To further uncover the structural information and successful laccase immobilization of BNNS-Arg@Lac, the XRD analysis, FTIR, and XPS were performed. As shown in Figure , two characteristic diffraction peaks were observed at 26.7 o and 42.1 o for both BNNS-Arg and BNNS-Arg@Lac, which is ascribed to the (111) and (200) face of boron nitrite, implying the arginine decoration and the subsequent laccase immobilization process of laccase did not change the host structure. From the FTIR, the fingerprint bonds of B-N stretching (1370 cm -1 ) and B-N bending (820 cm -1 ) can be observed in all BNNS-contained samples, which is contributed by the boron nitride substrate. The liquid nlaccase sample revealed C-O-C stretching (1099 cm -1 ), CONH peptide linkage (1630 cm -1 ), and an abundant O-H stretching peak that was contributed by H2O. Both BNNS-Arg and BNNS-Arg@Lac exhibited peaks corresponding to C-N bonds, O-H bending vibration of carboxyl groups, and C-O bonds, which overlapped with B-N stretching peaks (1370 cm -1 ). Owing to the addition of laccase, more C-N, O-H bending, and C-O peaks presented in BNNS-Arg@Lac, leading to a greater reduction of B-N stretching peaks. It could be due to the coverage of laccase on the BNNS-Arg surface. Another evidence of nlaccase immobilized on BNNS-Arg was the observation of signature peaks of nlaccase: C-O-C stretching and CONH peptide linkage, in BNNS-Arg@Lac samples. Further chemical state and composition were identified by the XPS. Illustrated in Figure , the XPS survey shows the presence of B 1s, C 1s, N 1s, and O 1s signals in both samples, which can be attributed to the incorporation of arginine within BNNS-Arg and additional amino acids in BNNS-Arg@Lac.