CN113875921A - Method for determining influence of freeze-thaw cycle on gluten protein characteristics - Google Patents
Method for determining influence of freeze-thaw cycle on gluten protein characteristics Download PDFInfo
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- A—HUMAN NECESSITIES
- A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
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- A23L3/36—Freezing; Subsequent thawing; Cooling
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- A—HUMAN NECESSITIES
- A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
- A23L—FOODS, FOODSTUFFS, OR NON-ALCOHOLIC BEVERAGES, NOT COVERED BY SUBCLASSES A21D OR A23B-A23J; THEIR PREPARATION OR TREATMENT, e.g. COOKING, MODIFICATION OF NUTRITIVE QUALITIES, PHYSICAL TREATMENT; PRESERVATION OF FOODS OR FOODSTUFFS, IN GENERAL
- A23L7/00—Cereal-derived products; Malt products; Preparation or treatment thereof
- A23L7/10—Cereal-derived products
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- A—HUMAN NECESSITIES
- A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
- A23P—SHAPING OR WORKING OF FOODSTUFFS, NOT FULLY COVERED BY A SINGLE OTHER SUBCLASS
- A23P20/00—Coating of foodstuffs; Coatings therefor; Making laminated, multi-layered, stuffed or hollow foodstuffs
- A23P20/20—Making of laminated, multi-layered, stuffed or hollow foodstuffs, e.g. by wrapping in preformed edible dough sheets or in edible food containers
- A23P20/25—Filling or stuffing cored food pieces, e.g. combined with coring or making cavities
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- A—HUMAN NECESSITIES
- A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
- A23V—INDEXING SCHEME RELATING TO FOODS, FOODSTUFFS OR NON-ALCOHOLIC BEVERAGES AND LACTIC OR PROPIONIC ACID BACTERIA USED IN FOODSTUFFS OR FOOD PREPARATION
- A23V2002/00—Food compositions, function of food ingredients or processes for food or foodstuffs
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- Engineering & Computer Science (AREA)
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Abstract
The invention discloses a method for determining the influence of freeze-thaw cycle on the characteristics of gluten protein, which specifically comprises the following steps: (1) cooling the just processed flour product to below 30 ℃ to obtain a normal-temperature flour product; (2) putting the normal-temperature flour product into a freezing chamber, and cooling and freezing the normal-temperature flour product within 30-60min at the temperature of-40 to-30 ℃ until the central temperature of the flour product is lower than-30 ℃ to obtain a frozen flour product; (3) and (3) carrying out external packaging on the frozen flour product, and then transferring the frozen flour product into a refrigerating chamber at the temperature of-18 to-30 ℃ for freezing and preserving, wherein the temperature is kept constant in the refrigerating chamber, so that the quality of the frozen flour product is prevented from being influenced by the occurrence of freeze-thaw cycles. The determination method selected by the invention can ensure that the internal tissue structure (such as the mucedin characteristic) of the flour product is not changed to the maximum extent, the flour product has elasticity and the flavor is as original as before.
Description
Technical Field
The invention relates to the technical field of frozen flour product processing, in particular to a method for determining influence of freeze-thaw cycle on facial gluten characteristics.
Background
The frozen flour product is various main foods which are prepared by processing flour serving as a main raw material and meat, vegetables and the like serving as auxiliary materials into various cooked or uncooked main foods, and then immediately adopting a quick-freezing process, and can be transported, stored and sold under a freezing condition, such as quick-frozen steamed stuffed buns, quick-frozen dumplings, quick-frozen steamed buns, steamed rolls, spring rolls and the like. The development of frozen dough products has become a new trend in the food industry due to the convenience of transportation, storage and consumption. Although the quality of the quick-frozen food is obviously improved along with the continuous improvement of the process technology, the problems of nutrient loss, quality and taste reduction and the like of frozen flour products in the market still generally exist.
At present, the quality improvement of frozen flour products at home and abroad is mostly in the stage of adding the modifying agent and quickly freezing to slow down the damage of the frozen flour products, but the practical problems of the safety of the modifying agent, the cost of the quick freezing technology and the like have adverse effects on the development of the frozen flour products. Therefore, it is of great practical significance to dig deeply the essential cause of the deterioration of the frozen dough product so as to solve the problem of the deterioration of the frozen dough product in a targeted manner.
At present, scholars at home and abroad have made relevant researches on factors such as freezing-thawing circulation of flour products, freezing storage time and the like. The researchers have pointed out that the deterioration of the quality of frozen dough or products is not much related to starch; besides starch, moisture content and distribution in flour products have a significant influence on the texture and quality of food products. The problem of moisture crystallization leading to a reduction in the quality of the dough or product has been extensively studied. Mucedin is a major component of frozen dough products, which is high in content except for starch and moisture, and therefore, it is likely that the influence of ice crystals on mucedin during freezing is an important cause of deterioration in quality of frozen dough products. Furthermore, the influence of temperature fluctuations, which can cause the recrystallization of ice crystals, cannot be avoided during frozen storage, which can further disrupt the network structure of wheat gluten.
In the prior art, the research on the gluten protein freeze-thaw cycle is not limited, but the influence of the freeze-thaw cycle on gluten protein under the influence of different temperatures is yet to be researched.
Disclosure of Invention
In view of the above, the present invention provides a method for determining the influence of freeze-thaw cycles on the properties of gluten proteins, so as to solve the deficiencies in the prior art.
In order to achieve the purpose, the invention adopts the following technical scheme:
a method for determining the influence of freeze-thaw cycles on the characteristics of gluten protein specifically comprises the following steps:
(1) cooling the just processed flour product to below 30 ℃ to obtain a normal-temperature flour product;
(2) putting the normal-temperature flour product into a freezing chamber, and cooling and freezing the normal-temperature flour product within 30-60min at the temperature of-40 to-30 ℃ until the central temperature of the flour product is lower than-30 ℃ to obtain a frozen flour product;
(3) and (3) carrying out external packaging on the frozen flour product, and then transferring the frozen flour product into a refrigerating chamber at the temperature of-18 to-30 ℃ for freezing and preserving, wherein the temperature is kept constant in the refrigerating chamber, so that the quality of the frozen flour product is prevented from being influenced by the occurrence of freeze-thaw cycles.
Further, in the step (1), the flour product comprises at least one of steamed stuffed bun, dumpling, steamed bread, steamed rolls and spring rolls; cooling to 18-25 deg.C.
The flour product selected by the invention has large demand, is easy to process and store; the temperature of the flour product which is just processed is firstly reduced to 18-25 ℃, so that the efficiency of temperature reduction and freezing can be improved.
Further, in the step (2), the temperature condition of the freezing chamber is-30 ℃; the time for cooling and freezing is 40 min.
The beneficial effect of adopting the further technical scheme is that the freezing speed has influence on the size and the position of the ice crystals formed in the food tissue. When the flour product is frozen rapidly, the flour product can pass through the largest ice crystal generation zone in the shortest time, and moisture in the flour product forms countless needle-shaped small ice crystals which are uniformly distributed in cells and intercellular spaces of the flour product.
Furthermore, in the step (3), when the outer package is carried out, the seal is tight to prevent air leakage; the temperature of the cold storage compartment was-30 ℃.
The further technical scheme has the beneficial effects that if the fluctuation range of the air temperature of the freezing and storing chamber is large and the surface of the frozen noodle product is dried frequently, the product is weightless, the skin is cracked or dropped, and the appearance and the internal quality of the noodle product are seriously influenced. Therefore, the invention ensures that the temperature is kept constant at-30 ℃ during the preservation period so as to avoid the occurrence of freeze-thaw cycles to influence the quality of frozen flour products.
According to the technical scheme, compared with the prior art, the invention has the following beneficial effects:
1. according to the method, different freezing temperatures (-6 ℃, 12 ℃, 18 ℃, 24 ℃ and-30 ℃) are set, so that the influence of the temperature and the number of freeze-thaw cycles on the quality and the structure of the mucedin is researched, and a theoretical basis is provided for revealing the change rule of the freezing temperature and the mucedin quality under the freeze-thaw cycles.
2. The determination method selected by the invention can ensure that the internal tissue structure (such as the mucedin characteristic) of the flour product is not changed to the maximum extent, the flour product has elasticity and the flavor is as original as before.
Drawings
FIG. 1 is a graph showing the effect of different low temperature freeze-thaw cycles on gluten water binding capacity for 1-5 times;
FIG. 2 is a graph of the effect of different temperature freeze-thaw cycles on the storage modulus and loss modulus of wheat gluten, wherein a1 and b1 are graphs of the storage modulus and loss modulus of the first freeze-thaw cycle, and a5 and b5 are graphs of the storage modulus and loss modulus of the fifth freeze-thaw cycle;
FIG. 3 is the transverse relaxation time (T) of wheat gluten2) The graph comprises F1, F5 and F5, wherein the F1 represents a transverse relaxation time graph of one freeze-thaw cycle (the curve at the peak is-30 ℃, 24 ℃, 6 ℃, 18 ℃ and 12 ℃ from top to bottom), and the F5 represents a transverse relaxation time graph of five freeze-thaw cycles (the curve at the peak is-30 ℃, 24 ℃, 18 ℃, 12 ℃ and 6 ℃ from top to bottom);
FIG. 4 is a microscopic structure diagram of different low-temperature freeze-thaw cycle mucedin, wherein a, b, c, d and e are 1200-fold microscopic structures diagrams; a1, b1, c1, d1 and e1 are respectively a freeze-thaw microscopic structure diagram for 1 time at-6 ℃, 12 ℃, 18 ℃, 24 ℃ and-30 ℃; a3, b3, c3, d3 and e3 are the structures of freeze-thaw for 3 times respectively; a5, b5, c5, d5 and e5 are the structures of 5 times of freeze thawing microstructure respectively;
FIG. 5 is a graph of infrared conversion spectra of mucedin five times in different low-temperature freeze-thaw cycles (curves are-6 deg.C, -12 deg.C, -24 deg.C, -18 deg.C, -30 deg.C from top to bottom).
Detailed Description
The technical solutions in the embodiments of the present invention are clearly and completely described below, and it is obvious that the described embodiments are only a part of the embodiments of the present invention, and not all embodiments. All other embodiments, which can be derived by a person skilled in the art from the embodiments given herein without making any creative effort, shall fall within the protection scope of the present invention.
Example 1
The method for determining the influence of freeze-thaw cycle on the gluten protein characteristics specifically comprises the following steps:
(1) cooling the just processed flour product (steamed stuffed bun) to 22 ℃ to obtain a normal-temperature flour product;
(2) placing the normal temperature flour product into a freezing chamber, and cooling and freezing at-30 deg.C within 40min until the central temperature of the flour product is lower than-30 deg.C to obtain frozen flour product;
(3) the frozen flour product is externally packaged, the sealing is tight, the air leakage is prevented, and then the frozen flour product is transferred into a refrigerating chamber at the temperature of minus 30 ℃ for freezing and preservation, wherein the temperature is kept constant during the freezing and thawing cycle, so that the quality of the frozen flour product is prevented from being influenced.
Example 2
The method for determining the influence of freeze-thaw cycle on the gluten protein characteristics specifically comprises the following steps:
(1) cooling the just processed flour product (dumpling) to 18 ℃ to obtain a normal-temperature flour product;
(2) placing the normal temperature flour product into a freezing chamber, and cooling and freezing at-40 deg.C within 30min until the central temperature of the flour product is lower than-30 deg.C to obtain frozen flour product;
(3) the frozen flour product is externally packaged, the sealing is tight, the air leakage is prevented, and then the frozen flour product is transferred into a refrigerating chamber at the temperature of 18 ℃ below zero for freezing and preservation, wherein the temperature is kept constant during the freezing and thawing cycle, so that the quality of the frozen flour product is prevented from being influenced.
Example 3
The method for determining the influence of freeze-thaw cycle on the gluten protein characteristics specifically comprises the following steps:
(1) cooling the just processed flour product (steamed bread) to 25 ℃ to obtain a normal-temperature flour product;
(2) placing the normal temperature flour product into a freezing chamber, and cooling and freezing at-30 deg.C within 60min until the central temperature of the flour product is lower than-30 deg.C to obtain frozen flour product;
(3) the frozen flour product is externally packaged, the sealing is tight, the air leakage is prevented, and then the frozen flour product is transferred into a refrigerating chamber at the temperature of minus 25 ℃ for freezing and preservation, wherein the temperature is kept constant during the freezing and thawing cycle, so that the quality of the frozen flour product is prevented from being influenced.
Performance testing
First, influence of freeze-thaw cycle on characteristics of facial fascia protein is explored
1 materials and methods
1.1 materials
Wheat flour, purchased from the Wudeli flour group.
1.2 Main instruments and devices
HYC-TH-800H programmable constant temperature and humidity test chamber, purchased from Hongyou detection instruments ltd, Dongguan city; multifuge X1R Centrifuge bench high speed Centrifuge, available from Thermo corporation, usa; aiphal-2LDplus vacuum freeze dryer, available from CHRIST Freeze dryer, Germany; HAAKE MERS III rotational rheometer, available from Thermo Scientific, Germany; NMI20-040V-I NMR Analyzer, available from Nymi Analyzer, Suzhou; quanta 200 scanning electron microscope, available from FEI, usa; TENSOR 27 Fourier transform infrared spectrometer, available from BRUKER, Germany.
1.3 test procedures
1.3.1 preparation of wheat gluten protein
Kneading wheat flour and water into dough at a ratio of 2:1, wrapping with preservative film, standing at room temperature for about 0.5h, and kneading and washing until the water is clear. Freeze-drying for 2 days by using a freeze dryer (removing starch floating on the surface after freeze-drying), grinding into powder, sieving with a 100-mesh sieve, and storing in a dryer for later use.
1.3.2 preparation of Wet gluten protein
Mixing mucedin with distilled water at a ratio of 1:2, wrapping the sample in a preservative film after kneading, and standing for 1h in a refrigerator at 4 ℃.
1.3.3 Freeze-thaw cycle design for treating mucedin at different temperatures
The wet gluten protein is frozen at-6 ℃, 12 ℃, 18 ℃, 24 ℃ and 30 ℃ for 24 hours and then thawed at room temperature (25 ℃) for 4 hours, the process is one freeze thawing, and the test is repeated for 3 times at five times and different temperatures.
1.3.4 Water binding Capacity determination
Weighing 1.00g of wheat gluten protein powder, placing the wheat gluten protein powder in a centrifuge tube for weighing, gradually adding water, uniformly mixing the sample by using a vortex oscillator, centrifuging for 10min at the rotating speed of 3000r/min after the time lasts for 0.5h, and removing the supernatant.
The water binding capacity of the gluten protein was calculated according to the following formula.
1.3.5 determination of rheological Properties
Dynamic rheology was measured using a rotational rheometer. The diameter of the flat plate is 40.00mm, the gap of the clamp is 1.50mm, the scanning frequency is 0.1-10Hz, the stress is 1%, the temperature is 25 ℃, and each sample is paralleled for 3 times.
1.3.6 transverse relaxation time (T)2) And determination of moisture distribution and migration
Determination of the transverse relaxation time (T-NMR) of a sample by means of low-field nuclear magnetic resonance (LF-NMR) techniques2) And moisture distribution and migration. The sampling frequency SW is 100KHz, the repeated sampling times NS is 4, the half-echo time TE is 0.8ms, the NECH is 5000, the number TD of sampling points is 400018, and the relaxation decay time T0 is 1500 ms.
1.3.7 scanning Electron microscopy characterization
And (3) after ion sputtering and gold spraying are carried out on the freeze-dried mucedin, the cross section structure of the sample is observed under a scanning electron microscope, and the observation times are set and photographed.
1.3.8 Fourier Infrared transform Spectroscopy
Mixing gluten protein powder and KBr, and grinding into fine powder. Scanning wave number 400-4000cm-1Taking 1600-1700cm-1The band spectrum of the segmented amide I is processed by Peakfit v4.12 software, baseline correction, Gaussian deconvolution and fitting by a second derivative. And calculating the secondary structure change of each part according to the area of the sub-peak in the graph.
1.3.9 data analysis
The data are subjected to statistical analysis by using Excel 2019 and SPSS.22, infrared data are processed by Fourier transform infrared spectrum self-contained Omnic 5.0 software, and an image is drawn by Origin 2017 software.
2 results and analysis
2.1 wheat gluten protein Water binding assay
Water retention, which is an ability to maintain water within its own system, is one of the important functional properties of proteins, with the greatest contribution of physical trapped water. The water molecules can interact with certain genes in the protein molecules, and have a remarkable effect of maintaining the three-dimensional space structure of the protein.
FIG. 1 is a graph showing the effect of different low temperature freeze-thaw cycles on the water binding capacity of gluten protein for 1-5 times.
As can be seen from FIG. 1, different temperatures and the number of freeze-thaw cycles have a greater effect on the water binding capacity of wheat gluten. Overall, temperature is directly related to the water binding capacity of the gluten protein. The water holding capacity of the mucedin is reduced from 3.6% to about 2.4% along with the reduction of the temperature (-6 to-30 ℃), which is probably because the crystallization of water molecules is increased along with the reduction of the temperature, the network structure of the mucedin is damaged to a certain degree, and the water holding rate is reduced. From the aspect of the number of freeze-thaw cycles, the water retention capacity of the mucedin is inversely related to the number of freeze-thaw cycles, i.e., the more the number of freeze-thaw cycles, the poorer the water binding capacity of the mucedin, which may cause the phenomenon that the recrystallization of ice crystals in the mucedin network destroys the structure of the mucedin to deteriorate the quality of the mucedin. Recrystallization also allows, to a certain extent, redistribution of water in the protein system resulting in denaturation of the gluten proteins and a reduced water retention. In addition, studies show that the recrystallization phenomenon generated by the temperature fluctuation from low to high in the freeze-thaw cycle is also related to the quality reduction of the mucedin.
2.2 wheat gluten protein rheological Property analysis
The wheat gluten protein is mainly composed of prolamine with elasticity and glutenin with viscosity, and contains a small amount of albumin and globulin. The storage modulus (G') refers to the energy absorbed or recovered after sinusoidal deformation in a vibration period and is used for representing the elastic nature of a substance; the loss modulus (G') refers to the energy lost or expended per cycle of sinusoidal deformation, indicating the viscous nature of the material.
Fig. 2 is a graph showing the effect of different temperature freeze-thaw cycles on the storage modulus and loss modulus of wheat gluten, wherein a1 and b1 are graphs of the storage modulus and loss modulus of the first freeze-thaw cycle, and a5 and b5 are graphs of the storage modulus and loss modulus of the fifth freeze-thaw cycle.
As can be seen from fig. 2, with decreasing temperature, both the storage modulus (G') and the loss modulus (G ") of the gluten system show an increasing trend, probably because the temperature decrease inhibits the depolymerization of the large aggregates of the gluten molecules, and both gliadins and glutenins act together to make the unique viscoelasticity of the gluten more pronounced, and the elasticity and viscosity of the gluten protein increase. On the other hand, the lower the temperature, the more strongly the binding effect is, and the lower the temperature, the more the hydrogen proton movement is bound, so that the viscoelasticity of mucedin tends to increase. From the aspect of freeze-thaw cycle, the viscoelasticity of the mucedin is reduced along with the increase of the number of freeze-thaw cycles, and the main reason for the phenomenon is that along with the increase of the number of freeze-thaw cycles, the binding water part in the mucedin system is damaged, the hydrophilic group is exposed, the stable state of water molecules in the original system is broken, and the phenomenon that the water retention property and the viscoelasticity of the mucedin are reduced is caused. At the same frequency, G 'and G' both gradually decline with the increase of the number of times of freezing and thawing, and the change amplitude of G 'is larger than that of G'. It follows that the freeze-thaw cycle of gluten causes irreversible malignant changes in the viscoelasticity of gluten, and that the lower the temperature the more pronounced the tendency to deteriorate its viscoelasticity is suppressed.
2.3 wheat gluten protein Water distribution and migration analysis
Nuclear magnetic resonance (LF-NMR) is a new technology applied in the food field, and can rapidly and nondestructively determine the spin-spin relaxation time (T) of water molecule fluidity from the micro2) Is used to characterize the moisture distribution and migration within the interior of the food system. According to the related research, T2Corresponding to 3 forms of water, which are respectively strong binding water (T)21) Hardly flowing water (weakly bound water) (T)22) And freezable water (T)23) Wherein T is21、T22、T23The relaxation time is between 0.01-10ms, 10-100ms, 10-1000ms respectively.
FIG. 3 is the transverse relaxation time (T) of wheat gluten2) Map, wherein F1 represents the one-time transverse relaxation of a freeze-thaw cycleTime diagrams (curves at the peak are-30 ℃, 24 ℃, 6 ℃, 18 ℃ and 12 ℃ from top to bottom in sequence), and F5 represents a transverse relaxation time diagram of five times of freeze-thaw cycle (curves at the peak are-30 ℃, 24 ℃, 18 ℃, 12 ℃ and 6 ℃ from top to bottom in sequence).
As can be seen in fig. 3, the peak time (0.4ms) was later for the samples of the different cryotreatments, indicating that the water molecules are strongly bound to the gluten groups. The peak appeared around 10ms, with peaks 1 and 3 being lower than peak 2, indicating a higher weakly bound water content in the sample. T is2Positively correlated with the degree of freedom of moisture, T2The shorter the length, the more tightly the binding between water molecules and the gluten protein is, the less easily the gluten protein is discharged, and the better the water holding capacity of the gluten protein is. T is2The length of the wheat gluten protein can be used for measuring the mobility of water, and the results show that the contents of strong bound water and weak bound water of the wheat gluten protein are in a reduction trend along with the increase of the number of freeze-thaw cycles, the freewater content capable of freezing is gradually increased, and the interaction force of the gluten protein and the water is weakened due to the influence of freeze thawing of the gluten protein, so that the conversion of partial bound water to the freewater is possibly caused. The generation of ice crystals in the freezing process also causes mechanical damage to the mucedin to a certain degree, the spatial conformation is changed in a small range, and water flows out from part of the combined water along with the spatial gap and free water in a synergistic manner during thawing. As can be seen from FIG. 3, the samples had shorter relaxation times at-24 ℃ and-30 ℃ and were more water-binding, indicating better quality at-6 ℃.
To more accurately analyze the effect of freeze-thaw cycles and temperature on gluten moisture distribution and migration, 3 state relative moisture content tables were prepared, as shown in tables 1 and 2.
TABLE 1 analysis of the relative moisture content of the gluten proteins in 3 states after one freeze-thaw cycle
TABLE 2 analysis of the relative moisture content of the 3 states in the gluten protein after five cycles of freeze-thawing
Note: the data in tables 1 and 2 are mean. + -. standard deviation, and the letters a, b, c, d, etc. in the same column indicate significant differences between treatments (P < 0.05).
From T2The graph shows that hydrogen protons exist in three states in the gluten protein: one is strongly bound water with a short relaxation time; one is weakly bound water with a longer relaxation time; the other is freewater which can freeze. The relative percentages of the three waters are expressed as P21(strongly bound water), P22(hardly flowing water) and P23(freewater that can freeze).
As shown in Table 1, with the temperature decreasing (-6 to-30 ℃), mucedin P was obtained under different low-temperature freeze-thaw cycles21(bound Water) content increased by 3.057%, P22Increase in (hardly running Water) content by 4.129%, P23The content of (freewater capable of freezing) is reduced by 1.149%, and the total peak area is obviously reduced, which indicates that the combined water and the water which is not easy to flow are not completely frozen in the freezing process. The bound water content may increase with decreasing temperature by increasing the atom-atom interactions in the hydrated structure due to the interaction of water with proteins, and vitrification may occur, causing irreversible migration of some of the water molecules in freezable water to the bound water, with a concomitant decrease in free water content. Through significance analysis, the temperature of P is in the range of-6 ℃ to-30 DEG C21(bound water), P22(hardly flowing water), P23(freewater available for freezing) and the total peak area (p) have no significant difference<0.05). From the temperature effect on the moisture distribution of gluten, a low temperature is more favorable for the stability of the gluten structure.
As shown in Table 2, P is the protein content of gluten after 5 freeze-thaw cycles21(bound water) content decreased by 3.007%, P22(hardly mobile Water) content increased by 4.8%, P23(freewater available for freezing) content reduction1.793% less, the total peak area decreased significantly. The reduction in bound water content may be due to the irreversible change in molecular structure during freezing, as ice crystal growth breaks down the secondary bonds of the gluten proteins; partial water loss and transformation after thawing lead to water environment change of the mucedin, and after repeated freezing and thawing, ice crystals grow and recrystallize, thereby further aggravating the damage of a network structure. It follows that an increase in the number of freeze-thaw cycles has a significant effect on the loss of gluten water and a decrease in temperature highlights the migration of freezable water into bound water.
2.4 scanning Electron microscopy characterization of wheat gluten proteins
FIG. 4 is a microscopic structure diagram of different low-temperature freeze-thaw cycle mucedin, wherein a, b, c, d and e are 1200-fold microscopic structures diagrams; a1, b1, c1, d1 and e1 are respectively a freeze-thaw microscopic structure diagram for 1 time at-6 ℃, 12 ℃, 18 ℃, 24 ℃ and-30 ℃; a3, b3, c3, d3 and e3 are the structures of freeze-thaw for 3 times respectively; a5, b5, c5, d5 and e5 are the structural diagrams of 5 freeze-thaw micrographs respectively.
As can be seen from FIG. 4, the network structure of the mucedin is in honeycomb distribution, the structure of the empty mucedin group which is not subjected to freeze-thaw cycle is complete, the surface is smooth, the structural organization is compact, the mucedin is in a three-dimensional network structure, the holes are uniformly distributed and have uniform size, and the diameter is about 10-15 μm. Glutenin polymers are in the form of continuous fibers and gliadins are small. When the temperature is increased from-30 ℃ to-6 ℃, the network structure of the mucedin still exists, but the pore volume in the network is continuously increased. Cracks and fractures occur to a certain degree in the structure of the mucedin, the apparent structure is gradually rough, and the degree of pore diameter roundness is reduced. This is probably because the network structure of the glutenin becomes thinner during freezing of the frozen wet wheat gluten, part of the glutenin fragments fall out of the protein system, and the original positions of the ice crystals become cavities.
As can be seen from FIG. 4, the structural change of the wheat gluten through the freeze-thaw cycle at-6 ℃ is more remarkable, the structural surface of the wheat gluten presents unevenness and obvious cracks on the wall of the hole, the holes are larger than those at-30 ℃, the holes are left after the ice crystals are sublimated, and the quality damage is more serious. This is probably because the temperature fluctuations in the freeze-thaw cycle cause the bound water on the surface of wheat gluten to freeze, the recrystallization of water is aggravated, and the growth of ice crystals causes mechanical damage to the network structure of gluten. In addition, the lower the temperature of the freeze-thaw cycle, the more obvious the constraint force on the movement of water molecules, on the contrary, the higher the temperature, the higher the possibility that the growth mode of the ice crystals tends to be diversified, and in addition, the temperature fluctuation and the cycle number increase, the more prominent the recrystallization effect on the water molecules, so that the volume of the ice crystals formed at the temperature of-6 ℃ tends to be larger than that at the temperature of-30 ℃. The temperature of minus 24 ℃ and minus 30 ℃ is close to the quick freezing temperature, the generation speed of crystal nuclei is high, the crystal nuclei can rapidly pass through the maximum ice crystal generation zone in a short time, and the volume of the ice crystals is small, so that the damage to the structure of the mucedin is small. When the temperature is the same, along with the increase of the number of times of freeze thawing, the cavities of the mucedin gradually increase, and even obvious fracture occurs. This result is consistent with the findings of Baier-SchenkA et al. The increase in the number of freeze-thaw cycles at the same temperature leads to a deteriorated microstructure, with a gluten microstructure-30 ℃ being better than-6 ℃ for the same number of times. The complex effects of various conditions have important influence on the surface and the interior of the network structure of the gluten, and the influence of temperature change and the number of freeze-thaw cycles on the microstructure of the gluten is obvious. Thus exhibiting the changes in the electron micrographs described above.
2.5 Fourier Infrared transform Spectroscopy (FTIR) analysis
FIG. 5 is a graph of infrared conversion spectra of mucedin five times in different low-temperature freeze-thaw cycles (curves are-6 deg.C, -12 deg.C, -24 deg.C, -18 deg.C, -30 deg.C from top to bottom).
The secondary structure of a protein refers to the way in which the polypeptide chain folds on itself in a protein molecule, including alpha-helices, random coils, beta-folds, and beta-turns, among others. The characteristic peak of the amide I band is mature at present and can reflect the related information of alpha-helix, irregular crimp, beta-fold, beta-turn angle and the like in the secondary structure of the protein. The characteristic hydrogen bonding patterns are closely related to their structure.
There are references to: 1600-1640 cm-1Is beta-sheet; 1640-1650 cm-1In random rollsKoji; 1650-1660 cm-1Is an alpha-helix; 1660-1700 cm-1Is a beta-turn. And (3) performing Gaussian deconvolution and second-order derivation treatment on the amide I band of the frozen wheat gluten protein sample to obtain a corresponding peak, and performing curve fitting on the amide I band by taking the position of the amide I band with the characteristic peak as a parameter. The results of the fitting are shown in table 3. At 1650cm-1The nearby peak is the characteristic peak of the mucedin amide I band, and is caused by the expansion and contraction of C ═ O and the vibration of N-H.
TABLE 3 distribution of wheat gluten secondary structure at five different low temperature freeze-thaw cycles
Note: the data in Table 3 above are mean. + -. standard deviation, and letters a, b, c, d, etc. in the same column indicate significant differences between treatments (P < 0.05).
As can be seen from Table 3, the secondary structure of wheat gluten proteins is dominated by β -sheet and β -turn. At-6 ℃, the characteristic peak of β -sheet was calculated to be 39.68%, the content of random coil was 10.36%, the content of α -helix was 14.22%, and the content of β -turn was 35.74%. As the temperature is lowered, the secondary structure in wheat gluten is also changed. The content of beta-sheet is increased, the content of alpha-helix and beta-turn is reduced, and the content of random coil is not obviously changed. β -turns are non-repetitive structures formed by the hydrogen bonding of the 1 st residue C ═ O to the 4 th residue N — H to form a tight ring. Within the range of-6 ℃ to-30 ℃, the beta-folding content is increased by 5.33 percent, and the alpha-helix content and the beta-turn content are respectively reduced by 5.06 percent and 3.02 percent. The changes in alpha-helix, random coil, beta-fold and beta-turn content indicate that different low temperatures produce different effects on the tenascin. Studies have shown that changes in the number of freeze-thaw cycles can have a significant effect on the secondary structure of mucedin, including random coiling, overall reduction in alpha-helices, and overall increase in beta-folds and beta-turns. However, this experiment shows that the alpha-helix and beta-turn are reduced and the beta-sheet is increased as the temperature is reduced under the same number of freeze-thaw cycles. This is probably because the influence of low temperature on wheat gluten is strong, and the suppression effect of the lower temperature on the cleavage of secondary bonds such as hydrogen bonds is more remarkable, and the tendency of deterioration of the secondary structure of wheat gluten is slow. The overall increase in beta-sheet may be due to a favorable change in structure due to a greater degree of inter-mucedin molecular aggregation with decreasing temperature. Furthermore, it is also possible that part of the alpha-helices and beta-turns in the mucedin are converted into beta-sheet structures. The beta-turn structure has stability, and the low temperature can promote the partial transformation phenomenon, thereby ensuring the stability of the mucedin. There is literature that changes in the secondary structure of proteins are associated with aggregation behavior. Probably because the temperature influences the water environment of the mucedin, the low temperature accelerates the growth of ice crystals to destroy hydrogen bonds maintaining alpha-helix and beta-turn structures, so that the ice crystals are dispersed into small molecular substances, and the small molecules are in a state of reaching the lowest energy to maintain the structure stability and are rearranged to form a beta-folded structure.
3 conclusion
Through analysis, the water holding capacity of the mucedin is gradually reduced along with the reduction of the temperature in the range of-6 to-30 ℃; the storage modulus (G ') and the loss modulus (G') increase with decreasing temperature; the microstructure holes of the mucedin are more uniform at minus 30 ℃ than at minus 6 ℃, and the structural integrity is better; the alpha-helix and beta-turn in the secondary structure are turned to beta-folding trend obviously, and the structure is more stable; in short, the more the number of freeze-thaw cycles, the worse the gluten quality, and the lower the temperature, the better the gluten quality. Provides a certain theoretical basis for revealing the influence of the freeze-thaw cycle on the structure of the gluten protein at different freezing temperatures.
Second, national Standard detection
The frozen flour products prepared in the embodiments 1 to 3 were taken and subjected to sensory evaluation according to the method of the Standard of the trade industry in the national trade of the people's republic of China SB/T10412-one 2007. The results are shown in Table 1.
Table 1 examples 1-4 sensory evaluation results of frozen pasta
As can be seen from Table 1, the sensory evaluation of the frozen flour products prepared in the examples 1-3 of the present invention all meet the requirements of "quick-frozen flour-rice food" SB/T10412-2007.
The above tests show that the determination method selected by the present invention can ensure the internal texture (such as the gluten characteristics) of the flour product to the maximum extent without being changed, and has elasticity and original flavor.
The previous description of the disclosed embodiments is provided to enable any person skilled in the art to make or use the present invention. Various modifications to these embodiments will be readily apparent to those skilled in the art, and the generic principles defined herein may be applied to other embodiments without departing from the spirit or scope of the invention. Thus, the present invention is not intended to be limited to the embodiments shown herein but is to be accorded the widest scope consistent with the principles and novel features disclosed herein.
Claims (7)
1. A method for determining the influence of freeze-thaw cycles on the characteristics of gluten protein is characterized by comprising the following steps:
(1) cooling the just processed flour product to below 30 ℃ to obtain a normal-temperature flour product;
(2) putting the normal-temperature flour product into a freezing chamber, and cooling and freezing the normal-temperature flour product within 30-60min at the temperature of-40 to-30 ℃ until the central temperature of the flour product is lower than-30 ℃ to obtain a frozen flour product;
(3) and (3) carrying out external packaging on the frozen flour product, and then transferring the frozen flour product into a refrigerating chamber at the temperature of-18 to-30 ℃ for freezing and preserving, wherein the temperature is kept constant in the refrigerating chamber, so that the quality of the frozen flour product is prevented from being influenced by the occurrence of freeze-thaw cycles.
2. The method of claim 1, wherein in step (1), the dough product comprises at least one of steamed stuffed buns, dumplings, steamed bread, steamed twisted rolls and spring rolls.
3. A method for determining the effect of a freeze-thaw cycle on gluten protein properties according to claim 1, wherein in step (1) the cooling is to 18-25 ℃.
4. A method for determining the influence of a freeze-thaw cycle on the gluten protein property according to claim 1, wherein in the step (2), the temperature condition of the freezing chamber is-30 ℃.
5. The method for determining the influence of freeze-thaw cycle on the gluten protein property as claimed in claim 1, wherein in step (2), the time for cooling and freezing is 40 min.
6. A method for determining the effect of freeze-thaw cycle on mucedin characteristics as claimed in claim 1, wherein in step (3), the outer packaging is performed with a tight seal to prevent air leakage.
7. A method for determining the effect of a freeze-thaw cycle on gluten protein characteristics as claimed in claim 1, wherein in step (3) the temperature of the cold storage compartment is-30 ℃.
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| EP0115108A1 (en) * | 1983-01-26 | 1984-08-08 | General Foods Corporation | Frozen dough having improved frozen storage shelf life |
| CN112120057A (en) * | 2020-09-28 | 2020-12-25 | 江南大学 | Dough making method capable of improving quality of frozen dough and application of dough making method |
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| CN112869001A (en) * | 2021-02-24 | 2021-06-01 | 江南大学 | Method for improving quality of frozen dough by using starch derivative |
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| EP0115108A1 (en) * | 1983-01-26 | 1984-08-08 | General Foods Corporation | Frozen dough having improved frozen storage shelf life |
| CN112120057A (en) * | 2020-09-28 | 2020-12-25 | 江南大学 | Dough making method capable of improving quality of frozen dough and application of dough making method |
| CN112704184A (en) * | 2020-12-31 | 2021-04-27 | 河南科技学院 | Sub-freezing method of frozen flour product |
| CN112869001A (en) * | 2021-02-24 | 2021-06-01 | 江南大学 | Method for improving quality of frozen dough by using starch derivative |
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