-
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
Background introduction
foodmate.
net/tag_766.
html" class="zdbq" title="Peanut related food information" target="_blank">Peanuts are a common food foodmate.
net/tag_3601.
html" class="zdbq" title="Allergen-related food information" target="_blank">allergens one, it has a high incidence of foodmate.
net/tag_657.
html" class="zdbq" title="Allergy-related food information" target="_blank">allergic reactions to produce serious and lasting effects on lifelong allergy individual characteristics.
Studies have shown that foodmate.
net/tag_4568.
html" class="zdbq" title="Fermentation related food information" target="_blank">fermentation can reduce the allergenicity of peanuts, and also improve the taste, digestibility and nutritional value of peanuts; in addition, fermentation bacteria and their metabolites can adjust the balance of Th1/Th2 reactions, enhance the epithelial barrier function, and help slow down The level of allergy even prevents allergies.
net/tag_766.
html" class="zdbq" title="Peanut related food information" target="_blank">Peanuts are a common food foodmate.
net/tag_3601.
html" class="zdbq" title="Allergen-related food information" target="_blank">allergens one, it has a high incidence of foodmate.
net/tag_657.
html" class="zdbq" title="Allergy-related food information" target="_blank">allergic reactions to produce serious and lasting effects on lifelong allergy individual characteristics.
Studies have shown that foodmate.
net/tag_4568.
html" class="zdbq" title="Fermentation related food information" target="_blank">fermentation can reduce the allergenicity of peanuts, and also improve the taste, digestibility and nutritional value of peanuts; in addition, fermentation bacteria and their metabolites can adjust the balance of Th1/Th2 reactions, enhance the epithelial barrier function, and help slow down The level of allergy even prevents allergies.
Natto foodmate.
net/tag_2120.
html" class="zdbq" title="Bacillus related food information" target="_blank">bacillus is a safe, acid, heat of foodmate.
net/tag_2217.
html" class="zdbq" title="Probiotics related food information" target="_blank">probiotics , a variety of functions of antimicrobial activity, anti-cancer, thrombolysis.
Bacillus natto also has a strong ability to produce enzymes and can effectively degrade foodmate.
net/tag_296.
html" class="zdbq" title="Protein-related food information" target="_blank">protein .
High pressure foodmate.
net/tag_4720.
html" class="zdbq" title="Sterilization related food information" target="_blank">sterilization commonly used in micro- foodmate.
net/tag_3587.
html" class="zdbq" title="Bio-fermentation related food information" target="_blank">biological fermentation and reduction sensitization peanuts.
In this study, Bacillus natto combined with high-pressure sterilization assisted fermentation process was used to reduce the allergenicity of raw peanut pulp.
The effect of fermentation on peanut allergens was foodmate.
net/tag_4657.
html" class="zdbq" title="Testing related food information" target="_blank">detected by ELISA and the changes in peanut foodmate.
net/tag_3855.
html" class="zdbq" title="Protein related food information" target="_blank">protein structure during the fermentation process were studied.
The structural characteristics and allergenicity of the protein provide new information and lay the foundation for the development of hypoallergenic peanut fermentation products.
net/tag_2120.
html" class="zdbq" title="Bacillus related food information" target="_blank">bacillus is a safe, acid, heat of foodmate.
net/tag_2217.
html" class="zdbq" title="Probiotics related food information" target="_blank">probiotics , a variety of functions of antimicrobial activity, anti-cancer, thrombolysis.
Bacillus natto also has a strong ability to produce enzymes and can effectively degrade foodmate.
net/tag_296.
html" class="zdbq" title="Protein-related food information" target="_blank">protein .
High pressure foodmate.
net/tag_4720.
html" class="zdbq" title="Sterilization related food information" target="_blank">sterilization commonly used in micro- foodmate.
net/tag_3587.
html" class="zdbq" title="Bio-fermentation related food information" target="_blank">biological fermentation and reduction sensitization peanuts.
In this study, Bacillus natto combined with high-pressure sterilization assisted fermentation process was used to reduce the allergenicity of raw peanut pulp.
The effect of fermentation on peanut allergens was foodmate.
net/tag_4657.
html" class="zdbq" title="Testing related food information" target="_blank">detected by ELISA and the changes in peanut foodmate.
net/tag_3855.
html" class="zdbq" title="Protein related food information" target="_blank">protein structure during the fermentation process were studied.
The structural characteristics and allergenicity of the protein provide new information and lay the foundation for the development of hypoallergenic peanut fermentation products.
research method
Peanut pulp (RPP) is made by mixing the stripped peanuts with water in a ratio of 1:9 (m/v), refining, and autoclaving the RPP at 121 ℃ for 20 min to obtain sterilized peanut pulp (APP) After inoculating 9.
8×105 CFU/mL of Bacillus natto and culturing at 37 ℃, the samples were collected after fermentation at different times (12, 24, 36, 48, 60 h) and labeled as FAPP-B-12, FAPP-B-24, FAPP-B-36, FAPP-B-48, FAPP-B-60.
The histones were extracted, and bovine serum albumin was used as the standard, and the protein concentration was determined by Bradford method.
SDS-PAGE was used to determine the molecular weight of each histone, and the IgE binding ability was determined by indirect ELISA.
Use scanning electron microscope to observe the microstructure of peanut protein, combine with circular dichroism to evaluate the changes of protein secondary structure and use UV spectrometer to measure the UV absorption spectra of different samples, determine the surface hydrophobicity of each sample by ANS method, and measure with SH-DNTB For the content of free sulfhydryl groups, the particle size of peanut protein is determined by a high-sensitivity nanoparticle analyzer.
8×105 CFU/mL of Bacillus natto and culturing at 37 ℃, the samples were collected after fermentation at different times (12, 24, 36, 48, 60 h) and labeled as FAPP-B-12, FAPP-B-24, FAPP-B-36, FAPP-B-48, FAPP-B-60.
The histones were extracted, and bovine serum albumin was used as the standard, and the protein concentration was determined by Bradford method.
SDS-PAGE was used to determine the molecular weight of each histone, and the IgE binding ability was determined by indirect ELISA.
Use scanning electron microscope to observe the microstructure of peanut protein, combine with circular dichroism to evaluate the changes of protein secondary structure and use UV spectrometer to measure the UV absorption spectra of different samples, determine the surface hydrophobicity of each sample by ANS method, and measure with SH-DNTB For the content of free sulfhydryl groups, the particle size of peanut protein is determined by a high-sensitivity nanoparticle analyzer.
results and analysis
The results show that autoclaving and fermentation will cause the gradual degradation of high molecular weight peanut protein (Figure 1).
The results of indirect ELISA showed that after autoclaving alone, the allergenicity of RPP was reduced by 66.
6%, which was further reduced with fermentation (Figure 2).
Using scanning electron microscope to observe the microstructure of peanut protein, it is found that FAPP-Bs has smaller aggregates and looser network structure (Figure 3).
This may be due to the protease produced by Bacillus natto during the fermentation process to catalyze the removal of peanut protein.
Caused by folding and degradation.
The results of circular dichroism (Figure 4) and ultraviolet absorption spectroscopy (Figure 5) showed that autoclaving and fermentation induced hydrolysis, unfolding and conformational changes of peanut protein, as well as the reduction of α-helices.
These changes will significantly affect the table The formation of bits.
Changes in protein hydrophobicity usually reflect changes in its tertiary and quaternary structures.
ANS fluorescent probes and SH-DNTB were used to measure the changes in surface hydrophobicity and free sulfhydryl groups of peanut protein after different treatments.
The results showed that after 48 hours of fermentation, The tertiary structure of peanut protein is most affected; high temperature sterilization will cause protein aggregation, which may cause free sulfhydryl groups to form disulfide bonds within or between molecules.
The further reduction of free sulfhydryl content during the fermentation process may be related to the resulting protein or peroxide The substance causes free sulfhydryl groups to hide or oxidize.
Particle size analysis showed that, due to protein aggregation caused by autoclaving, the particle size of APP was mostly distributed between 550 nm and 100 nm.
The results of indirect ELISA showed that after autoclaving alone, the allergenicity of RPP was reduced by 66.
6%, which was further reduced with fermentation (Figure 2).
Using scanning electron microscope to observe the microstructure of peanut protein, it is found that FAPP-Bs has smaller aggregates and looser network structure (Figure 3).
This may be due to the protease produced by Bacillus natto during the fermentation process to catalyze the removal of peanut protein.
Caused by folding and degradation.
The results of circular dichroism (Figure 4) and ultraviolet absorption spectroscopy (Figure 5) showed that autoclaving and fermentation induced hydrolysis, unfolding and conformational changes of peanut protein, as well as the reduction of α-helices.
These changes will significantly affect the table The formation of bits.
Changes in protein hydrophobicity usually reflect changes in its tertiary and quaternary structures.
ANS fluorescent probes and SH-DNTB were used to measure the changes in surface hydrophobicity and free sulfhydryl groups of peanut protein after different treatments.
The results showed that after 48 hours of fermentation, The tertiary structure of peanut protein is most affected; high temperature sterilization will cause protein aggregation, which may cause free sulfhydryl groups to form disulfide bonds within or between molecules.
The further reduction of free sulfhydryl content during the fermentation process may be related to the resulting protein or peroxide The substance causes free sulfhydryl groups to hide or oxidize.
Particle size analysis showed that, due to protein aggregation caused by autoclaving, the particle size of APP was mostly distributed between 550 nm and 100 nm.
Figure 1 Relative molecular weight of proteins extracted from RPP, APP and FAPP-Bs
(M, the molecular weight of the standard protein; 1-7 in turn represent the protein extracted from RPP, APP, FAPP-B-12, FAPP-B-24, FAPP-B-36, FAPP-B-48, FAPP-B-60 )
Figure 2 Allergenicity of RPP, APP and FAPP-Bs proteins
Figure 3 The appearance of the freeze-dried product (first row) and protein scanning electron microscope (the second row and third row are 200 and 4000 respectively), 1-7 represent RPP, APP, FAPP-B-12, FAPP-B in turn -24, FAPP-B-36, FAPP-B-48, FAPP-B-60 freeze-dried products and their proteins
Figure 4 (A) Circular dichroism of RPP, APP, FAPP-Bs; (B) Calculate the corresponding secondary structure according to their ratio
Figure 5 The tertiary structure of proteins extracted from RPP, APP and FAPP-Bs.
A, ultraviolet absorption spectrum; B, fluorescence emission spectrum; C, free sulfhydryl (SH) content
A, ultraviolet absorption spectrum; B, fluorescence emission spectrum; C, free sulfhydryl (SH) content
in conclusion
The results showed that high-pressure sterilization and Bacillus natto fermentation can degrade peanut protein, change protein conformation and reduce α-helix, causing changes in the particle size of peanut protein, resulting in a significant reduction in the IgE binding properties of raw peanuts.
Therefore, the use of Bacillus natto combined with high-pressure sterilization-assisted fermentation is an effective process for producing low-allergenic, high-quality peanut products.
Therefore, the use of Bacillus natto combined with high-pressure sterilization-assisted fermentation is an effective process for producing low-allergenic, high-quality peanut products.
