Effects of high pressure and low temperature on β-lactoglobulin unfolding and aggregation
- 31 May 2001
- journal article
- Published by Elsevier in Food Hydrocolloids
- Vol. 15 (3) , 215-232
- https://doi.org/10.1016/s0268-005x(01)00017-0
Abstract
No abstract availableKeywords
This publication has 50 references indexed in Scilit:
- High-pressure effects on β-lactoglobulin interactions with ligands studied by fluorescencePublished by Elsevier ,2003
- Enzyme sensitivity towards high pressure at low temperatureFood Biotechnology, 1998
- Structure of Pressure-Assisted Cold Denatured Lysozyme and Comparison with Lysozyme Folding IntermediatesBiochemistry, 1997
- Structure of the Pressure-Assisted Cold Denatured State of UbiquitinBiochemical and Biophysical Research Communications, 1997
- The Role of Phenylalanine 31 in Maintaining the Conformational Stability of Ribonuclease P2 from Sulfolobus solfataricus under Extreme Conditions of Temperature and PressureBiochemistry, 1997
- Pressure effects on the stability of lipoxygenase: Fourier transform-infrared spectroscopy (FT-IR) and enzyme activity studiesZeitschrift für Lebensmittel-Untersuchung und Forschung, 1995
- Cold-induced conformational changes of ribonuclease A as investigated by subzero transverse temperature gradient gel electrophoresisBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1994
- Heat and cold denaturation of β‐lactoglobulin BFEBS Letters, 1992
- The cold‐induced denaturation of lactate dehydrogenase at sub‐zero temperatures in the absence of perturbantsFEBS Letters, 1989
- Fourth‐Derivative Spectrophotometry Analysis of Tryptophan Environment in ProteinsEuropean Journal of Biochemistry, 1983