摘要

Cross-linked enzyme aggregates from bovine pancreatic lipase were prepared by co-aggregation of lipase and BSA (Lipase-BSA-CLEAs). The main factors in the preparation of lipase-BSA-CLEAs were optimized. The highest activity recovery was around 75% under the condition of using 1% (v/v) glutaraldehyde as cross-linker and 0.05 g/L bovine serum albumin as feeder for 2 h cross linking. The optimum temperature for both lipase-CLEAs and lipase- BSA-CLEAs was measured as 60 A degrees C, which is 10 A degrees C higher than that of free lipase. Moreover, the lipase-BSA-CLEAs evidenced higher thermal stability and excellent reusability in comparison with the lipase-CLEAs. Lipase-BSA-CLEAs retained more than 75% of the initial activity after eight cycles of reuse, while lipase-CLEAs only retained 20% of its initial activity. Additionally, lipase-BSA-CLEAs showed more storage stability than free lipase and lipase-CLEAs. The high stability and recyclability of lipase-BSA-CLEAs make it efficient for different industrial applications.