title: Probing thermal behaviour of microbial transglutaminase with fluorescence and in silico methods.
abstract: BACKGROUND
  Knowledge of transglutaminase behaviour at thermal treatment allows efficient applications in food processing. The heat-induced conformational changes of microbial transglutaminase were studied by fluorescence spectroscopy and a molecular modelling approach.
  
  
  RESULTS
  The experimental results indicate the unfolding of transglutaminase in a single-phase reaction, at temperatures over 60 °C. The incidence of conformational changes is also supported by the increase of both intrinsic and 1-anilino-8-naphthalene sulfonate fluorescence intensity with temperature. Changes in the secondary and tertiary structure of transglutaminase were outlined after running molecular dynamics simulations at temperatures ranging from 25 °C to 80 °C.
  
  
  CONCLUSIONS
  The motif's particularities varied with the temperature, suggesting structural rearrangements of the protein, mainly in helices. The largest deviation from the structure equilibrated at 25 °C was observed at 80 °C.
authors: Dunarea de Jos University of Galati, Faculty of Food Science and Engineering, Galati, Romania.
authors: Iuliana
authors: I
authors: Aprodu
authors: Nicoleta
authors: N
authors: Stănciuc
authors: Iuliana
authors: I
authors: Banu
authors: Gabriela
authors: G
authors: Bahrim
mesh_terms: D001426:Bacterial Proteins / Q000737:chemistry*; D003198:Computer Simulation; D005511:Food Handling; D005516:Food Microbiology; D006358:Hot Temperature; D006801:Humans; D011489:Protein Denaturation; D017510:Protein Folding; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D013050:Spectrometry, Fluorescence; D011503:Transglutaminases / Q000737:chemistry*
chemical_list: D001426:Bacterial Proteins; D011503:Transglutaminases