Comparative study of covalent and hydrophobic interactions for α-amylase immobilization on cellulose derivatives.

Indispensability of enzymes in living systems, their unique characteristics and simultaneous focus on development of greener methods have led to substitution of various chemical reactions by enzyme catalyzed reactions. One of the aspects in enzyme research is immobilization of enzymes. Immobilization provides a platform for reusability of significant enzymes. Varieties of methods have been explored for enzyme immobilization such as entrapment, adsorption, ionic interactions etc. Keeping in view the industrial utility of α-Amylase in leather, paper and other industries related to starch hydrolysis, we immobilized α-Amylase on cellulose isolated from banana peel. In present study, two different methods of immobilization - covalent bonding (Cellulose Dialdehyde as a support) and hydrophobic interactions (Nano Cellulose- Cetyl Trimethyl Ammonium Bromide) were used. Cellulose obtained from bio-waste has been characterized using Fourier transform Infrared Spectroscopy (FT-IR), Thermogravimetric Analysis (TGA), Scanning Electron Microscopy (SEM), X-ray Diffraction (XRD). In this comparative study, Cellulose Dialdehyde (CDA) immobilized enzyme depicts high reusability, good enzyme loading, storage capacity up to 49 days, optimum pH 6, optimum temperature 95 °C, good pH and thermal stability as compared to native enzyme having optimum pH and temperature of 7 and 37 °C. On the contrary, nanocellulose - Cetyl Trimethyl Ammonium Bromide (NC-CTAB) matrix shows good enzyme loading and optimum pH shift of about 3 units but poor recyclability. Outcome of this study presents the promising nature of covalent mode of immobilization for industrial use.