• Title/Summary/Keyword: heat treatment of protein

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Effects of Temperature during Moist Heat Treatment on Ruminal Degradability and Intestinal Digestibility of Protein and Amino Acids in Hempseed Cake

  • Karlsson, Linda;Ruiz-Moreno, M.;Stern, M.D.;Martinsson, K.
    • Asian-Australasian Journal of Animal Sciences
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    • v.25 no.11
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    • pp.1559-1567
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    • 2012
  • The objective of this study was to evaluate ruminal degradability and intestinal digestibility of crude protein (CP) and amino acids (AA) in hempseed cake (HC) that were moist heat treated at different temperatures. Samples of cold-pressed HC were autoclaved for 30 min at 110, 120 or $130^{\circ}C$, and a sample of untreated HC was used as the control. Ruminal degradability of CP was estimated, using the in situ Dacron bag technique; intestinal CP digestibility was estimated for the 16 h in situ residue using a three-step in vitro procedure. AA content was determined for the HC samples (heat treated and untreated) of the intact feed, the 16 h in situ residue and the residue after the three-step procedure. There was a linear increase in RUP (p = 0.001) and intestinal digestibility of RUP (p = 0.003) with increasing temperature during heat treatment. The $130^{\circ}C$ treatment increased RUP from 259 to 629 g/kg CP, while intestinal digestibility increased from 176 to 730 g/kg RUP, compared to the control. Hence, the intestinal available dietary CP increased more than eight times. Increasing temperatures during heat treatment resulted in linear decreases in ruminal degradability of total AA (p = 0.006) and individual AA (p<0.05) and an increase in intestinal digestibility that could be explained both by a linear and a quadratic model for total AA and most individual AA (p<0.05). The $130^{\circ}C$ treatment decreased ruminal degradability of total AA from 837 to 471 g/kg, while intestinal digestibility increased from 267 to 813 g/kg of rumen undegradable AA, compared with the control. There were differences between ruminal AA degradability and between intestinal AA digestibility within all individual HC treatments (p<0.001). It is concluded that moist heat treatment at $130^{\circ}C$ did not overprotect the CP of HC and could be used to shift the site of CP and AA digestion from the rumen to the small intestine. This may increase the value of HC as a protein supplement for ruminants.

The Heat Shock Protein 27 (Hsp27) Operates Predominantly by Blocking the Mitochondrial-Independent/Extrinsic Pathway of Cellular Apoptosis

  • Tan, Cheau Yih;Ban, Hongseok;Kim, Young-Hee;Lee, Sang-Kyung
    • Molecules and Cells
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    • v.27 no.5
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    • pp.533-538
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    • 2009
  • Heat shock protein 27 (Hsp27) is a molecular chaperone protein which regulates cell apoptosis by interacting directly with the caspase activation components in the apoptotic pathways. With the assistance of the Tat protein transduction domain we directly delivered the Hsp27 into the myocardial cell line, H9c2 and demonstrate that this protein can reverse hypoxia-induced apoptosis of cells. In order to characterize the contribution of Hsp27 in blocking the two major apoptotic pathways operational within cells, we exposed H9c2 cells to staurosporine and cobalt chloride, agents that induce mitochondria-dependent (intrinsic) and -independent (extrinsic) pathways of apoptosis in cells respectively. The Tat-Hsp27 fusion protein showed a greater propensity to inhibit the effect induced by the cobalt chloride treatment. These data suggest that the Hsp27 predominantly exerts its protective effect by interfering with the components of the extrinsic pathway of apoptosis.

Allergenicity Reduction of Milk (우유에서의 알레르겐 저감화 방법)

  • Ha, Woel-Kyu
    • Journal of Dairy Science and Biotechnology
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    • v.26 no.1
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    • pp.27-36
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    • 2008
  • This review was written to introduce updated data on the structure and function of the major milk proteins identified as allergens, the characterization of their epitopes in each allergenic milk proteins, and the reduction of milk protein allergenicity. Most mammalian milk protein, even protein present at low concentration, are potential allergens. Epitopes identified in milk proteins are both conformational(structured epitope) and sequential epitopes(linear epitope), throughout the protein molecules. Epitopes on casein and whey proteins are reported to be sequential epitope and conformational epitopes, respectively. Conformational epitopes on whey protein are changed into sequential epitope by heat denaturation during heat treatment. Several methods have been proposed to reduce allergenicity of milk proteins. Most ideal and acceptable method to make hypoallergenic milk or formula, so far, is the hydrolysis of allergenic milk proteins by enzymes that has substrate specificity, such as pepsin, trypsin, or chymotrypsin. Commercial formulas based on milk protein hydrolysate are available for therapeutic purpose, hypoantigenic formula for infants from families with a history of milk allergy and hypoallergenic formula for infants with existing allergic symptoms.

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Effects of Extraction Method on the Carnosine, Protein, and Iron Contents of Eel (Anguilla japonica) Extracts (뱀장어 (Anguilla japonica) 추출물 중의 Carnosine, 단백질 및 철분 함량에 미치는 추출방법의 영향)

  • Song, Ho-Soo;Lee, Keun-Tai;Kang, Ok-Ju
    • Korean Journal of Fisheries and Aquatic Sciences
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    • v.39 no.5
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    • pp.384-390
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    • 2006
  • To improve the extractability of carnosine and the levels of pro-oxidants such as iron in eel (Anguilla japonica) extracts, we examined the effects of extraction time, temperature, ion exchange chromatography and ultrafiltration (UF). The respective protein and total iron were reduced approximately 55 and 60% at 60$^{\circ}C$, 63 and 70% at 80$^{\circ}C$, 68 and 76% at 100$^{\circ}C$ and 82 and 48% with ion exchange chromatography, respectively, compared to the untreated extract. However, there was no significant difference in the carnosine levels in the eel extracts. Ultrafiltration reduced the protein content of the extract by 52% compared with the untreated extract. UF reduced the protein contents of the samples from 60, 80, and 100% heat treatment and ion exchange chromatography treatment by 27, 50, 46 and 47%, respectively. UF reduced the total iron contents of the identical four treatments by 14, 22, 23, and 43%, respectively, while UF increased the carnosine by 23, 17, 20, and 6%, respectively.

Comparison of the Heat Treatment Intensity in Infant Formulae (조제분유의 열처리 정도 비교)

  • Park, Young-Hee;Hong, Youn-Ho
    • Korean Journal of Food Science and Technology
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    • v.23 no.5
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    • pp.627-632
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    • 1991
  • The heat treatment indicators such as HMF contents, lactulose contents and whey protein denaturation rates were measured to refer to the heat treatment intensity of domestic market infant formulae. The HMF contents showed $21.0{\sim}43.9{\mu}mol/l:$ in the case of powder types, the HMF contents in enriched nutrient products(ii) were higher whereas in the case of liquid types they were packed in cans(i). The lactulose contents showed $2.5{\sim}11.4mg/100ml$ in the powder type and $27.0{\sim}164.8mg/100ml$ in the liquid type. There was much difference in the lactulose contents according to the product types. Compared with the ADPI standards, most of infant formulae were considered to be medium-heat class. The whey protein denaturation rates were $1.1{\sim}69.4%$ in the powder type and $37.4{\sim}71.3%$ in the liquid type.

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A Comparison Study on Functional Properties of Peanut Protein and Chemically Modified Peanut Protein (분리 땅콩 단백질과 화학적으로 수식화한 단백질간의 식품학적 특성 비교)

  • Sohn, Kyung-Hee;Min, Sung-Hee;Park, Hyun-Kyung;Park, Jin
    • Korean journal of food and cookery science
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    • v.7 no.2
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    • pp.97-104
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    • 1991
  • This study was carried out in order to study the protein functionality such as foaming and emulsifying properties by succinylation of peanut protein isolates. Succinylated and unsuccinylated peanut protein isolate was tested for to find out the effect of pH, heat treatment and sodium chloride concentration on the solubility, foam expansion, foam stability, emulsion capacity and emulsion stability. The results are summarized as follows; 1. Succinylation enhanced the solubility of peanut protein isotate (PPI). The solubility of succinylated PPI markedly increased at pH 4.5. When the protein solutions was heated, the solubility of succinylated PPI greatly increased than PPI at pH 3. With addition of NaCl, solubility of succinylated PPI increased at pH 7 and pH 9. 2. The foam expansion of PPI and succinylated PPI on pH was no difference between both proteins. Addition of NaCl and heat treatment caused steeply increased in foam expansion at pH 3. 3. The foam stability of PPI and succinylated PPI showed the lowest value at pH 4.5. When PPI and succinylated PPI was heated, foam stability of two proteins incensed at pH 3 and showed similar aspects between PPI and succinylated PPI. However, at pH 9 stability of succinylated PPI decreased by heat treatment over $60^{\circ}C$. 4. Emulsion capacity of succinylated PPI on pH was markedly increased and showed the highest value at pH 11. At pH 4.5 which is isoelectric point of PPI, emulsion capacity of PPI by succinylation improved than that of PPI. When succinylated PPI was heated, emulsion capacity was greatly increased at pH 2 and pH 7. With NaCl was added, emulsion capacity of succinylated PPI increased than that of PPI. 5. Emulsion stability of PPI and succinylated PPI was affected by pH and showed its highest value at pH 11. At pH 4.5, emulsion stability of succinylated PPI increased than that of PPI. Addition of NaCl and heat treatment caused slightly increased in emulsion stability of succinylated PPI.

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Functional Properties of Soy Protein Isolate from Heat Treated Soybean (열처리 대두에서 분리한 대두 단백질의 기능성)

  • Yoon, Hye-Hyun;Jeon, Eun-Jae
    • Korean Journal of Food Science and Technology
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    • v.36 no.1
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    • pp.38-43
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    • 2004
  • Effects of heat treatment on functional properties of soy protein were examined. Soy protein isolate (SPI) was prepared from Korean soybean varieties, Manli and Taekwang, subjected to heat treatment at $60^{\circ}C$ for 30, 60, 90, and 120 min. pH-solubility results of SPI showed typical U-shape profiles with minimum solubility at pH 4-5 of isoelectric points of soy proteins, longer heat treatments showing slightly higher solubility. Water absorption, emulsifying activity, emulsion stability, and emulsion capacity of SPI increased, while oil absorption decreased, with heating time in Manli variety. Manli and Taekwang showed the highest emulsion capacities after 90-and 60-min heat treatments, respectively. Foam expansion of all SPIs increased with heating time up to 90 min. Texture profile analysis showed heat treatment up to 90 min significantly increased hardness, adhesiveness, springiness, gumminess, and chewiness, whereas significantly decreased cohesiveness of SPI gels (p<0.05).

Caffeine Induces the Stress Response and Up-Regulates Heat Shock Proteins in Caenorhabditis elegans

  • Al-Amin, Mohammad;Kawasaki, Ichiro;Gong, Joomi;Shim, Yhong-Hee
    • Molecules and Cells
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    • v.39 no.2
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    • pp.163-168
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    • 2016
  • Caffeine has both positive and negative effects on physiological functions in a dose-dependent manner. C. elegans has been used as an animal model to investigate the effects of caffeine on development. Caffeine treatment at a high dose (30 mM) showed detrimental effects and caused early larval arrest. We performed a comparative proteomic analysis to investigate the mode of action of high-dose caffeine treatment in C. elegans and found that the stress response proteins, heat shock protein (HSP)-4 (endoplasmic reticulum [ER] chaperone), HSP-6 (mitochondrial chaperone), and HSP-16 (cytosolic chaperone), were induced and their expression was regulated at the transcriptional level. These findings suggest that high-dose caffeine intake causes a strong stress response and activates all three stress-response pathways in the worms, including the ER-, mitochondrial-, and cytosolic pathways. RNA interference of each hsp gene or in triple combination retarded growth. In addition, caffeine treatment stimulated a food-avoidance behavior (aversion phenotype), which was enhanced by RNAi depletion of the hsp-4 gene. Therefore, up-regulation of hsp genes after caffeine treatment appeared to be the major responses to alleviate stress and protect against developmental arrest.

Degradation of Polyhedral Proteins of Nuclear Polyhedrosis Viruses in the Gut Juice of Several Lepidopteran Larvae (곤충 핵다각체병 바이러스 다각체 단백질의 소화액에 의한 분해)

  • 진병래;박범석;우수동;김주읍;강석권
    • Microbiology and Biotechnology Letters
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    • v.21 no.6
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    • pp.513-519
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    • 1993
  • The alkaline protease in the polyhedra preparation of Spodoptera litura nuclear polyhedrosis virus was successfully inactivated by heating at 100C for 20 minutes. SDS-PAGE analysis indicated that heat inactivated polyhedra is composed of major proteins of 31kDa and presumptive its polymer protein of 62kDa. However, this polyhedra was converted into several smaller molecular weight proteins when treated with midgut juice, but not by treatment with heat-inactivated midgut juice.

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Factors Affecting on Protein Stability of Mixed Cow and Soy Milk (콩우유와 우유 혼합유의 단백질 안정성에 미치는 영향인자)

  • 정남용;김우정
    • The Korean Journal of Food And Nutrition
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    • v.7 no.4
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    • pp.345-352
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    • 1994
  • High protein beverage of cow-soy milk was prepared by mixing the soymilk and commercial homogenized cow milk in the various ratios. Effect of heat treatment, pH and addition of calcium and sucrose was studied on the water-soluble nitrogen of cow-soy milk The heat-treated soymilk at 10$0^{\circ}C$ were centrifuged at the range of 830~29,900xg for 30 min and 11,200xg was found to be proper for determination of the degree of protein denaturation by centrifugal method. When soymilk was heated at 70~10$0^{\circ}C$ for 30~240 min, soluble nitrogen (QA SN) in supernatant of protein was decreased to 78.0~56.8% due to protein denaturation. Most of heat denaturation of protein was found to be occurred during Initial heating 10$0^{\circ}C$ for all mixed cow-soy milk. The sedimentation of SN was maximum at pH 4.0 In the range of pH 3~8. Addition of sucrose affected little on oASN while calcium addition reduced %SN significantly to approx. 55% for soymilk(100%). The effect of Ca was less as the ratio of cow milk increased.

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