title: Influence of disulfide bonds on the conformational changes and activities of refolded phytase.
abstract: Aspergillus sp. phytase contains five disulfide bonds. In order to elucidate their role, the reactivation and refolding of phytase in the absence and presence of dithiothreitol (DTT) was investigated. The results indicated that the disulfide bonds play an important role in the catalytic activity and conformational stability of the enzyme.
authors.affiliation: College of Life Science, Shandong Agricultural University, Shandong Tai'an 271018, People's Republic of China.
authors.forename: G Y
authors.initials: GY
authors.lastname: Song
authors.forename: X Y
authors.initials: XY
authors.lastname: Wang
authors.forename: M
authors.initials: M
authors.lastname: Wang
mesh_terms: D010832:6-Phytase / Q000737:chemistry* / Q000378:metabolism*; D002021:Buffers; D002942:Circular Dichroism; D004220:Disulfides / Q000378:metabolism*; D004229:Dithiothreitol / Q000494:pharmacology; D004789:Enzyme Activation / Q000187:drug effects; D006863:Hydrogen-Ion Concentration; D011489:Protein Denaturation / Q000187:drug effects; D017510:Protein Folding; D020673:Protein Renaturation; D012996:Solutions; D013050:Spectrometry, Fluorescence; D014508:Urea / Q000494:pharmacology
chemical_list: D002021:Buffers; D004220:Disulfides; D012996:Solutions; D014508:Urea; D010832:6-Phytase; D004229:Dithiothreitol