Induced structural change to β-lactoglobulin by combined pressure and temperature
Authors:
- L.-A TedfordLTL.-A Tedford
- C.J SchaschkeCSC.J Schaschke
- 1 April 2000
- journal article
- research article
- Published by Elsevier in Biochemical Engineering Journal
- Vol. 5 (1) , 73-76
Abstract
No abstract availableKeywords
This publication has 17 references indexed in Scilit:
- Review : High-pressure, microbial inactivation and food preservationFood Science and Technology International, 1995
- Exploiting the effects of high hydrostatic pressure in biotechnological applicationsTrends in Biotechnology, 1994
- High-Pressure Unfolding and Aggregation of .beta.-Lactoglobulin and the Baroprotective Effects of SucroseJournal of Agricultural and Food Chemistry, 1994
- Application of High Pressure for Spore Inactivation and Protein DenaturationJournal of Food Science, 1994
- Denaturation of Bovine Serum Albumin (BSA) and Ovalbumin by High Pressure, Heat and ChemicalsJournal of Food Science, 1992
- Some recent aspects of the use of high-pressure for protein investigations in solutionHigh Pressure Research, 1989
- Introduction of High Pressure to Food Processing: Preferential Proteolysis of β‐Lactoglobulin in Milk WheyJournal of Food Science, 1987
- The structure of β-lactoglobulin and its similarity to plasma retinol-binding proteinNature, 1986
- High Pressure Effects on Proteins and other BiomoleculesAnnual Review of Biophysics and Bioengineering, 1982
- ENZYMES UNDER EXTREMES OF PHYSICAL CONDITIONSAnnual Review of Biophysics and Bioengineering, 1981