylases from microbial sources is a unique enzyme that belongs to the N-terminal nucleophilic hydrolase structural superfamily. It catalyzes the selective hydrolysis of side chain amide/acyl bond of penicillins and cephalosporins whereas the labile amide/acyl bond in the β-lactam ring remains intact. Main body of abstractThis review summarizes the production aspects of PGA from various microbial sources at optimized conditions. The minimal yield from wild strains has been extensively improved using varying strain improvement techniques like recombination and mutagenesis; further applied for the subsequent synthesis of 6-aminopenicillanic acid, which is an intermediate molecule for synthesis of a wide range of novel β-lactam antibiotics. Immobilization of PGA has also been attempted to enhance the durability of enzyme for the industrial purposes. Short conclusionThe present review provides an emphasis on exploitation of E. coli to enhance the microbial production of PGA. The latest achievements in the production of recombinant enzymes have also been discussed. Besides E. coli, other potent microbial strains with PGA activity must be explored to enhance the yields. Graphical abstract▪
Highlights
Discovery of penicillin G amidase Enzymes are the ideal biocatalysts which provide ecofriendly environmental conditions for different processes to occur mildly, of great importance to the industries [5]
Short conclusion: The present review provides an emphasis on exploitation of E. coli to enhance the microbial production of Penicillin G amidases or acylases (PGA)
PGA was firstly reported in the mycelium of Penicillium chrysogenum Q176 in the year 1950 as an enzyme with potential to catalyze the hydrolysis of penicillin G into phenyl acetic acid (PAA) and an unknown compound called “penicillin” (6-APA) in the form of hygroscopic crystalline needles giving 158–159 °C melting point [20, 21]
Summary
Penicillin G amidases or acylases (PGA) (penicillin amidohydrolase: EC 3.5.1.11) is one of the principal enzymes at an industrial level used to catalyze the enzymatic hydrolysis of various penicillins by cleaving their amide bond to yield 6-APA and its corresponding organic acid [1]. The first executed hydrolysis by immobilized PGA involved penicillin G and cephalosporin G as substrates [11] This method was quickly implemented to be used by the pharmaceutical industry since the mild conditions were appropriate for the stability and activity of PGA [12]. PGAs are potentially useful biocatalysts in various ways such as protection of amino and hydroxyl groups during peptide synthesis and resolution of racemic mixtures of chiral compounds [17, 18]. They are known to work as a promising candidate for linker cleavage studies of structures for combinatorial chemistry due to their high substrate specificity concerning the acyl residue [19]
Sign-in/Register to view highlights & summary Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
