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pH Affects the Thermal Inactivation Parameters of R‐Phycoerythrin from Porphyra yezoensis
Author(s) -
OrtaRamirez A.,
Merrill J.E.,
Smith D.M.
Publication year - 2000
Publication title -
journal of food science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.772
H-Index - 150
eISSN - 1750-3841
pISSN - 0022-1147
DOI - 10.1111/j.1365-2621.2000.tb09415.x
Subject(s) - phycoerythrin , isoelectric point , chemistry , porphyra , molecular mass , chromatography , kinetics , fluorescence , biochemistry , food science , analytical chemistry (journal) , microbiology and biotechnology , biology , enzyme , botany , algae , flow cytometry , physics , quantum mechanics
R‐phycoerythrin (PE), a protein that fluoresces in the visible range, was purified from Porphyra yezoensis. PE had a molecular mass of 292 kDa and an isoelectric point of 4.1 to 4.2. Thermal inactivation parameters of PE, calculated on the basis of fluorescence loss, were determined under different pH conditions. PE was more thermostable between pH 5.0 and 8.0, and became more heat sensitive at pH 4.0 and 10.0. PE at pH 6.0 had the highest D value (12258.7 min) at 70 °C. The z values of PE increased from 4.58 °C at pH 5.0 to 9.15 °C at pH 9.0. PE could be used as a time‐temperature integrator by adjusting the inactivation kinetics of PE to match those of target microorganisms in a thermal process.