• Korean Journal of Fisheries and Aquatic Sciences
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• v.36 no.3
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• pp.198-203
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• 2003

Heat-induced surimi gels were prepared using various concentration of ATC as a additives and calcium agent. Regardless of various concentration of ATC, there were no difference the moisture $(80.4-81.2\%)\;and\;crude\;ash\;(1.4-1.\5%)$ contents. The pH of heat-induced surimi gels were decreased 7.16 to 7.04 depend on increasing ATC concentration. The whiteness, breaking force and gel strength of $0.09\%$surimi gel were improved significantly difference (p<0.05). Sensory evaluation on texture and whiteness were also similar to determination by color and texture meters. In mineral content of heat-induced surimi gel calcium content was increased 26 to 54 mg/100g depend on increasing ATC concentration, while phosphorus content was not change. The optimal concentration of ATC for preparation of high quality heat-induced surimi gel was $0.09\%$. The shelf-life of heat-induced surimi gel did not extend by addition of $0.09\%$ ATC.

• Korean Journal of Fisheries and Aquatic Sciences
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• v.36 no.3
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• pp.204-209
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• 2003

Utilization of soluble protein recovered from surimi wastewater using calcium powder of cuttle bone were examined. The crude ash content of the heat-induced surimi gel was increased linearly by increasing substitution ratio of recovered protein-ATC toward commercial surimi. Moisture (approximately $76\%$) and lipid $(0.2\%)$ contents were not change, but their protein contents were decreased 15.7 to $14.3\%$ depend on increasing of substitution ratio. The white index of the heat-induced surimi gel by color meter was increased up to $10\%$ of substitution ratio. There were no difference between $0\%\;and\;5\%$ substituted surimi gel in the gel strength. The sensory score on white index and texture of the heat-induced surimi gel did not change in 0 to $10\%$ as a substitution ratio of recovered protein-ATC toward commercial surimi, while decreased in more $15\%.$ The optimal substitution ratio of recovered protein-ATC as a bulking agent was $10\%.$ The heat-induced surimi gel prepared with $10\%$ substitution of recovered protein-ATC was similar to the content and composition of total amino. acids, and superior to calcium content and the ratio of calcium and phosphorus toward those of commercial surimi.

• Food Science of Animal Resources
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• v.31 no.6
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• pp.817-826
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• 2011

The technological effects of Makgeolli lees fiber (0, 0.5, 1.0, 2.0, and 4.0%) on chicken salt-soluble breast meat proteins in a model system on proximate composition, physicochemical properties, and textural properties were investigated. Makgeolli lees fiber was obtained from Makgeolli brew processing, and the by-products showed good dietary fiber. The moisture and ash contents, water holding capacity, redness, yellowness, hardness, and apparent viscosity of chicken salt-soluble meat protein heat-induced gel systems with Makgeolli lees fiber were all higher than the control without Makgeolli lees fiber. However, protein solubility and electrophoretic patterns did not differ among the control and treatments with Makgeolli lees fiber samples. The chicken salt-soluble protein heat-induced gel systems incorporating Makgeolli lees fiber had improved water holding capacity, textural properties, and viscosity due to Makgeolli lees fiber addition. These results suggest that the addition of 4.0% Makgeolli lees fiber to gel is helpful to improve the physical properties of heat-induced gels.

• Food Science of Animal Resources
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• v.39 no.2
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• pp.229-239
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• 2019

The objectives of this study were to determine the interaction between porcine myofibrillar proteins and various gelatins (bovine hide, porcine skin, fish skin, and duck skin gelatins) and their impacts on gel properties of porcine myofibrillar proteins. Porcine myofibrillar protein was isolated from pork loin muscle (M. longissimus dorsi thoracis et lumborum). Control was prepared with only myofibrillar protein (60 mg/mL), and gelatin treatments were formulated with myofibrillar protein and each gelatin (9:1) at the same protein concentration. The myofibrillar protein-gelatin mixtures were heated from $10^{\circ}C$ to $75^{\circ}C$ ($2^{\circ}C/min$). Little to no impacts of gelatin addition on pH value and color characteristics of heat-induced myofibrillar protein gels were observed (p>0.05). The addition of gelatin slightly decreased cooking yield of heat-induced myofibrillar protein gels, but the gels showed lower centrifugal weight loss compared to control (p<0.05). The addition of gelatin significantly decreased hardness, cohesiveness, gumminess, and chewiness of heat-induced myofibrillar gels. Further, sodium dodecyl poly-acrylamide gel electrophoresis (SDS-PAGE) showed no interaction between myofibrillar proteins and gelatin under non-thermal conditions. Only a slight change in the endothermic peak (probably myosin) of myofibrillar protein-gelatin mixtures was found. The results of this study show that the addition of gelatin attenuated the water-holding capacity and textural properties of heat-induced myofibrillar protein gel. Thus, it could be suggested that well-known positive impacts of gelatin on quality characteristics of processed meat products may be largely affected by the functional properties of gelatin per se, rather than its interaction with myofibrillar proteins.

• Journal of the Korean Society of Food Science and Nutrition
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• v.33 no.10
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• pp.1676-1684
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• 2004

Gel properties of recovered protein from mackerel, frozen blackspotted croaker, chicken breast and pork leg using acidic and alkaline processing were evaluated. Myofibrillar protein from mackerel by acidic processing did not form a heat-induced gel. However, the recovered protein including sarcoplasmic protein formed heatinduced gel. Breaking force of gel from mackerel processed at pH 10.5 was the lowest. A deformation value of frozen blackspotted croaker was the highest, followed by chicken breast, pork leg and mackerel. Whiteness of frozen blackspotted croaker was the highest among heat-induced gel. Breaking force, deformation and whiteness were decreased by addition of recovered protein from mackerel, but price was increased. A breaking force and whiteness of heat-induced gel added recovered protein from chicken breast were increased, and the price was greatly decreased. When the constraint of breaking force, deformation and price of raw material were set up above 110 g, 4.5 mm and below 2,000 won/kg. A optimum formulation for blending protein was 36∼50% for frozen blackspotted croaker, 34∼40% for chicken breast, 14∼25% for pork leg. The heat-induced gel of recovered protein from frozen blackspotted croaker showed compact structure compared to that of recovered protein from mackerel. A formulation of chicken breast and pork leg based on blackspotted croaker can be used in surimi based seafood products having various texture.

• Journal of Animal Science and Technology
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• v.62 no.4
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• pp.533-542
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• 2020

The objective of this study was to observe the interactions between salt-soluble proteins extracted from beef and elephant foot yam (Amorphophallus campanulatus) flour in heat-induced gel matrix development. The effect of salt concentration; 0.5%, 1.0%, 1.5%, and 2.0% in weight/weight basis (w/w), during protein extraction on pH, salt-soluble protein concentration and myofibril fractions of beef extract was determined firstly, and no significant effect was found. The beef salt-soluble proteins extracted using salt solution at different concentrations were then added with elephant foot yam flour at 5%, 10%, and 15% w/w, gelatinized at 90℃ for 20 min, and cooled down at 4℃ for 12 h. The interactions between beef salt-soluble proteins and elephant foot yam flour resulted in an improved gel strength (p < 0.01) and the addition level of elephant foot yam flour affected the pH, instrumental color, moisture, crude protein, and ash content significantly. The addition of elephant foot yam flour also reduced the size of the pores in the gel matrix as shown by scanning electron microscope (SEM) photographs. These suggest that elephant foot yam flour well interacts with beef salt-soluble proteins to form gel matrix.

• Preventive Nutrition and Food Science
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• v.10 no.2
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• pp.191-197
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• 2005

There exist two interesting phenomena in making seafood products from surimi. When salted surimi is kept at a constant low temperature $(4\~40^{\circ}C)$, its rheological properties change from sol to gel, which is called 'setting'. Seafood processors can exploit changes that occur during setting in preparation of surimibased products, because heating at high temperatures, after the pre-heating during the setting process, enhances the gel-strength of salted surimi. Contrarily, when salted surimi or low-temperature set gel is heated at moderate temperatures $(50\~70^{\circ}C)$, a deterioration of gel is observed. The phenomenon is termed 'modori'. In the modori temperature range, heat-stable cysteine proteinases such as cathepsin B, H, Land L-Iike hydrolyze the myosins responsible for gel-formation, resulting in gel weakening modori. This article reviews molecular events occurring during gel setting that improve the quality of surimi-based products, and inhibition of modori by applying proteinase inhibitors. Application of recombinant protein technology to surimi-based products is introduced and its prospects for practical use are discussed.

• Preventive Nutrition and Food Science
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• v.2 no.4
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• pp.281-284
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• 1997

Heat-induced gelation is an important functional property of whey proteins. Preheating of calcium reduced whey was reported to increase gel strength. 5% whey-protein solutions were preheated at pH7 and at various temperatures(60~8$0^{\circ}C$) for 15 minutes. The amount of soluble aggregates and denaturation enthalpy of preheated whey proteins were measured. Preheating temperature was negatively correlated with denaturation enthalpy($R^2$=0.857, P=0.08) and positive with the amount of soluble aggregates($R^2$=0.921, P=0.002). Denaturation enthalpy was negatively correlated with gel strength($R^2$=0.93, P=0.002). Soluble aggregates and gel strength were positively correlated($R^2$=0.972, P=0.0003). The formation of three dimensional gel network requires controlled protein denaturation and aggregation. Since preheating leads to the partial denaturation of proteins and the formation of soluble aggregates, preheated whey proteins have a higher gel strength than non-preheated one.

• Journal of Physiology & Pathology in Korean Medicine
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• v.18 no.2
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• pp.496-499
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• 2004

We have previously observed that Bambusae Caul is in Liquamen (BCL) stimulates the adipose conversion of 3T3-L1 cells and molecular chaperones were involved in the process of the assembly and replacement of laminin subunits in Bovine aortic endothelial cells(BAEC). Endothelial cells are exposed to continuous shear stress due to the blood flow. Heat shock protens(hsp) are a well-known stress response protein, namely, stress proteins. To investigate effects of BCL on the stress proteins induced by heating in endothelial cells, we have analyzed synthetic amounts of stress proteins in sodium dodecyl sulfate gel electrophoresis under reducing conditions. Under the condition of heating stress, BCL inhibited the synthesis of stress proteins in endothelial cells. These results suggest that BCL may have an important role for expression of stress proteins induced by heating in endothelial cells.

• The Korean Journal of Food And Nutrition
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• v.11 no.2
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• pp.228-236
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• 1998

Egg is an important foods containing many good proteins. But it is well known that egg protein has a lot of allergenicity. The purpose of this study is to develop the methods to reduce the allergenicity of egg. I tried various experimental methods ; For example, heat treatment, irradiation with ultraviolet and microwaves, treatment with polyphosphate, enzyme hydrolysis and PCA inhibition test using guinea pigs and degrees of hydrolysis. The results obtained were as follows ; 1. Heat treatment reduced allergenicity of egg protein. The longer the heat time, the better the effect. 2. Irradiating with ultraviolet and microwave increased both the degree of protein hydrolysis and PCA inhibition reduced the allergenicity. Ultraviolet was more effective than microwaves on egg protein. Fertilized eggs did not reduce allergenicity. 3. Enzyme treatment increased the degree of hydrolysis and PCA inhibition, and reduced allergenicity considerably. Alcalase was more effective than neutrase. 4. Adding polyphosphate did not induced protein hydrolysis, but increased PCA inhibition and reduced allergenicity. 5. The picture of various treatments of egg gel by SEM showed a light surface which indicated that protein was desolved. Neutrase was lighter than alcalase, and the longer the heating time, the lighter the surface became. 6. Measurements of the hardness of egg gel by Instron showed that the longer the reaction time with enzyme, the softer it became.