Full text loading...
Penicillin G amidase is an industrially significant enzyme widely employed in the production of semi-synthetic β-lactam antibiotics through the hydrolysis of Penicillin G to 6-aminopenicillanic acid. Owing to its commercial importance, extensive research has focused on improving the operational stability, reusability, and catalytic efficiency of PGA through various immobilization strategies.
Optimization of multiple parameters for free and immobilized Penicillin G Acylase (PGA) is critical for improving the enzyme's catalytic effectiveness, stability, and reusability in industrial and medicinal applications. This procedure entails methodically altering and analyzing variables such as substrate concentration, mechanical stability, cycle number, and storage conditions, and their effects on operational stability, pH, and temperature. PGA was optimized by entrapment on collagen hydrogel beads, resulting in collagen hydrogel + gelatin hybrid gel beads.
Immobilized PGA in Collagen Hydrogel + gelatin hybrid beads showed superior thermal stability, reusability, and storage stability as compared to gelatin-immobilized PGA. The entrapment of PGA onto Collagen Hydrogel + gelatin hybrid beads revealed several advantages and could be used in the production of 6-aminopenicillanic acid (6APA).
The study investigated the biochemical behavior of Penicillin G amidase (PGA) immobilized on collagen hydrogel and a collagen–gelatin bio-composite. Relative analysis focused on enzyme activity, stability, and mechanical strength, revealing insights into their appropriateness as immobilization matrices for enhanced PGA performance in industrial biocatalysis applications.
Hydrogel + gelatin hybrid beads are more beneficial in industrial applications due to their greater stability and usability. PGA entrapment onto Hydrogel + gelatin hybrid beads has shown numerous advantages and may be useful in the manufacture of 6APA (6-aminopenicillanic acid).