Hemoglobin Immobilized Peroxidase Activity

Enzymatic reaction and mimetic enzyme are the most important issues in the pop fields such as supramolecular chemistry and biomimetic chemistry. Enzymatic polymerization has extensive application in the synthesis of special functional polymer materials. The peroxidase activity of hemoglobin (Hb) was studied because the same active site of Hb to horseradish peroxidase (HRP). The immobilization of Hb was investigated to increase its utilization ratio.Several samples of Hb crosslinked by Glutaraldehyde (GTA) were preparated in different molar ratio of GTA to Hb. Images of the crosslinked Hb molecular were taken by AFM. With the increase of molar ratio, the number of Hb molecular crosslinked increased, so does the molecular size. The peroxidase activity of the Hb declined in a certain degree compared to non-crosslinked Hb tested by Trinder reaction.Hemoglobin was embeded in polyvinylalcoho-acrylic acid (PVA-AAc) hydrogel prepared by irradiation. There are some factors affect the swelling capacity of PVA-AAc hydrogel, such as the degree of PVA, the content of AAc, and irradiation dose. Nano-silver PVA-AAc hydrogel was prepared, and the translating ratio of Ag~+ to Ag and the releasing velocity of siver in water were also investigated. The peroxidase activity of the Hb in the hydrogel was under research, too.Poly-o-phenylenediamine (PoPD) was selectively catalysed by Hb and immobilized Hb in aqueous micell solution. The structure and property of the polymer were investigated by IR, FL, CV, GPC, XRD and ~1HNMR. Thermal analysis shows that the PoPD catalysed by Hb and crosslinked Hb have perfect thermostability, and with only 15% loss of weight in 35O℃. AFM was used to get the image of PoPD, the polymer particles are evenly dispersed on mica base. When it was observed under a smaller range (625nm×625nm), we find that the grain diameter is under 100nm, which matches up to the result we get by XRD.