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The Primary Study On Some Enzyme Properties Of Pepsin Processed By Biological Molecule

Posted on:2008-01-18Degree:MasterType:Thesis
Country:ChinaCandidate:Z LiFull Text:PDF
GTID:2120360242963683Subject:Biochemistry and Molecular Biology
Abstract/Summary:PDF Full Text Request
Oleanolic Acid & Rutin as natural medicine take(?) orally will inevitably interact with digestive enzymes. So we studied the effect of Oleanolic Acid & Rutin on the important digestive enzymes.We chose pepsin which is important in digestion of amylum and saccharide that play key role in digestion of proteins. First, importantwe studied the effect of Oleanolic Acid & Rutin on activity of pepsin, then, we studied the effect of Oleanolic Acid & Rutin on structure of pepsin by UV spectra and fluorescence spectra.Through experiment we found that Oleanolic Acid could inhibit the digestive enzymes. When the concentration ratio of Oleanolic Acid to enzymes is 5/1, the inhibition ratios of Oleanolic Acid on the enzymes are 26.6%.When We adding different concentrations of Oleanolic Acid & Rutin into the enzymes, the UV absorption of pepsin rised according to the rising concentration of Oleanolic Acid. The Oleanolic Acid & Rutin treatment led to the quenching of intrinsic fluorescence of the enzymes. The Lineweaver-Burk plots showed that the quenching of Oleanolic Acid to the enzymes was probably a static quenching process, the quenching constant K of pepsin is 1.81×10~4 L/mol.s. The number of binding sites of pepsin is 1.2. The quenching of Rutin to the enzymes was probably a static quenching process also, the quenching constant K of pepsin is 1.80×10~6 L/mol·s. The number of binding sites of pepsin is 1.19.
Keywords/Search Tags:Oleanolic Acid, Rutin, Pepsin, UV spectra, Fluorescence spectra
PDF Full Text Request
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