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Development of (α-Amylase Coated Magnetic Nanofiber for the Hydrolysis of Starch.

(α-Amylase가 고정화된 Magnetic Nanofiber를 이용한 전분 분해공정 개발

  • Kim, Hyun (Department of Chemical and Biochemical Engineering Chosun University) ;
  • Lee, Jung-Heon (Department of Chemical and Biochemical Engineering Chosun University)
  • 김현 (조선대학교 생명화학공학과) ;
  • 이중헌 (조선대학교 생명화학공학과)
  • Published : 2007.09.30

Abstract

Magnetically separable enzyme-coated nanofibers were developed for the hydrolysis of starch. Stability of ${\alpha}-amylase-coated$ nanofiber was greatly improved and its residual activity was maintained over 92.7% after 32 days incubation at room temperature and under shaking conditions (200 rpm). The recovery of enzyme was high and enzyme activity after 10 recycle was 95.2% of its original activity. Developed enzyme-coated nanofibers were used for the hydrolysis of starch. When 0.5 mg of magnetically separable enzyme nanofibers was used, 40 g/l of starch (2 ml) was completely degraded within 40 min. The continuous enzyme reactor was developed and used for starch hydrolysis and 76% of starch (30 g/l) was hydrolyzed with 1 hr residence time.

References

  1. Bai, S., Z. Guo, W. Liu and Y. Sun. 2006. Resolution of (+/-)-menthol by immobilized Candida rugosa lipase on superparamagnetic nanoparticles. Food Chemistry 96, 1-7 https://doi.org/10.1016/j.foodchem.2005.01.047
  2. Chen, J. P. and W. S. Lin. 2003. Sol-gel powders and supported sol-gel polymers for immobilization of lipase in ester synthesis. Enzyme and Microbial Technology 32, 801-811 https://doi.org/10.1016/S0141-0229(03)00052-8
  3. Hong, J., P. Gong, D. Xu, L. Dong and S. Yao. 2007. Stabilization of [alpha]-chymotrypsin by covalent immobilization on amine-functionalized superparamagnetic nanogel. Journal of Biotechnology 128, 597-605 https://doi.org/10.1016/j.jbiotec.2006.11.016
  4. Hong, J., D. Xu, P. Gong, H. Sun, L. Dong and S. Yao. 2007. Covalent binding of [alpha]-chymotrypsin on the magnetic nanogels covered by amino groups. Journal of molecular catalysis. B, Enzymatic 45, 84-90 https://doi.org/10.1016/j.molcatb.2006.11.009
  5. Jiang, D. S., S. Y. Long, J. Huang, H. Y. Xiao and J. Y. Zhou. 2005. Immobilization of Pycnoporus sanguineus laccase on magnetic chitosan microspheres. Biochemical Engineering Journal 25, 15-23 https://doi.org/10.1016/j.bej.2005.03.007
  6. Kim, B. C. S. Nair, J. Kim, J. H. Kwak, J. W. Grate, S. H. Kim and M. B. Gu. 2005. Preparation of biocatalytic nanofibres with high activity and stability via enzyme aggregate coating on polymer nanofibres. Nanotechnology 7, S382-S388
  7. Kim, J., H. Jia and P. Wang. 2006. Challenges in biocatalysis for enzyme-based biofuel cells. Biotechnol. Adv. 30, 25-33
  8. Lozano, P., E. Garcia-Verdugo, R. Piamtongkam, N. Karbass, T. D. Diego, M. I. Burguete, S. V. Luis and J. L. Iborra. 2007. Bioreactors Based on Monolith-Supported Tonic Liquid Phase for Enzyme Catalysis in Supercritical Carbon Dioxide. Advanced Synthesis & Catalysis 349, 1077-1084 https://doi.org/10.1002/adsc.200600554
  9. van Roon, J. L., R. M. Boom, M. A. Paasman, J. Tramper, C. G. Schroen and H. H. Beeftink. 2005. Enzyme distribution and matrix characteristics in biocatalytic particles. Journal of Biotechnol. 119, 400-415 https://doi.org/10.1016/j.jbiotec.2005.04.012
  10. Wang, W., L. Deng, Z. H. Peng and X. Xiao. 2007. Study of the epoxydized magnetic hydroxyl particles as a carrier for immobilizing penicillin G acylase. Enzyme and Microbial Technology 40, 255-561 https://doi.org/10.1016/j.enzmictec.2006.04.020
  11. Zayats, M., R. Baron, I. Popov and I. Willner. 2005. Biocatalytic growth of Au nanoparticles: from mechanistic aspects to biosensors design. Nano Lett. 5, 21-25 https://doi.org/10.1021/nl048547p

Cited by

  1. Nanomaterials as novel supports for the immobilization of amylolytic enzymes and their applications: A review vol.3, pp.1, 2017, https://doi.org/10.1515/boca-2017-0004