• Journal of Animal Science and Technology
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• v.44 no.1
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• pp.105-112
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• 2002

In order to investigate the effects of heat treatment of three animal by-products(feather meal, tallow meal, viscera meal) on in situ ruminal degradation characteristics and gastrointestinal availability of dietary crude protein(CP), three ruminally and duodenally cannulated dry Holstein cows were employed. Cows were fed a diet containing 60% concentrate and 40% orchard grass hay, and had free access to water and mineral block. Experimental feeds were processed for 4 hr at 149$^{\circ}C$ in a forced-air oven, and were passed through a 1-mm screen. Degradation kinetics of feed protein in the rumen were fitted to an exponential type model, and intestinal availability was estimated by the mobile nylon bag technique. Effective CP degradabilities in the rumen for feather meal, tallow meal and viscera meal were 30.2%, 75.0% and 56.4% at 5% passage rate per hour(k=0.05), respectively. In addition, heat treatment increased effective ruminal CP degradability on feather meal and viscera meal treatments, whereas decreased in tallow meal treatment(P$<$0.05). Gastrointestinal CP disappearances of feather meal, tallow meal and viscera meal were 56.2%, 18.6%, and 37.9%, respectively. In addition, heat treatment decreased the gastrointestinal CP disappearance on feather meal and viscera meal treatment, but increased in tallow meal treatment(P$<$0.05). Intestinal availability of rumen undegradable protein(A-UDP) was 80.4% for feather meal, 83.8% for tallow meal and 86.9% for viscera meal. In addition, heat treatment increased A-UDP on feather meal and tallow meal treatment, 94.0% and 91.3%, respectively, but decreased on viscera meal treatment, 76.5%(P$<$0.05).

• Applied Biological Chemistry
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• v.37 no.4
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• pp.259-265
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• 1994

To investigate the effects of protein concentration, heat treatment and pH on the foaming properties of sodium caseinate, surface tension, apparent viscosity, turbidity, foaming ability and foam stability at 1.0, 3.0, 5.0, 7.0 and 10.0% (W/V), at 55 and $65^{\circ}C$ and at pH 6.0, 7.0 and 8.0 were examined. The conditions of protein concentrations for the foaming abilities were $3.0{\sim}7.0%$ (W/V). Foam stabilities of heated sodium caseinates were worse than those of unheated sodium caseinates (control) at pH6.0 and 7.0 (p<0.05), while the heated one were better than the unheated at pH 8.0, 10.0% concentrations (p<0.05). Also foam stabilities of sodium caseinate at pH 6.0 were higher than those at pH 7.0 and 8.0. Foaming ability and foam stability were inconsistently effected by changing protein concentration, heat treatment and pH.

• Korean Journal of Environmental Biology
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• v.21 no.3
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• pp.313-318
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• 2003

Environmental stresses, such as heat shock, alcohol and physiological salt have been shown to induce a group of protein called heat shock protein (HSPs) in various tissues. In this investigation, we studied that arsenic stress would alter contraction of isolated rat aorta and expression of heat shock protein 70 and investigated the relation between expression of HSP 70 and vascular contractility of isolated rat aorta. Rat aorta strips, mounted in organ baths were exposed to 0, 0.5, 1,2 and 4 mM arsonic for 60 min. and 1,3 and 8 hours later tested for contractile response and expression of heat shock protein 70. Contractility of rat aorta were determined by isometric transducer connected to computerized physiograph and expression of HSP 70 was characterized by western blotting, respectively. Potassium chloride (55 mM) significantly augmented vascular contractility of yat aorta by 39％ compared with the control at 8 hours but not one or three hours after treatment of 4 mM arsenic. Arsonic stress (4 mM) also increased the expression of HSP 70 in rat aorta at 8 hours but one or three hours compared with the control and HSP expressed in vascular smooth muscle cells and some expressed in endothelium cells. These results suggest that arsenic stress not only did alter the magnitude of the contractile response to high potassium chloride but also increased the expression of HSP 70 in the rat aorta.

• Korean Journal of Clinical Laboratory Science
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• v.49 no.4
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• pp.460-469
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• 2017

Heat shock proteins (HSPs) are induced as a self-defense mechanism of cells when exposed to various external stresses, such as high fever, infection, free radicals, and heavy metals. They affect the prognosis in the process of tumor formation. HSP is classified into four families: HSP27, HSP60, HSP90, and HSP100, depending on molecular weight. Heat shock protein 90 (HSP90), a molecular chaperone, plays an important role in the cellular protection against various stressful stimuli and in the regulation of cell cycle progression and apoptosis. In the present study, we assessed the differential expression of HSP90 family proteins in non-small cell lung cancer (NSCLC), and the correlation of their expression levels with clinicopathologic factors and patient survival rates. The result of this study can be summarized as follows; $HSP90{\alpha}$ showed higher expression in patients with no lymphovascular invasion (p=0.014). $HSP90{\beta}$ showed a higher expression of squamous cell carcinoma (p=0.003), and an over expression of glucose-related protein (GRP94) was significantly associated with poor differentiation (p=0.048). However, none of the HSP90 proteins showed a significant association with the survival status in patients with NSCLC. This study also indicates that $HSP90{\alpha}$ might contribute more to the carcinogenesis of NSCLC than $HSP90{\beta}$, and GRP94 and isoform selectivity should be considered when HSP90 inhibitors are studied or utilized in the treatment of NSCLC.

• The Korean Journal of Zoology
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• v.39 no.1
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• pp.47-53
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• 1996

We examined the expression of the heat shock proteins (HSPs) and glucose-regulated proteins (GRPs) during phorbol 1 2-myristate 1 3-acetate (PMA)-induced megakaryocytic differentiation of human er"'throleukemia K562 cells. PMA-treated K562 cells showed a cell growth arrest and alteration in morphology and patterns of gpllIa and c-myc expression, characteristic of megakaryocytic differentiation. During the megakaryocytic differentiation, HSP9OA, HSP9OB, and HSP28 mRNA and protein levels markedly decreased, while GRP78/B and GRP94 mRNA levels were enhanced. On the other hand, HSP7OA and HSP7OB mRNA levels were reduced, but HSP7O protein levels were not changed by PMA treatment. These results suggest specific roles for the HSPs and GRPs in K562 cell proliferation and megakaryocic differentiation.tion.

• Asian-Australasian Journal of Animal Sciences
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• v.15 no.5
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• pp.732-739
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• 2002

Milk samples with different phenotype combination of $\{kappa}$-casein and ${\beta}$-lactoglobulin and different preheating temperatures of 30, 70, 75 and $80^{\circ}C$ were used for cheesemaking under laboratory conditions. For the 853 batches of cheese, mean composition was 59.64% total solids, 30.24% fat and 23.66% protein, and the whey contained 6.93% total solids, 0.30% fat and 0.87% protein. Least squares analysis of the data indicated that heating temperature of the milk and ${\kappa}$-CN/${\beta}$-LG phenotypes had significant effects on cheese and whey compositions. The total solids, fat and protein contents of cheese were negatively correlated with preheating temperatures of milk. Cheese from BB/BB phenotype milk had the highest and those from AA/AA phenotype milk had the lowest concentrations of total solids, fat and protein. Mean recoveries of milk components in the cheese were 53.71% of total solids, 87.15% of fat, and 80.32% of protein. For the 10 different types of milk, maximum recoveries of milk components in cheese occurred with preheating temperature of $70^{\circ}C$ or $75^{\circ}C$ and lowest recoveries occurred at $80^{\circ}C$. The whey averaged 6.94% total solids, 0.30% fat and 0.87% protein. Losses of milk components in the whey were lowest for milk preheated at $80^{\circ}C$ and for milk containing the BB/BB phenotype.

• Korean journal of food and cookery science
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• v.6 no.3 s.12
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• pp.9-15
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• 1990

Peanut prptein isolate was tested for the purpose of finding out the effect of pH, Sodium Chloride concentration and heat treatment on the solubility, surface hydrophobicity, foam expansion and foam stability. The solubility of peanut protein isolate was affected by pH and showed the lowest value at pH 4.5. When the peanut protein isolate was heated, the solubility decreased at pH 3 and pH 7 but at pH 9 solubility increased. At all pH range, solubility decreased as NaCl was added. The surface hydrophobicity of peanut protein isolate showed the highest value at pH 1.5. Generally, at acidic pH range the surface hydrophobicity was high, but at alkaline region, the surface hydrophobicity increased as the temperature increased. And when NaCl was added, the surface hydrophobicity was also increased. Foam expansion of peanut protein isolate was no significant difference among the values about pH. When the peanut protein was heated and NaCl was added, foam expansion was increased at pH 7. Foam stability was significantly low at pH 4.5 and foam stability was increased at acidic pH region below pH 4.5. At pH 7 and pH 9, heat treatment above $60^{\circ}C$ increased foam stability. When NaCl was added, foam stability was significantly increased at pH 3 and pH 7.

• Korean journal of food and cookery science
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• v.20 no.3
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• pp.256-264
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• 2004

The effects of irradiation on the functional and structural characteristics of soy protein isolates were studied. Soymilk was irradiated at 1, 5, and l0kGy, after which soy protein isolates were prepared. The functional properties of soy protein isolates were examined including solubility, emulsion capacity and stability, foam capacity and stability, structural properties as represented by SDS-PAGE pattern, and secondary and tertiary structures. The solubility and emulsion capacity were increased by radiation treatment at 1kGy however the values were adversely affected again as dosage was increased above 5kGy. As irradiation dosage increased, an increase of foaming capacity at 1kGy and a decreasing turnover afterwards were also noted in foaming capacity, although the differences were not statistically significant. The SDS-PAGE pattern showed fragmentation and aggregation of protein molecules as affected by irradiation in proportion to the dosage increase. The results of CD and fluorescence spectroscopy revealed increased aperiodic structure contents with the dosage increase. It was assumed that irradiation dosagefrom 5 to l0kGy could initiate minimal denaturation of protein in various foods compared to general heat treatment.

• Journal of Microbiology and Biotechnology
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• v.29 no.7
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• pp.1022-1032
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• 2019

Probiotics are known to provide the host with immune-modulatory effects and are therefore of remarkable interest for therapeutic and prophylactic applications against various disorders, including inflammatory diseases. Weissella cibaria JW15 (JW15) has been reported to possess probiotic and antioxidant properties. However, the effect of JW15 on inflammatory responses has not yet been reported. Therefore, the objective of the current study was to evaluate the anti-inflammatory potential of JW15 against lipopolysaccharide (LPS) stimulation. The production of pro-inflammatory factors and the cellular signaling pathways following treatment with heat-killed JW15 was examined in LPS-induced RAW 264.7 cells. Treatment with heat-killed JW15 decreased nitric oxide and prostaglandin $E_2$ production via down-regulation of the inducible nitric oxide synthase and cyclooxygenase-2. In addition, treatment with heat-killed JW15 suppressed the expression of pro-inflammatory cytokines, interleukin $(IL)-1{\beta}$, IL-6, and tumor necrosis factor-${\alpha}$. The anti-inflammatory properties of treating with heat-killed JW15 were associated with mitogen-activated protein kinase signaling pathway-mediated suppression of nuclear factor-${\kappa}B$. These results indicated that JW15 possesses anti-inflammatory potential and provide a molecular basis regarding the development of functional probiotic products.

• The Korean Journal of Food And Nutrition
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• v.14 no.6
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• pp.562-567
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• 2001

In order to utilize okara protein as a food auditive, nutritional composition of soymilk okara was investigated. Protein in okara Is highly insoluble due to excessive heat treatment during soymilk processing. Protein content of okara was 37.3% as compared to 42.5 % for soybean. Carbohydrate and lipid contents of okara were 40.6% and 17.9%, respectively. Okara lipid extracted with chloroform-methanol consisted of neutral lipid, glycolipid and phospholipid, with neutral lipid making up 98.6% . Linoleic acid, ileic acid, and palmitic acids accounted for about 80% of the total fatty acids with linoleic acid sharing 50.3% of the total. Amino acid composition of okara protein was dissimilar to that of soy Protein : Cysteine was totally absent in okara while lysine, which is the limiting amino acid of soy protein, was present in higher amount in okara on dry weight basis. Both aqueous extract of okara protein and soy Protein were found to have ACE inhibitory activity.