-
Categories
-
Pharmaceutical Intermediates
-
Active Pharmaceutical Ingredients
-
Food Additives
- Industrial Coatings
- Agrochemicals
- Dyes and Pigments
- Surfactant
- Flavors and Fragrances
- Chemical Reagents
- Catalyst and Auxiliary
- Natural Products
- Inorganic Chemistry
-
Organic Chemistry
-
Biochemical Engineering
- Analytical Chemistry
-
Cosmetic Ingredient
- Water Treatment Chemical
-
Pharmaceutical Intermediates
Promotion
ECHEMI Mall
Wholesale
Weekly Price
Exhibition
News
-
Trade Service
Traditional roast chicken is mainly based on experienced masters, the quality of roast chicken is unstable, the flavor is lost, and how to accurately maintain the original flavor is a difficult and hot spot
.
In this study, the effects of constant temperature heat treatment on the microstructure of
myofibrillar protein and its binding ability to spice flavor substances were studied by multispectral and molecular docking simulation.
The results showed that heat treatment significantly changed the structure and rheology of myofibrillar protein, and affected the adsorption performance
of myofibrillar protein.
The hydroxyl content and hydrophobicity of myofibrillar protein increased with the extension of heat treatment time, and the unfolding and aggregation of proteins led to significant changes in the particle size of myofibrillar protein during heat treatment
.
In addition, heat treatment leads to a decrease in the α-helix of the myofibrillar protein molecule and an increase in β-folding, resulting in a significant decrease
in the absolute zeta potential of myofibrillar protein.
At the same time, the heated myofibrillar protein forms large, irregular clustered aggregates
.
In addition, the viscosity and roughness of myofibrillar protein increase
after heating.
The change of structure and physicochemical properties of myofibrillar protein affects its ability
to bind to spice flavor substances to a certain extent.
At the same time, amino acid residues interact with spice source flavor substances through various bonds to form a stable myofibrillar protein-spice source flavor complex
.
The results provide a theoretical basis for the interaction mechanism between spice flavor substances and chicken protein, which is helpful to promote the flavor regulation
of chicken protein foods.
.
In this study, the effects of constant temperature heat treatment on the microstructure of
myofibrillar protein and its binding ability to spice flavor substances were studied by multispectral and molecular docking simulation.
The results showed that heat treatment significantly changed the structure and rheology of myofibrillar protein, and affected the adsorption performance
of myofibrillar protein.
The hydroxyl content and hydrophobicity of myofibrillar protein increased with the extension of heat treatment time, and the unfolding and aggregation of proteins led to significant changes in the particle size of myofibrillar protein during heat treatment
.
In addition, heat treatment leads to a decrease in the α-helix of the myofibrillar protein molecule and an increase in β-folding, resulting in a significant decrease
in the absolute zeta potential of myofibrillar protein.
At the same time, the heated myofibrillar protein forms large, irregular clustered aggregates
.
In addition, the viscosity and roughness of myofibrillar protein increase
after heating.
The change of structure and physicochemical properties of myofibrillar protein affects its ability
to bind to spice flavor substances to a certain extent.
At the same time, amino acid residues interact with spice source flavor substances through various bonds to form a stable myofibrillar protein-spice source flavor complex
.
The results provide a theoretical basis for the interaction mechanism between spice flavor substances and chicken protein, which is helpful to promote the flavor regulation
of chicken protein foods.
The findings were published online in the International Journal of Biological Macromolecules (JCR Zone I, IF=8.
025
).
Dr.
Xiangxiang Sun is the first author of the paper, and Prof.
Dequan Zhang and Prof.
Zhenyu Wang are co-corresponding authors
.
The research was supported
by the Beijing Municipal Innovation Team of Modern Agricultural Industrial Technology System (BAIC06-2022-BJJQ-G12), the National Key R&D Program of China (2019YFC1606200), and the Agricultural Science and Technology Innovation Project of the Chinese Academy of Agricultural Sciences (CAAS-ASTIP-2022-IFST).
025
).
Dr.
Xiangxiang Sun is the first author of the paper, and Prof.
Dequan Zhang and Prof.
Zhenyu Wang are co-corresponding authors
.
The research was supported
by the Beijing Municipal Innovation Team of Modern Agricultural Industrial Technology System (BAIC06-2022-BJJQ-G12), the National Key R&D Program of China (2019YFC1606200), and the Agricultural Science and Technology Innovation Project of the Chinese Academy of Agricultural Sciences (CAAS-ASTIP-2022-IFST).
Original link: https://doi.
org/10.
1016/j.
ijbiomac.
2022.
12.
312
org/10.
1016/j.
ijbiomac.
2022.
12.
312