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Study On The Characters Of Hemoglobin By Recombining Hemoglobin Using Chemically Modified Heme

Posted on:2012-11-02Degree:MasterType:Thesis
Country:ChinaCandidate:H S LingFull Text:PDF
GTID:2120330335964445Subject:Biochemistry and Molecular Biology
Abstract/Summary:PDF Full Text Request
As an efficient biocatalyst, peroxidase is a scavenger of peroxide in vivo. It can catalyze many reactions that protect cells, antioxidant, anti-aging, and it has been widely used in food, cosmetics fields and biochemical reagents. Nevertheless, its further industrial application is greatly limited due to its low thermostability and low reactivity in organic media, and also is very expensive when application in industry. In this study, Phenol or 4-Biphenylol was used to modify the hemin to improve the characteristics of hemoglobin(Hb). The modified hemin group was recombined with apo-hemoglobin to prepare a novel artificial hemoglobin. Absorption spectral scan demonstrated that the artificial recombined hemoglobins with modified hemin were successfully obtained. The experimental results showed that the peroxidase-like activity of modified hemoglobins have been enhanced compared to that of native hemoglobin, and the enzymatic activity of modified hemoglobin with 4-Biphenylol modified hemin was as about 1.6 folds high as that of native hemoglobin.The cofactor modification increased the themostability or tolerance of HB both in aqueous buffer and some organic solvents. The effects of temperature on hemoglobin activity were that, the decline curve of the modified hemoglobin, such as after putting 4-Biphenylol Hb in the water at 40℃for 10 min, the experimental results showed that the peroxidase-like activity of it was still able to maintain 80%relatively, which showed that the heat resistance of the reassembly of hemoglobin has been improved, increased by about 20% compared with natural hemoglobin. Enzymatic tolerance of modified hemoglobins in acetone, acetonitrile, dimethyl sulfoxide, ethanol, and tetrahydrofuranwe five organic solvents were stronger than that of the control, and the residual enzymatic activity kept higher as the concentration of organic solvents increased.
Keywords/Search Tags:chemical modification, heme, hemoglobin, peroxidase, enzymatic activity
PDF Full Text Request
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