Conformation and Activity of Sol-Gels Encapsulated Cross-Linked Enzyme Aggregates of Lipase from Burkholderia cepacia
Cross-linked enzyme aggregates (CLEAs) of lipase from Burkholderia cepacia (BCL) were explored using different precipitants and different amount of glutaraldehyde as cross-linkers. The ‘fresh’ and ‘mature’ CLEAs-BCL was successfully encapsulated with sol-gel support. The latter showed the highest specific enzyme activity, which was 1.7 and 13.2-fold over CLEAs-BCL before encapsulation with sol-gel and free BCL, respectively. It performed high transesterification activity with the biodiesel yield of 88.5%. The ‘mature’ CLEAs-BCL presented high stability in the ranges of temperature (30-70 ºС) and pH (pH = 5-10). Scanning electron microscopy (SEM) and circular dichroism (CD) studies showed that the morph secondary structure of ‘fresh’ and ‘mature’ CLEAs-BCL was variant to some extent, which may be responsible for the catalytic activity variance.
Yungang Li, Pengcheng Wang, Liqun Ai, Xiaoming Sang and Jinglong Bu
Y. Liu et al., "Conformation and Activity of Sol-Gels Encapsulated Cross-Linked Enzyme Aggregates of Lipase from Burkholderia cepacia", Advanced Materials Research, Vols. 291-294, pp. 614-620, 2011