Cellulose can be easily oxidized to oxycellulose with periodic acid

which can serve as a carrier for the immobilization of hemoglobin acting like a bionic gill

to extract oxygen from sea water

which may provide a source of oxygen for human life support in an undersea environment.The present paper studied the mechanism of hemoglobin immobilization on periodate oxycellulose.It was found that only by the unique activation procedure

that the cotton was first oxidized with NaIO 4

then treated with 5.0mol/L NaOH and again oxidized with NaIO4

the carrier thus obtained was able to immobilize a very high amount of Hb

i.e.1.0g Hb/g cellulose.When cellulose was oxidized only once with NaIO4

although the aldehyde group content was rather high

the linking amount of Hb was very low.The mechanism was studied by means of X-diffractioin

infrared spectrum and determination of functional groups.It was found that Hb was immobilized by the interaction between the aldehyde groups in the oxycellulose and the amino groups on Hb.And the microcrystalline structure in cellulose was the main hindrance in immobilization process.Alkaline degradation of periodate oxycellulose led to destruction of the microcrystalline structure.The alkaline degradation and Cannizzaro reaction also resulted in a complete loss of aldehyde groups.In order to obtain maximum amount of immobilized Hb

a second oxidation with NaIO4 was necessary to produce aldehyde groups.