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Interaction of sodium benzoate with trypsin by spectroscopic techniques.

Spectrochimica acta. Part A, Molecular and biomolecular spectroscopy (2011-09-06)
Yue Mu, Jing Lin, Rutao Liu
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.

MATERIALS
Product Number
Brand
Product Description

Supelco
Sodium benzoate, Pharmaceutical Secondary Standard; Certified Reference Material
Sigma-Aldrich
Sodium benzoate, ReagentPlus®, 99%
Sigma-Aldrich
Sodium benzoate, BioXtra, ≥99.5%
Sigma-Aldrich
Sodium benzoate, puriss., meets analytical specification of Ph. Eur., BP, FCC, E211, 99.0-100.5% (calc. to the dried substance), powder
Sigma-Aldrich
Sodium benzoate, purum p.a., ≥99.0% (NT)