Abstract
Three polysaccharide matrices (κ-Carrageenan (Carr), gellan gum, and agar) were grafted via glutaraldehyde (GA) and pea protein (PP). The grafted matrices covalently immobilized β-D-galactosidase (β-GL). Nonetheless, grafted Carr acquired the topmost amount of immobilized β-GL (iβ-GL). Thus, its grafting process was honed via Box-Behnken design and was further characterized via FTIR, EDX, and SEM. The optimal GA-PP-Carr grafting comprised processing Carr beads with 10% PP dispersion of pH 1 and 25% GA solution. The optimal GA-PP-Carr beads acquired 11.44 Ug(-1) iβ-GL with 45.49% immobilization efficiency. Both free and GA-PP-Carr iβ-GLs manifested their topmost activity at the selfsame temperature and pH. Nonetheless, the β-GL K(m) and V(max) values were reduced following immobilization. The GA-PP-Carr iβ-GL manifested good operational stability. Moreover, its storage stability was incremented where 91.74% activity was offered after 35 storage days. The GA-PP-Carr iβ-GL was utilized to degrade lactose in whey permeate with 81.90% lactose degradation efficiency.