Amino-derivatized lignocomposite (ADL-composite) has been designed as an artificial lignin polymer (P1) of monolignol (coniferyl alcohol, CA) enhanced by aniline insertion (P2). The derivatized lignopolymeric (P2) layer covered the surface of a methacrylate particles (SC2/SC6) functionalized previously with amino phenolic crosslinker (p-phenylenediamine (p-Ph-2-NH2) or p-amino-2-hydroxybenzoic acid (p-NH2-SalA)). One-pot biocatalytic approach allowed to combine the preparation of the polymeric materials and also its attachment on the particles surface. Thus, the monolignol (CA) will be oxi-copolymerized together with aniline on the amino prefunctionalized support surface. The oxidation process was performed using H2O2 reagent and catalyzed by peroxidase enzyme (horseradish peroxidase, HRP). The biocatalytic process was evaluated in term of aromatic monomers (CA and aniline) conversion. The chemical structure and properties of the resulted ADL-composites were investigated using specific techniques (e.g. FTIR, TPD, TGA, static contact angle, elemental analysis, and gel permeation chromatography). Attachment of P1/P2 polymer on the particles improved the hydrophobicity and also the basicity of the composite surface. Lipase enzyme was immobilized on the ADL-composites for testing the applicability of ADL-composites for biocatalyst preparation. SEM analysis allowed to notice the modification of ADL-composites surface after enzyme immobilization. Immobilized lipase exhibited better activity compared with free lipase demonstrating the efficiency of ADL-composite as support for enzyme immobilization.