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Study On The Effect Of Mesoporous Polymer Channel Microenvironment On Enzyme Activity

Posted on:2021-03-12Degree:MasterType:Thesis
Country:ChinaCandidate:H T YangFull Text:PDF
GTID:2381330626454911Subject:Physical chemistry
Abstract/Summary:PDF Full Text Request
The engineering of enzymes is severely hampered due to their low operational stability and difficulty of reuse,while enzymes immobilization can effectively overcome these problems.The carrier microenvironment is an important factor affecting the immobilized enzyme.Therefore,studying the influence of carrier microenvironment on enzyme loading and activity has important theoretical significance and practical value.The main work of this dissertation is summarized as follows:1.In this dissertation,a series of ordered mesoporous polymers were synthesized by solvent volatilization-induced self-assembly method,and their Zeta potential was modulated by metal doping to achieve the loading of cytochrome C.The results show that the Zeta potential of the synthesized polymer carrier is different due to the doping of metal elements;the pure carbon polymer carrier cannot immobilize cytochrome C due to the mismatch of charge;as the carrier zeta potential increases,the enzyme load also increases,and there is a good linear relationship between the two.This shows that the Zeta potential of the carrier is a key factor in determining the supported enzyme catalyst loading.Among them,PTi O2 has the largest Zeta potential,reaching 24.5 m V,and its maximum load is 248 mg/g;the loading of Ti O2-1.03@C-N carrier with the smallest Zeta potential also reaches 97 mg/g.2.At room temperature,using toluene as a solvent,the activity and reusability of the enzyme were investigated by the oxidation reaction of pyrogallol in the presence of hydrogen peroxide.The results show that the activity of the immobilized enzyme is higher than that of the free enzyme,and the activity can reach up to 5.6 mg/min.mg.This is because the change in the Zeta potential of the carrier provides different microenvironments for the enzyme,and the electronic valence state of the Fe changes before and after immobilization.The diffraction peak of Fe3+ shifts to a high binding energy,which is more conducive to its generation Cyt CFe4+=O,to promote the reaction.The reaction rate is closely related to the Zeta potential of the carrier,and there is a clear linear relationship between the two.The immobilized enzyme has high stability.After many cycles,the enzyme can still maintain 80% of the activity;and after being left at low temperature for half a year,it still retains 30% of the activity.
Keywords/Search Tags:Immobilized enzyme, Zeta potential, Cytochrome C
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