Premium
High pressure unfolding of ovalbumin
Author(s) -
Smith Drummond,
Galazka Vanda B.,
Wellner Nicholas,
Sumner Ian G.
Publication year - 2000
Publication title -
international journal of food science and technology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.831
H-Index - 96
eISSN - 1365-2621
pISSN - 0950-5423
DOI - 10.1046/j.1365-2621.2000.00395.x
Subject(s) - ovalbumin , chemistry , circular dichroism , molten globule , quenching (fluorescence) , fourier transform infrared spectroscopy , folding (dsp implementation) , protein folding , fluorescence , solvent , fluorescence spectroscopy , protein secondary structure , spectroscopy , naphthalene , photochemistry , crystallography , organic chemistry , biochemistry , chemical engineering , physics , immune system , electrical engineering , quantum mechanics , engineering , immunology , biology
Summary The effects of high pressure processing of ovalbumin have been investigated. After treatment with pressures in excess of 400 MPa at pH 6.5, circular dichroism (CD) and Fourier transform infra‐red spectroscopy (FTIR) spectroscopy showed limited irreversible changes in secondary structure. Fluorescence and derivative spectroscopy as well as fluorescence‐quenching experiments indicated greater solvent exposure of aromatic residues in pressure‐treated protein. Pressure treatment also caused enhanced binding of anilino‐1‐naphthalene‐8‐sulphonic acid (ANS). The pressure necessary to cause these changes was lower at low pH. These data indicate a pressure‐induced molten‐globule formation. The pressurized protein may be structurally similar to forms of the protein found at acid pH or as intermediates in protein folding.