A novel immobilized enzyme enhances the conversion of phosphatidylserine in two-phase system

Abstract

A novel immobilized enzyme reactor was developed as prototypes for biosynthetic purposes and the performance in the phosphatidylserine (PS) synthesis was evaluated. Phospholipase D (PLD) was immobilized into ordered mesoporous silica cube (OMSC) modified with octadecyltrimethoxysilane (-C18). The modified OMSC with immobilized PLD (OMSC-C18-PLD) preserved more than 90 % of its activity after incubation at 40 ℃ for 2 h, while the free enzyme showed only 23.25 % of its maximum activity. OMSC-C18-PLD could achieve 91.2 % PS conversion and less than 5 % hydrolysis reaction within 9 h, and still maintain more than 30 % enzyme activity after 9 consecutive runs. The catalytic efficiency (CE) of free and immobilized enzyme were 24.24 μmol / (gh) and 35.87 μmol / (gh), respectively. The half-life period of enzyme increased from 25 days to 40 days after immobilization. Transphosphatidylation reaction catalyzed by OMSC-C18-PLD approved its practical applications in the phosphatidylserine synthesis.