title: Interaction of sodium benzoate with trypsin by spectroscopic techniques.
abstract: The toxicity of sodium benzoate to trypsin was investigated by fluorescence spectroscopy, synchronous fluorescence spectroscopy, UV-visible absorption spectroscopy and circular dichroism (CD) spectroscopy under mimic physiological conditions. Sodium benzoate could unfold trypsin by decreasing the β-sheet structure, which leads to more exposure of internal amino acid groups and the obvious intrinsic fluorescence quenching with the rising concentration of sodium benzoate. The results of spectroscopic measurements indicated that sodium benzoate changed the internal microenvironment of trypsin and induced the alteration of the whole molecule, which were performed toxic effects on the organism. Trypsin and sodium benzoate interacted with each other to produce a substance by van der Waals forces and hydrogen bond, the model of which was shown by AutoDock software.
authors: Shandong Key Laboratory of Water Pollution Control and Resource Reuse, School of Environmental Science and Engineering, Shandong University, Shandong Province, Jinan, PR China.
authors: Yue
authors: Y
authors: Mu
authors: Jing
authors: J
authors: Lin
authors: Rutao
authors: R
authors: Liu
mesh_terms: D000818:Animals; D002417:Cattle; D002942:Circular Dichroism; D005520:Food Preservatives / Q000633:toxicity*; D006860:Hydrogen Bonding; D008958:Models, Molecular; D011485:Protein Binding; D011487:Protein Conformation; D020160:Sodium Benzoate / Q000633:toxicity*; D013050:Spectrometry, Fluorescence; D014357:Trypsin / Q000737:chemistry / Q000378:metabolism*
chemical_list: D005520:Food Preservatives; D014357:Trypsin; D020160:Sodium Benzoate