Investigation of Thermal Denaturation of Barley Nonspecific Lipid Transfer Protein 1 (ns-LTP1b) by Nuclear Magnetic Resonance and Differential Scanning Calorimetry

The process of thermal denaturation of a covalently modified form of barley grain nonspecific lipid transfer protein 1b (ns-LTP1b) was investigated by nuclear magnetic resonance (NMR) and differential scanning calorimetry up to 115 °C. The denaturation was found to be irreversible and highly coopera...

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Bibliographic Details
Published in:Journal of agricultural and food chemistry 2009-09, Vol.57 (18), p.8444-8452
Main Authors: MATEJKOVA, Michaela, DKOVA, Jitka Zí, ZIDEK, Lukáš, WIMMEROVA, Michaela, CHMELIK, Josef, SKLENAR, Vladimír
Format: Article
Language:English
Subjects:
Biological and medical sciences
Calorimetry, Differential Scanning
Carrier Proteins - chemistry
Cereal and baking product industries
Chemical Changes Induced by Processing/Storage
Food industries
Fundamental and applied biological sciences. Psychology
Hordeum - chemistry
Hot Temperature
Magnetic Resonance Spectroscopy
Plant Proteins - chemistry
Protein Denaturation
Seeds - chemistry
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Summary:The process of thermal denaturation of a covalently modified form of barley grain nonspecific lipid transfer protein 1b (ns-LTP1b) was investigated by nuclear magnetic resonance (NMR) and differential scanning calorimetry up to 115 °C. The denaturation was found to be irreversible and highly cooperative. A method of numerical quantitative analysis allowing us to fit the NMR data to a transition state model without further simplification was developed. On the basis of the obtained values of transition state enthalpy and entropy, the rate of denaturation was calculated as a simple measure of protein stability at various temperatures. The effect of disulfide bond reduction on thermal denaturation of ns-LTP1b was studied and discussed in the context of quality control of barley products during storage and processing.
ISSN:0021-8561
1520-5118
DOI:10.1021/jf902580f