Conformation and Activity of Sol-Gels Encapsulated Cross-Linked Enzyme Aggregates of Lipase from Burkholderia cepacia

Abstract:

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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.

Info:

Periodical:

Advanced Materials Research (Volumes 291-294)

Edited by:

Yungang Li, Pengcheng Wang, Liqun Ai, Xiaoming Sang and Jinglong Bu

Pages:

614-620

DOI:

10.4028/www.scientific.net/AMR.291-294.614

Citation:

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

Online since:

July 2011

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$35.00

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