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Probing thermal behaviour of microbial transglutaminase with fluorescence and in silico methods
Author(s) -
Aprodu Iuliana,
Stănciuc Nicoleta,
Banu Iuliana,
Bahrim Gabriela
Publication year - 2012
Publication title -
journal of the science of food and agriculture
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.782
H-Index - 142
eISSN - 1097-0010
pISSN - 0022-5142
DOI - 10.1002/jsfa.5799
Subject(s) - tissue transglutaminase , chemistry , fluorescence , in silico , protein tertiary structure , conformational change , fluorescence spectroscopy , protein secondary structure , molecular dynamics , protein structure , biophysics , biochemistry , enzyme , computational chemistry , biology , quantum mechanics , gene , physics
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. CONCLUSION: 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. © 2012 Society of Chemical Industry