Immobilization of Lecitase? Ultra onto a Novel Polystyrene DA-201 Resin: Characterization and Biochemical Properties
详细信息 查看全文
- 作者：Ning Liu (1)
Min Fu (1)
Yong Wang (2)
Qiangzhong Zhao (1)
Weizheng Sun (1)
Mouming Zhao (1) - 关键词：Lecitase? ultra ; Immobilization ; Adsorption ; FTIR ; Esterification
- 刊名：Applied Biochemistry and Biotechnology
- 出版年：2012
- 出版时间：November 2012
- 年：2012
- 卷：168
- 期：5
- 页码：1108-1120
- 全文大小：443KB
- 参考文献：1. Bojsen, K., Svendsen, A., Fuglsang, C. C., Patear, S., Borch, K., Vind, J., et al.. (2000). Novozymes A/S, Denmark. PCT International Application WO2000/32758.
2. Fernandez-Lorente, G., Filice, M., Terreni, M., Guisan, J. M., Fernandez-Lafuente, R., & Palomo, J. M. (2008). Lecitase? ultra as regioselective biocatalyst in the hydrolysis of fully protected carbohydrates strong modulation by using different immobilization protocols. / Journal of Molecular Catalysis B: Enzymatic, 51, 110-17. CrossRef
3. Sheelu, G., Kavitha, G., & Fadnavis, N. W. (2008). Efficient immobilization of lecitase in gelatin hydrogel and degumming of rice bran oil using a spinning basket reactor. / Journal of the American Oil Chemists-Society, 85, 739-48. CrossRef
4. Yang, B., Wang, Y. H., & Yang, J. G. (2006). Optimization of enzymatic degumming process for rapeseed oil. / Journal of the American Oil Chemists-Society, 83, 653-58. CrossRef
5. Mishra, M. K., Kumaraguru, T., Sheelu, G., & Fadnavis, N. W. (2009). Lipase activity of Lecitase? Ultra: characterization and applications in enantioselective reactions. / Tetrahedron: Asymmetry, 20, 2854-860. CrossRef
6. Wang, Y., Zhao, M., Song, K., Wang, L., Tang, S., & William, W. R. (2010). Partial hydrolysis of soybean oil by phospholipase A1 (Lecitase Ultra). / Food Chemistry, 121, 1066-072. CrossRef
7. Liu, N., Wang, Y., Zhao, Q., Zhang, Q., & Zhao, M. (2011). Fast synthesis of 1,3-DAG by Lecitase? Ultra-catalyzed esterification in solvent-free system. / European Journal of Lipid Science and Technology, 113, 973-79. CrossRef
8. Iyer, P. V., & Ananthanarayan, L. (2008). Enzyme stability and stabilization—aqueous and non-aqueous environment. / Process Biochemistry, 43, 1019-032. CrossRef
9. Fernandez-Lorente, G., Palomo, J. M., Guisan, J. M., & Fernandez-Lafuente, R. (2007). Effect of the immobilization protocol in the activity, stability, and enantioselectivity of Lecitase? Ultra. / Journal of Molecular Catalysis B: Enzymatic, 47, 99-04. CrossRef
10. Cabrera, Z., Fernandez-Lorente, G., Palomo, J. M., Guisan, J. M., & Fernandez-Lafuente, R. (2008). Asymmetric hydrolysis of dimethyl 3-phenylglutarate catalyzed by Lecitase Ultra?: effect of the immobilization protocol on its catalytic properties. / Enzyme and Microbial Technology, 43, 531-36. CrossRef
11. Garcia-Galan, C., Berenguer-Murcia, A., Fernandez-Lafuente, R., & Rodrigues, R. C. (2011). Potential of different enzyme immobilization strategies to improve enzyme performance. / Advanced Synthesis and Catalysis, 353, 2885-904. CrossRef
12. Mateo, C., Palomo, J. M., Fernandez-Lorente, G., Guisan, J. M., & Fernandez-Lafuente, R. (2007). Improvement of enzyme activity, stability and selectivity via immobilization techniques. / Enzyme and Microbial Technology, 40, 1451-463. CrossRef
13. Hernandez, K., Garcia-Galan, C., & Fernandez-Lafuente, R. (2011). Simple and efficient immobilization of lipase B from / Candida antarctica on porous styrene–divinylbenzene beads. / Enzyme and Microbial Technology, 49, 72-8. CrossRef
14. Liu, T., Liu, Y., Wang, X., Li, Q., Wang, J., & Yan, Y. (2011). Improving catalytic performance of / Burkholderia cepacia lipase immobilized on macroporous resin NKA. / Journal of Molecular Catalysis B: Enzymatic, 71, 45-0. CrossRef
15. Shi, Z., & Shi, R. (2005). / The application of resin for adsorption and separation in medical industry. Beijing: Chemical Industry.
16. Cheirsilp, B., Jeamjounkhaw, P., & H-Kittikun, A. (2009). Optimizing an alginate immobilized lipase for monoacylglycerol production by the glycerolysis reaction. / Journal of Molecular Catalysis B: Enzymatic, 59, 206-11. CrossRef
17. Byler, D. M., & Susi, H. (1986). Examination of the secondary structure of proteins by deconvolved FTIR spectra. / Biopolymers, 25, 469-87. CrossRef
18. Gao, Y., Tan, T. W., Nie, K. L., & Wang, F. (2006). Immobilization of lipase on macroporous resin and its application in synthesis of biodiesel in low aqueous media. / Chinese Journal of Biotechnology, 22, 114-18. CrossRef
19. Rodrigues, R. C., & Fernandez-Lafuente, R. (2010). Lipase from / Rhizomucor miehei as a biocatalyst in fats and oils modification. / Journal of Molecular Catalysis B: Enzymatic, 66, 15-2. CrossRef
20. Fernandez-Lorente, G., Palomo, J. M., Cabrera, Z., Guisan, J. M., & Fernandez-Lafuente, R. (2007). Specificity enhancement towards hydrophobic substrates by immobilization of lipases by interfacial activation on hydrophobic supports. / Enzyme and Microbial Technology, 41, 565-69. CrossRef
21. Wilson, L., Palomo, J. M., Fernandez-Lorente, G., Illanes, A., Guisan, J. M., & Fernandez-Lafuente, R. (2006). Effect of lipase-lipase interactions in the activity, stability and specificity of a lipase from / Alcaligenes sp. / Enzyme and Microbial Technology, 39, 259-64. CrossRef
22. Al-Duri, B., & Yong, Y. P. (1997). Characterisation of the equilibrium behaviour of lipase PS (from / Pseudomonas) and lipolase 100L (from / Humicola) onto Accurel EP100. / Journal of Molecular Catalysis B: Enzymatic, 3, 177-88. CrossRef
23. Hoshino, K., Taniguchi, M., Katagiri, M., & Fujii, M. (1992). Properties of amylase immobilized on a new reversibly soluble–insoluble polymer and its application to repeated hydrolysis of soluble starch. / Journal of Chemical Engineering of Japan, 25, 569-74. CrossRef
24. Serefoglou, E., Litina, K., Gournis, D., Kalogeris, E., Tzialla, A. A., Pavlidis, I. V., et al. (2000). Smectite clays as solid supports for immobilization of glucosidase: synthesis, characterization, and biochemical properties. / Chemistry of Materials, 28, 4106-115.
25. Kharrat, N., Ali, Y. B., Marzouk, S., Gargouri, Y., & Karra-Chaabouni, M. (2011). Immobilization of / Rhizopus oryzae lipase on silica aerogels by adsorption: comparison with the free enzyme. / Process Biochemistry, 46, 1083-089. CrossRef
26. Peng, R., Lin, J., & Wei, D. (2010). Purification and characterization of an organic solvent-tolerant lipase from / Pseudomonas aeruginosa CS-2. / Applied Biochemistry and Biotechnology, 162, 733-43. CrossRef
27. Rahman, R. N. Z. R. A., Bahrum, S. N., Salleh, A. B., & Basri, M. (2006). S5 lipase: an organic solvent tolerant enzyme. / Journal of Microbiology, 44, 583-90.
28. Brady, D., & Jordaan, J. (2009). Advances in enzyme immobilisation. / Biotechnology Letters, 31, 1639-650. CrossRef - 作者单位：Ning Liu (1)
Min Fu (1)
Yong Wang (2)
Qiangzhong Zhao (1)
Weizheng Sun (1)
Mouming Zhao (1)
1. College of Light Industry and Food Sciences, South China University of Technology, Guangzhou, 510640, China
2. Department of Food Science and Engineering, Jinan University, Guangzhou, 510632, China - ISSN：1559-0291
文摘
A simple, rapid, and economic method of enzyme immobilization was developed for phospholipase Lecitase? ultra (LU) via interfacial adsorption. The effect of nature of the polystyrene supports and the kinetic behavior and stability of immobilized lecitase? ultra (IM-LU) were evaluated. Six macroporous resins (AB-8, X-5, DA-201, NKA-9, D101, D4006) and two anion resins (D318 and D201) were studied as the supports. DA-201 resin was selected because of its best immobilization effect for LU. Immobilization conditions were investigated, including immobilization time, pH, and enzyme concentration. IM-LU with a lipase activity of 1,652.4?±-.6?U/g was obtained. The adsorption process was modeled by Langmuir and Freundlich equations, and the experimental data were better fit for the former one. The kinetic constant (K m) values were found to be 192.7?±-.2?mM for the free LU and 249.3?±-.4?mM for the IM-LU, respectively. The V max value of free LU (169.5?±-.3?mM/min) was higher than that of the IM-LU (53.8?±-.5?mM/min). Combined strategies of scanning electron micrograph, thermogravimetric analysis, and Fourier transform infrared (FTIR) spectroscopy were employed to characterize the IM-LU. FTIR spectroscopy showed that the secondary conformation of the enzyme had changed after immobilization, through which a decrease of α-helix content and an increase of β-sheet content were observed. The IM-LU possessed an improved thermal stability as well as metal ionic tolerance when compared with its free form. The reusability of IM-LU was also evaluated through catalyzing esterification reaction between oleic acid and glycerol. It exhibited approximately 70?% of relative esterification efficiency after six successive cycles. This immobilized enzyme on hydrophobic support may well be used for the synthesis of structural lipids in lipid area.