Article

Cellulose

, Volume 18, Issue 5, pp 1251-1256

Immobilization of protein on cellulose hydrogel

  • Noriyuki IsobeAffiliated withDepartment of Biomaterials Science, Graduate School of Agricultural and Life Sciences, The University of Tokyo
  • , Da-Sol LeeAffiliated withDepartment of Plant and Environmental New Resources, College of Life Sciences, Kyung Hee University
  • , Ye-Jin KwonAffiliated withDepartment of Plant and Environmental New Resources, College of Life Sciences, Kyung Hee University
  • , Satoshi KimuraAffiliated withDepartment of Biomaterials Science, Graduate School of Agricultural and Life Sciences, The University of TokyoDepartment of Plant and Environmental New Resources, College of Life Sciences, Kyung Hee University
  • , Shigenori KugaAffiliated withDepartment of Biomaterials Science, Graduate School of Agricultural and Life Sciences, The University of Tokyo
  • , Masahisa WadaAffiliated withDepartment of Biomaterials Science, Graduate School of Agricultural and Life Sciences, The University of TokyoDepartment of Plant and Environmental New Resources, College of Life Sciences, Kyung Hee University
  • , Ung-Jin KimAffiliated withDepartment of Plant and Environmental New Resources, College of Life Sciences, Kyung Hee UniversityBioenergy Research Center, College of Life Sciences, Kyung Hee University Email author 

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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 hydrogel Periodate oxidation Dialdehyde cellulose Immobilized enzyme Biomaterials