Characterization of non-covalent immobilized Candida antartica lipase b over PS-b-P4VP as a model bio-reactive porous interface

• Published in: Colloids and Surfaces B: Biointerfaces
• Main Authors: Pazol, Jessika, Vázquez, Adriana, Nicolau, Eduardo
• Format: Text
• Language: English
• Published: 2019
• Subjects: Article; Antarc*; Antarctica; antartic*
• Online Access: http://www.ncbi.nlm.nih.gov/pmc/articles/PMC6815258/; http://www.ncbi.nlm.nih.gov/pubmed/31404792; https://doi.org/10.1016/j.colsurfb.2019.110418

The design of interfaces that selectively react with molecules to transform them into compounds of industrial interest is an emerging area of research. An example of such reactions is the hydrolytic conversion of ester-based molecules to lipids and alcohols, which is of interest to the food, and pharmaceutical industries. In this study, a functional bio-interfaced layer was designed to hydrolyze 4-nitrophenyl acetate (pNPA) and Ricinus Communis (castor) oil rich in triglycerides using lipase b from Candida antarctica (CALB, EC 3.1.1.3). The attachment of CALB was performed via non-covalent immobilization over a polymer film of vertically aligned cylinders that resulted from the self-assembly of the di-block copolymer polystyrene-block-poly(4-vinyl pyridine) (PS-b-P4VP). This polymer-lipase model will serve as the groundwork for the design of further bioactive layers for separation applications requiring similar hydrolytic processes. Results from the fabricated functional bio-interfaced material include cylinders with featured pore size of 19 nm, d spacing of 34 nm, and ca. 40 nm of thickness. The polymer-enzyme layers were physically characterized using AFM, XPS, and FTIR. The immobilized enzyme was able to retain 91% of the initial enzymatic activity when using 4-nitrophenyl acetate (pNPA) and 78% when exposed to triglycerides from castor oil.