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

Abstract:

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.

• Periodical: Advanced Materials Research (Volumes 291-294)
• Pages: 614-620
• DOI: https://doi.org/10.4028/www.scientific.net/AMR.291-294.614
• Online since: July 2011
• Authors: Yun Liu, Yu Ling Guo, Da Wei Chen, Cheng Peng, Yun Jun Yan
• Keywords: Burkholderia Cepacia Lipase (BCL), Circular Dichroism (CD), Ross-Linked Enzyme Aggregates (CLEAS), Scanning Electron Microscope (SEM), Sol-Gel Encapsulation

References

[1] L. Cao, F. van Rantwijk and R.A. Sheldon: Org. Lett.Vol. 2, April 2000, pp.1361-1364.

[2] R. Schoevaart, M.W. Wolbers, M. Golubovic, M. Ottens, A.P.G. Kieboom, F. van Rantwijk, L.A.M. van der Wielen, R.A. Sheldon: Biotechnol. Bioeng., vol. 87, Sep. 2004, pp.754-762.

DOI: 10.1002/bit.20184

[3] S. Shah, A. Sharma, M.N. Gupta: Anal. Biochem., vol. 351, April 2006, pp.207-213.

[4] I. Matijosyte, I.W.C.E. Arends, S. de Vries, R.A. Sheldon: J. Mol. Catal. B: Enzym., vol. 62, Feb. 2010, pp.142-148.

[5] R.A. Sheldon, R. Schoevaart, L.M. van Langen: Biocatal. Biotransfor., vol. 23, May 2005, pp.141-147.

[6] B.S. Aytar and U. Bakir: Process Biochem., vol.43, Feb.2008, pp.125-131.

[7] D.I. Perez, F. van Rantwijk, R.A. Sheldon: Adv. Synth. Catal., vol. 351, Sep. 2009, pp.2133-2139.

DOI: 10.1002/adsc.200900303

[8] A.E. Fazary, S. Ismadji, Y.H. Ju: Int. J. Biol. Macromol., vol. 44, Apr. 2009, pp.240-248.

[9] F. Lopez-Gallego, L. Betancor, A. Hidalgo, N. Alonso, R. Fernández-Lafuente, J.M. Guisán: Biomacromolecules, vol. 6, Jul-Aug. 2005, pp.1839-1842.

DOI: 10.1021/bm050088e

[10] P. Kaul, A. Stolz , U. C. Banerjee: Adv. Synth. Catal., vol. 349, Aug. 2007, pp.2167-2176.

[11] N.A. Pchelintsev, M.I. Youshko, V.K. Švedas: J. Mol. Catal. B:Enzym., vol. 56, April 2009, pp.202-207.

[12] Y. Liu, H. Tan, X. Zhang, Y.J. Yan, B.H. Hameed: Process Biochem., vol. 45, March 2010, pp.1176-1180.

[13] Y. Liu, Y.J. Yan, X. Zhang, H. Tan, H.L. Xin, A.Yao: AIChE J., vol. 56, June 2010, pp.1659-1665.

[14] M. Petkar, A. Lali, P. Caimi, M. Daminati: J Mol Catal B: Enzym vol. 39, March 2006, pp.83-90.

[15] S. Shah, A. Sharma, M. N. Gupta: Anal. Biochem., vol. 351, Apr. 2006, pp.207-213.

[16] R. Tyagi, R. Batra, M.N. Gupta: Enzyme Microb. Technol., vol. 24, Oct. 1999, pp.348-353.

[17] R. Schoevaart, M.W. Wolbers, M. Golubovic, M. Ottens, A.P.G. Kieboom, F.V. Rantwijik, L.A.M. van der Wielen, R.A. Sheldon: Biotechnol. Bioeng., vol. 20, Sep. 2004, pp.754-762.

DOI: 10.1002/bit.20184

[18] S. Pan, X. Liu, Y. Xie, Y. Yi, C. Li, Y. Yan, Y. Liu: Bioresource Technol., vol. 101 Aug. 2010, pp.9822-9824.