The Applicability of near Infrared Reflectance Spectroscopy for Determining Solubility and Digestibility of Heated Protein under High Pressure
- 1 March 1995
- journal article
- Published by SAGE Publications in Journal of Near Infrared Spectroscopy
- Vol. 3 (2) , 73-79
- https://doi.org/10.1255/jnirs.58
Abstract
The potential of near infrared (NIR) reflectance spectroscopy for non-destructively probing structural changes in protein during the process of denaturation was investigated. Lysozyme as a model protein was adjusted to 15% moisture content, placed in a steel cylinder and then heated at 30, 90, 120 and 150°C under pressure conditions of 10, 15, 30 and 45 MPa. Significant changes were observed in absorption bands near 2144, 2168 and 2208 nm with increases in temperature and pressure. The spectral changes were, in general, much larger for samples subjected to both high temperature and pressure than for those subjected to high temperature only. It is likely that these changes are due to changes in the secondary structure of protein. Absorbance changes at the above wavelengths showed high correlations to variations in solubility and digestibility of protein treated under high heat and pressure conditions. The results of multiple linear regression analysis suggest that NIR spectroscopy may be used to predict the solubility and digestibility of protein.Keywords
This publication has 8 references indexed in Scilit:
- Studies on Spectra/Structure Correlations in Near-Infrared Spectra of Proteins and Polypeptides. Part I: A Marker Band for Hydrogen BondsApplied Spectroscopy, 1994
- Effect of Secondary Structures of Protein on Determination of Protein Content by Near Infrared Spectroscopy.NIPPON SHOKUHIN KOGYO GAKKAISHI, 1994
- High-resolution NMR study of the pressure-induced unfolding of lysozymeBiochemistry, 1992
- Crystal structure of hen egg-white lysozyme at a hydrostatic pressure of 1000 atmospheresJournal of Molecular Biology, 1987
- CHEMICAL AND PHYSICOCHEMICAL CHANGES IN FIELD BEAN AND SOYBEAN PROTEINS TEXTURIZED BY EXTRUSIONJournal of Food Science, 1979
- The Formation, Isolation and Importance of Isopeptides in Heated ProteinsPublished by Springer Nature ,1977
- PROTEIN MEASUREMENT WITH THE FOLIN PHENOL REAGENTJournal of Biological Chemistry, 1951
- Infra-red spectroscopic studies of globular protein structureProceedings of the Royal Society of London. Series A. Mathematical and Physical Sciences, 1951