کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
2086434 1545536 2015 10 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
Effect of thermal and electric field treatment on the conformation of Ara h 6 peanut protein allergen
موضوعات مرتبط
علوم زیستی و بیوفناوری علوم کشاورزی و بیولوژیک دانش تغذیه
پیش نمایش صفحه اول مقاله
Effect of thermal and electric field treatment on the conformation of Ara h 6 peanut protein allergen
چکیده انگلیسی


• The study was conducted on the Ara h 6 allergen to evaluate the thermal and electric field effects using Molecular Dynamics.
• Secondary structure changes were observed in the molecule for both static and oscillating electric fields.
• Oscillating electric field in combination with thermal treatment has resulted in higher levels of structural deviations.
• Radius of Gyration and Solvent Accessible Surface Area (SASA) analysis showed compaction in the Ara h 6 molecule.

The study uses molecular dynamic simulation to evaluate the effect of static and oscillating electric field (2450 MHz) of intensity 0.05 V/nm at different temperatures 300 K, 380 K and 425 K on structural conformation of Ara h 6 peanut protein allergen. The conformational changes in the protein were studied with respect to root mean square deviation, radius of gyration, dipole moment and solvent accessible surface area. The increase in temperature and application of external electric fields, both static and oscillating fields had significant effect on the conformation of Ara h 6, specifically the helical secondary structures. It was observed that the root mean square deviation increased with a rise in temperature and application of external electric fields had no significant effect on it at any given temperatures. This study also demonstrated that exposure to external stresses including thermal and electric fields induces conformational changes in the protein structure, which may impact its physico-chemical properties.Industrial relevance
• The work was performed to understand the influence of food processing on protein and the changes in their structure using molecular modeling concept.
• Molecular Dynamics Simulations have been applied to visualize the folding and unfolding of the protein structure depending on the amount of stress applied on the system.
• This work can help in modification and optimization of process parameters (like temperature and time) to enhance the protein functional properties and digestibility in the end product.
• Increasing digestibility would automatically result in higher nutritional absorption in the body, decreased immunoreactivity and overall better nutritional quality.

ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Innovative Food Science & Emerging Technologies - Volume 30, August 2015, Pages 79–88
نویسندگان
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