Neh Nupur, Ashish and Mira Debnath (Das) Pages 121 - 132 ( 12 )
Background: Penicillin G amidase (PGA) (EC 188.8.131.52) are enzymes that are mainly involved in the synthesis of semi-synthetic }-lactam antibiotics. Soluble PGA is costly and lacks long term operational stability. We revised most of the patents related to Penicillin G amidase (PGA) immobilization in the section "Recent Patents on Immobilized Penicillin G Amidase".
Objective: The aim of this work was to study comparative biochemical property of PGA enzyme immobilized in two hydro-gel beads - Ca-alginate and alginate+chitosan hybrid and morphologically characterised by SEM.
Methods: PGA immobilized in alginate+chitosan hybrid bead shows high pH and thermal stability. Km, Vmax and Effectiveness factor (1) value of free PGA were 56.19 mg/ml, 1.786 U/ml and 1, respectively. These parameters for PGA immobilized alginate beads were 64.84 mg/ml, 0.781U/ml and 0.437, respectively and for PGA immobilized alginate+chitosan hybrid beads were 87.08 mg/ml, 0.622 U/ml and 0.348, respectively.
Results: Immobilized PGA on alginate+chitosan hybrid beads gave the highest thermal stability, reusability and storage stability than alginate immobilized PGA. Conclusion: The entrapment of PGA on alginate+chitosan hybrid beads revealed several advantages and could be used in 6APA (6- aminopenicillanic acid) production.
Penicillin G amidase, immobilization, alginate bead, alginate+chitosan hybrid beads, PGA immobilization, J3-Tactam antibiotics.
School of Biochemical Engineering, Indian Institute of Technology, (Banaras Hindu University), Varanasi-221005, U.P., India.