Entrapment of surfactant modified lipase within zeolitic imidazolate framework (ZIF)-8

Mostly, enzyme activity is reduced after immobilization of enzyme within MOF due to unfavourable conformational changes occurred during the immobilization procedure. In this context, lipase was activated by surfactants (in order to get a highly active enzyme) followed by encapsulation within zeolitic imidazolate framework (ZIF)-8 via one-pot facile self-assembly method. The prepared lipase-SDS ZIF-8 exhibited 250% enhanced activity compared to native form. The prepared biocomposite was characterized and analysed by X-ray diffraction (XRD), Fourier transform infrared (FT-IR) and scanning electron microscopy (SEM). Thermo-stability was determined for prepared lipase-SDS ZIF-8 biocomposite in the range of 50-70 degrees C, which showed more than two-folds enhanced stability in terms of half-life. Further, immobilized lipase retained 76% of residual activity even after six repetitive cycles and, it showed 91% residual activity after twenty days of long term storage. Finally, lipase-SDS ZIF-8 was tested for chemical stability in polar denaturing solvents which showed excellent stability as compared to free lipase. (C) 2019 Elsevier B.V. All rights reserved.