Cellulose

, 18:1251

Immobilization of protein on cellulose hydrogel

Authors

  • Noriyuki Isobe
    • Department of Biomaterials Science, Graduate School of Agricultural and Life SciencesThe University of Tokyo
  • Da-Sol Lee
    • Department of Plant and Environmental New Resources, College of Life SciencesKyung Hee University
  • Ye-Jin Kwon
    • Department of Plant and Environmental New Resources, College of Life SciencesKyung Hee University
  • Satoshi Kimura
    • Department of Biomaterials Science, Graduate School of Agricultural and Life SciencesThe University of Tokyo
    • Department of Plant and Environmental New Resources, College of Life SciencesKyung Hee University
  • Shigenori Kuga
    • Department of Biomaterials Science, Graduate School of Agricultural and Life SciencesThe University of Tokyo
  • Masahisa Wada
    • Department of Biomaterials Science, Graduate School of Agricultural and Life SciencesThe University of Tokyo
    • Department of Plant and Environmental New Resources, College of Life SciencesKyung Hee University
    • Department of Plant and Environmental New Resources, College of Life SciencesKyung Hee University
    • Bioenergy Research Center, College of Life SciencesKyung Hee University
Article

DOI: 10.1007/s10570-011-9561-8

Cite this article as:
Isobe, N., Lee, D., Kwon, Y. et al. Cellulose (2011) 18: 1251. doi:10.1007/s10570-011-9561-8

Abstract

A technique of immobilizing an enzyme/antibody was developed using cellulose hydrogel prepared from an aqueous alkali-urea solvent. Partial oxidation by sodium periodate activated the cellulose gel for introducing aldehyde groups. Proteins were covalently introduced to cellulose gel by a Schiff base formation between the aldehyde and the amino groups of proteins, and stabilized by a reduction of imines. Coloring reactions confirmed the high activity of the immobilized enzymes. The activity of the immobilized enzymes increased with aldehyde content, but the effect leveled off at a low degree of oxidation, at approximately 8.1 of oxidized glucose/100 glucose unit. The amount of immobilized peroxidase calculated from the activity was 8.0 ng/g for an aldehyde content of 0.18 mmol/g: 14.6 ng/g for both 0.46 mmol/g and 1.04 mmol/g. The same method could be applied to the peroxidase antibody. Thus, various active proteins could be immobilized on cellulose gels by mild and facile processing. Owing to high mechanical and chemical stability of cellulose, this technique and resulting materials are potentially useful in biochemical processing and sensing technologies.

Keywords

Cellulose hydrogelPeriodate oxidationDialdehyde celluloseImmobilized enzymeBiomaterials

Copyright information

© Springer Science+Business Media B.V. 2011