Polyacrylamide Gel-Entrapped Fungal Manganese Peroxidase with Enhanced Catalytic, Stability and Reusability Characteristics

Protein Pept Lett. 2016 Jul 19. Online ahead of print.

Abstract

In the present study, polyacrylamide gel (PAG) was utilized as bolster material for the immobilization of in-house extracted and partially purified manganese peroxidase (MnP) through entrapment technique. The entrapment technique impelled incredibly compelling MnP immobilization (87.3±3.3%) and conferred remarkable stability to the enzyme (37.2±2.4%) following two months of storage at 4°C. The PAG-assisted immobilization expanded the reaction time of MnP after 10 min of response when contrasted with a partially purified free MnP counterpart, which demonstrated the highest activity after 5.0 min. Following PAG-assisted immobilization, an improvement in the optimal temperature and a chemical (an alkaline) shift in the pH optima of MnP were recorded. Moreover, a significant enhancement in the thermo-stability was also observed after immobilization. After 72 h, PAG-entrapped-MnP exhibited 41.2% residual activity at 50°C, whereas the free counterpart lost its activity completely under the same conditions. Furthermore, the PAG-entrapped-MnP also showed an excellent recycling efficiency and retained more than 50% of its initial activity after five consecutive reaction cycles. In conclusion, owing to the economic feasibility, carrier-supported MnP may be a promising candidate for various applications in different sectors of the modern world.