• 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.

• 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.

• 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.

• Korean Journal of Poultry Science
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• v.26 no.2
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• pp.85-95
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• 1999

The mechanically deboned chicken meat(MDCM) has several limits in using for in using for in processed meat products as a main material because of poor color and textural properties, chance of microbial contamination and lipid oxidation. There has been a growing interest all over world in the application of MDCM to the surimi process. The surimi made from MDCM contains a high concentration of myofibrillar protein since this processing involves repeated washing processes with an aqueous solution in order to remove heme pigments, fat and other undesirable substances. The quality of the surimi made from MDCM is affected by various processing factors, such as kinds of wash solution, ion strength, washing cycle, temperature, pH changes, composition, part of muscle, particle size, and rigor state etc. A number of researchers havee investigated the effect of the various washing conditions on the properties of surimi gels. A fuller information of all the factors affecting surimi processing and gel formation by heat-induced gelation has not been known yet.

• Korean Journal of Fisheries and Aquatic Sciences
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• v.52 no.6
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• pp.555-561
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• 2019

We examined the quality characteristics of four kinds of Alaska pollack Theragra chalcogramma surimi (APS), five kinds of golden threadfin bream Nemipterus virgatus surimi (GTS), and two kinds of giant squid Ommastrephes bartrami surimi (GSS) used in Korea. The volatile basic nitrogen contents of APS, GTS, and GSS increased with decreasing grade to 6.8-9.8, 5.5-8.3, and 143.5-177.7 mg/100 g, respectively. The Ca²⁺-ATPase activities of APS and GTS decreased with decreasing grade to 0.63-0.83 and 0.60-0.80 pi μmole/min/mg, respectively. The Ca²⁺-ATPase activity of RA-grade GSS was 0.82-0.91 pi μmole/min/mg. The whiteness values of APS, GTS, and GSS heat-induced gels were 54.0-71.4, 53.9-71.0, and 52.2-70.3, respectively, and that of both APS and GTS decreased with decreasing grade. The gel strengths of APS and GTS heat-induced gels were 412.3-769.4 and 280.2-456.5 g·cm, respectively, and decreased with decreasing grade. The total amino acid contents of SA-grade APS, SSA-grade GTS, and RA-grade GSS were 17,328.1, 17,965.0, and 14,846.8 mg/100 g, respectively, and the major amino acids were glutamic acid, aspartic acid, arginine, leucine, lysine, proline, alanine, and phenylalanine. The primary minerals were sodium (136.6-164.9 mg/100 g), potassium (45.7-160.4 mg/100 g), phosphorus (35.0-73.5 mg/100 g), sulfur (22.8-56.4 mg/100 g), and calcium (18.0-203.4 mg/100 g).

• Journal of the Korean Society of Food Science and Nutrition
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• v.25 no.6
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• pp.922-927
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• 1996

In order to investigate heat-induced gelation properties of $\alpha-lactalbumin(\alpha-La),$ total free SH groups, half-cystine, and disulfide bond contents of $\alpha-La$ gels prepared in 0.1M Tris-HCI buffer(pH 8.0) were measured. The samples were heated at $90^{\circ}C$ for 40 minutes under different PH and concentrations of NaCl, $CaCl_2,$ $\alpha-La,$ N-ethylrnaleirnide(NEM), and dithiothreitol(DTT). Total free SH groups were low at high concentrations of $\alpha-La$ and at pH 6.5~8.5, and were $14.72~18.58\mu\textrm{m}ol/g$ and $14.17~16.11\mu\textrm{m}ol/g,$ respectively. Half-cystine contents of NEM-induced gels decreased with increasing concentration of NEM, and were $1.03~39.17\mu\textrm{m}ol/g.$ Disulfide bonds of DTT-induced gels increased with increasing concentration of DTT, and were $70.04~71.80\mu\textrm{m}ol/g$.

• The Journal of Korean Physical Therapy
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• v.20 no.1
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• pp.57-65
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• 2008

Purpose: Heat shock proteins (HSPs) are a group of proteins that are activated when cells are exposed to a variety of environmental stresses, such as infection, inflammation, exposure to toxins, starvation, hypoxia, brain injury, or water deprivation. The activation of HSPs by environmental stress plays a key role in signal transduction, including cytoprotection, molecular chaperone, anti-apoptotic effect, and anti-aging effects. However, the precise mechanism for the action of small HSPs, such as HSP27 and mitogen-activated protein kinases (MAPKs: extracellular-regulated protein kinase 1/2 (ERK1/2), p38MAPK, stress-activated protein kinase/c-Jun N-terminal kinase (SAPK/JNK), is not completely understood, particularly in application of cell stimulators including platelet-derived growth factor (PDGF), angiotensin II (AngII), tumor necrosis factor $\alpha$ (TNF$\alpha$), and $H_2O_2$. This study examined the relationship between stimulators-induced enzymatic activity of HSP27 and MAPKs from rat smooth and skeletal muscles. Methods: 2-dimensional electrophoresis (2DE) and matrix assisted laser desorption ionizationtime-of-flight/time-of-flight (MALDI-TOF/TOF) analysis were used to identify HSP27 from the intact vascular smooth and skeletal muscles. Three isoforms of HSP27 were detected on silver-stained gels of the whole protein extracts from the rat aortic smooth and skeletal muscle strips. Results: The expression of PDGF, AngII, TNF$\alpha$, and $H_2O_2$-induced activation of HSP27, p38MAPK, ERK1/2, and SAPK/JNK was higher in the smooth muscle cells than the control. SB203580 (30${\mu}$M), a p38MAPK inhibitor, increased the level of HSP27 phosphorylation induced by stimulators in smooth muscle cells. Furthermore, the age-related and starvation-induced activation of HSP27 was higher in skeletal muscle cells (L6 myoblast cell lines) and muscle strips than the control. Conclusion: These results suggest, in part, that the activity of HSP27 and MAPKs affect stressors, such as PDGF, AngII, TNF$\alpha$, $H_2O_2$, and starvation in rat smooth and skeletal muscles. However, more systemic research will be needed into physical therapy, including thermotherapy, electrotherapy, radiotherapy and others.

• Journal of the Korean Society of Food Science and Nutrition
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• v.31 no.3
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• pp.438-444
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• 2002

Interactions between meat proteins and hydrocolloids in a model system may play an important role for the improvement of textural properties in low-fat sausage mixtures. The objective of this study was to determine gel properties as affected by the type and level of hydrocolloid, various pH values of meat protein-hydrocolloid mixture before cooking, and internal cooking temperatures. The desirable heat-induced gels (HIGs) were formed at least pH values above 6.0. The addition of konjac flour (KF), kappa-carrageenan (CN) and locust bean gum (LBG) to extracted salt soluble proteins (2%) improved the gel strength with increased levels (0.5∼1.5%) and HIGs containing CN had the highest (p<0.05) gel strength. The increase of cooking temperature increased gel strength, depending on pH and type of hydrocolloid. However, the minimun internal cooking temperature to make viscoelastic HIGs was 70$^{\circ}C$. These results indicated that desirable HIGs were manufactured with each hydrocolloid concentration of 1% and minimum cooking temperature of 70$^{\circ}C$ with pH values higher than 6.0.

• Food Science of Animal Resources
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• v.29 no.5
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• pp.590-598
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• 2009

The aim of this study was to model and optimize the calcium alginate (CA) and microbial transglutaminase (TG) systems to form a cold-set myofibrillar protein (MP) gel containing 0.1 M or 0.3 M NaCl using a response surface methodology. The gel strengths of cold-set and heat-induced MP gels, and cooking yields were measured. All measured parameters showed determination coefficients ($R^2$) above 0.7 without a lack-of-fit. The CA system had the best results with component ratios of 1.0:0.3:1.0 corresponding to sodium alginate, calcium carbonate and glucono-$\delta$-lactone, respectively, and was favourable at 0.1 M NaCl. In contrast, the TG system only had an effect on cold-set MP gelation at 0.3 M salt, and the optimal ratio of TG to sodium caseinate was 0.6:0.5. By combining the two systems at 0.3 M NaCl, an acceptable cold-set MP gel with an improved texture and high cooking yield could be formed. Therefore, these results indicated that the functionality of the cold-set MP gel could be enhanced by combining these two optimized gelling system.

• Journal of Periodontal and Implant Science
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• v.28 no.1
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• pp.103-120
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• 1998

Prokaryotic and eukaryotic cells respond to heat stress and other environmental abuses by synthesizing a small set of stress proteins and by inhibiting post-transcription synthesis of normal proteins. The purpose of the present study was to document the stress response produced by inflamed gingival tissue in vivo, and cytokine inducted human periodontal ligament cells. Human PDL cells were exposed to TNF-$\alpha$(1ng/ml), INF-$\gamma$(200 U/ml), LPS(100ug/ml), combination of cytokine, and SDS-PAGE gels running and Western blotting analysis was done. In vivo studies, the healthy gingival tissusse of a control group and inflamed gingival tissue of adult periodontitis were studied by immunohistochemistry and histology. The results were as follows 1. HSP 47 was distributed on basal layer in healthy gingiva, but stronger stained in basal, suprabasal, and spinous layer of inflamed gingiva. 2. HSP 47 was rare on endothelial cells and mononuclear cells in healthy gingiva, but stronger expressed in inflamed gingiva. 3. HSP 70 expression was rare on epihelium and inflammatory cells hi both healthy & inflamed gingiva. 4. HSP 70 was actively expressed on endothelial cells and inflammatory cells of capillary lumen in moderately & mild inflamend gingiva. 5. PDL cells showed low level of HSP 47 protein expression which was significantly induced by cytokine stimulation (LSP only and combination). 6. Maximum HSP 70 protein induction was seen with stimulation by a combination of the cytokine, Combination of TNF-$\alpha$, INF-$\gamma$, LPS have been shown to synergistically effects of HSP 70 expression. On the above findings, HSP Is influenced by cytokine and chronic inflammation in vivo, and may be involved in protection of tissue during periodontal inflammatiom.