• Title/Summary/Keyword: Protein Denaturation

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Effects of Morphological Characteristics of Muscle Fibers on Porcine Growth Performance and Pork Quality

  • Lee, Sang Hoon;Kim, Jun-Mo;Ryu, Youn Chul;Ko, Kwang Suk
    • Food Science of Animal Resources
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    • v.36 no.5
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    • pp.583-593
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    • 2016
  • The aim of this study was to investigate the effects of morphological characteristics of porcine muscle fibers on growth performance, muscle fiber characteristics, and pork quality taken from the longissimus dorsi muscle. A total of 239 crossbred pigs (164 castrated males and 75 females) were used in this study. Experimental pigs were categorized by the total number of muscle fiber (TNF: High and Low) and cross sectional area of muscle fiber (CSAF: Large, Middle, and Small). Their combinations were classified into six groups (High-Large, HL; High-Middle, HM; High-Small, HS; Low-Large, LL; Low-Middle, LM; Low-Small, LS). The TNF and CSAF were significantly (p<0.05) correlated with growth rate and carcass productivity, while the only of the type I number had no meaningful relationships excluding the correlation with loin area (p<0.001). The proportion of type I area was positively correlated with pH45 min while the proportion of type IIB area was negatively correlated with pH45 min and pH24 h (p<0.05). Drip loss and protein denaturation had strong relationships with the proportion of type IIB number or area. The HL group exhibited the greatest growth performance. In addition, the HL group had significantly greater values in protein solubility than the other groups. In conclusion, this study suggest that high TNF combined to large CSAF improve the ultimate lean meat productivity and assure normal meat quality simultaneously with increased both proportion of number and area of type I, type IIA muscle fibers and lowered proportion of number and area of type IIB.

Acid and Chemical Induced Conformational Changes of Ervatamin B. Presence of Partially Structured Multiple Intermediates

  • Sundd, Monica;Kundu, Suman;Jagannadham, Medicherla V.
    • BMB Reports
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    • v.35 no.2
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    • pp.143-154
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    • 2002
  • The structural and functional aspects of ervatamin B were studied in solution. Ervatamin B belongs to the $\alpha+\beta$ class of proteins. The intrinsic fluorescence emission maximum of the enzyme was at 350 nm under neutral conditions, and at 355 nm under denaturing conditions. Between pH 1.0-2.5 the enzyme exists in a partially unfolded state with minimum or no tertiary structure, and no proteolytic activity. At still lower pH, the enzyme regains substantial secondary structure, which is predominantly $\beta$-sheet conformation and shows a strong binding to 8-anilino-1-napthalene-sulfonic acid (ANS). In the presence of salt, the enzyme attains a similar state directly from the native state. Under neutral conditions, the enzyme was stable in urea, while the guanidine hydrochloride (GuHCl) induced equilibrium unfolding was cooperative. The GuHCl induced unfolding transition curves at pH 3.0 and 4.0 were non-coincidental, indicating the presence of intermediates in the unfolding pathway. This was substantiated by strong ANS binding that was observed at low concentrations of GuHCl at both pH 3.0 and 4.0. The urea induced transition curves at pH 3.0 were, however, coincidental, but non-cooperative. This indicates that the different structural units of the enzyme unfold in steps through intermediates. This observation is further supported by two emission maxima in ANS binding assay during urea denaturation. Hence, denaturant induced equilibrium unfolding pathway of ervatamin B, which differs from the acid induced unfolding pathway, is not a simple two-state transition but involves intermediates which probably accumulate at different stages of protein folding and hence adds a new dimension to the unfolding pathway of plant proteases of the papain superfamily.

Impact of Humectants on Physicochemical and Functional Properties of Jerky: A Meta-Analysis

  • Shine Htet Aung;Ki-Chang Nam
    • Food Science of Animal Resources
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    • v.44 no.2
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    • pp.464-482
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    • 2024
  • This study aimed to determine the effects of humectants on moisture content, water activity, tenderness, color, microbiological analysis, protein denaturation, and oxidation of jerky. A thorough search for papers published in scientific journals that examined the impacts of humectants on jerky was carried out using Web of Science, Google Scholar, PubMed, and Science Direct. Only 14 studies matched inclusion requirements. They were used in the meta-analysis to synthesise quantitative findings. In the current investigation, jerky produced with beef, poultry, goat, or pork was used. The standardised mean difference (SMD) between treatments with humectants and controls was examined to investigate the effects of humectants using random-effects models. Heterogeneity was investigated using meta-regression. A subgroup analysis was carried out for significant factors. Results revealed that the addition of humectants had no significant impact on water activity, pH, fat, ash, CIE L*, or CIE a* (p>0.05). However, humectant addition significantly increased moisture (SMD=1.28, p<0.05), CIE b* (SMD=1.67, p<0.05), and overall acceptability (SMD=1.73, p<0.05). It significantly decreased metmyoglobin (SMD=-0.96, p<0.05), shear force (SMD=-0.84, p<0.05), and protein (SMD=-1.61, p<0.05). However, it was difficult to get a firm conclusion about how humectants affected the myofibrillar fragmentation index, total plate count, and 2-thiobarbituric acid-reactive substances because there were fewer than ten studies. To sum up, the proper use of humectants in jerky demands careful attention to both type and quantity, needing a delicate balancing act with other contributing factors.

Enhancement of Cookie Quality by Microwave Treatment of Allergy Reaction-reduced "Ofree" Wheat Flour (마이크로웨이브 조사를 통한 알러지 저감 밀 오프리의 제과 가공적성 개선)

  • Park, JinHee;Yoon, Young-Mi;Son, Jae-Han;Choi, Chang-Hyun;Kim, Kyeong-Hoon;Kim, Kyeong-Min;Cheong, Young-Keun;Kang, Chon-Sick;Yang, Jinwoo
    • KOREAN JOURNAL OF CROP SCIENCE
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    • v.64 no.4
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    • pp.366-372
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    • 2019
  • The use of flour milled from the Ofree wheat cultivar for baking attenuates allergies because some of the genes related to the allergic reaction have been knocked because some of its genes related to allergic reactions have been knocked down or knocked out through genetic mutation. However, the utilization of this flour is limited because the Ofree grain contains high content of total protein and gluten. Microwave irradiation has been used for changing the protein and gluten characteristics of wheat flour. Thus, this study investigated appropriate conditions of microwave irradiation to enhance the utilization of Ofree flour. As a result, when the flour was microwave-treated for 2 min, although the total protein and gluten contents were not changed, some qualities of the baked sugar-snap cookies, such as spread factor (diameter and thickness) and appearance (crack), were ameliorated. However, excessive heat treatment of the flour for over 3 min led to protein denaturation, which negatively affected the quality of the products. These results indicate that 2 min of microwave irradiation of flour that has high content of total protein and gluten can be used for the enhancement of cookie quality. Therefore, these results are expected to increase the utilization of Ofree wheat flour.

Effect of different short-term high ambient temperature on chicken meat quality and ultra-structure

  • Zhang, Minghao;Zhu, Lixian;Zhang, Yimin;Mao, Yanwei;Zhang, Mingyue;Dong, Pengcheng;Niu, Lebao;Luo, Xin;Liang, Rongrong
    • Asian-Australasian Journal of Animal Sciences
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    • v.32 no.5
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    • pp.701-710
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    • 2019
  • Objective: This study investigated the effect of different acute heat stress (HS) levels on chicken meat quality and ultra-structure. Methods: Chickens were randomly divided into 7 groups to receive different HS treatments: i) $36^{\circ}C$ for 1 h, ii) $36^{\circ}C$ for 2 h, iii) $38^{\circ}C$ for 1 h, iv) $38^{\circ}C$ for 2 h, v) $40^{\circ}C$ for 1 h, vi) $40^{\circ}C$ for 2 h, and vii) un-stressed control group ($25^{\circ}C$). Blood cortisol level, breasts initial temperature, color, pH, water holding capacity (WHC), protein solubility and ultra-structure were analyzed. Results: HS temperatures had significant effects on breast meat temperature, lightness ($L^*$), redness ($a^*$), cooking loss and protein solubility (p<0.05). The HS at $36^{\circ}C$ increased $L^*{_{24h}}$ value (p<0.01) and increased the cooking loss (p<0.05), but decreased $a^*{_{24h}}$ value (p<0.05). However, as the temperature increased to $38^{\circ}C$ and $40^{\circ}C$, all the values of $L^*{_{24h}}$, cooking loss and protein denaturation level decreased, and the differences disappeared compared to control group (p>0.05). Only the ultimate $pH_{24h}$ at $40^{\circ}C$ decreased compared to the control group (p<0.01). The pH in $36^{\circ}C$ group declined greater than other heat-stressed group in the first hour postmortem, which contributed breast muscle protein degeneration combining with high body temperature, and these variations reflected on poor meat quality parameters. The muscle fiber integrity level in group $40^{\circ}C$ was much better than those in $36^{\circ}C$ with the denatured position mainly focused on the interval of muscle fibers which probably contributes WHC and light reflection. Conclusion: HS at higher temperature (above $38^{\circ}C$) before slaughter did not always lead to more pale and lower WHC breast meat. Breast meat quality parameters had a regression trend as HS temperature raised from $36^{\circ}C$. The interval of muscle fibers at 24 h postmortem and greater pH decline rate with high body temperature in early postmortem period could be a reasonable explanation for the variation of meat quality parameters.

Cloning and Expression of Escherichia coli Ornithine Transcarbamylase Gene, argI (Escherichia coli 오르니틴 트란스카바밀라제의 유전자 argI의 클로닝 및 발현)

  • Riu, Key-Zung;U, Zang-Kual;Ko, Young-Hwan;Kim, Chan-Shik;Song, Sung-Jun;Oh, Young-Seon;Lee, Sun-Joo
    • Applied Biological Chemistry
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    • v.38 no.2
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    • pp.118-122
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    • 1995
  • Escherichia Coli ornithine transcarbamylase is the enzyme which catalyzes the L-citrulline biosynthesis from L-ornithine and carbamyl phosphate. To facilitate the purification of enzyme which will be used for many biochemical studies such as structure and function relationships and catalytic mechanisms, the cloning and expression of E. coli argI gene for ornithine transcarbamylase was conducted. argI was amplified from genomic DNA of E. coli strain of $DH5{\alpha}$, by polymerization chain reaction (PCR) method. The amplified argI gene was ligated to the prokaryotic expression vector pKK223-3 and used for transformation of E. coli TB2 which was deficient of ornithine transcarbamylase. The over-produced enzyme by the tnansformant was purified by ammonium sulfate fractionation, heat denaturation and affinity chromatography. The result of SDS denaturation gel electrophoresis for the purified enzyme showed a single band of about 38 kDa of ornithine transcarbamylase. Kinetic data for the expressed enzyme gave almost the s?????? values as those of the wild type enzyme. The $k_{cat}$, of the enzyme was $1.0{\times}10^5min^{-1}$, and $K_ms$ for ornithine and carbamyl phosphate were 0.35 mM and 0.06 mM, respectively.

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Improvement on Textural Properties of Soybean Curd by Freeze Denaturation of Soybeans (대두의 동결처리에 의한 두부의 텍스쳐 특성의 증진)

  • Baik, Sang-Ho;Kim, Myung-Kon;Yun, Sei-Eok;Joo, Hyun-Kyu
    • Korean Journal of Food Science and Technology
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    • v.28 no.2
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    • pp.267-272
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    • 1996
  • Effect of freezing of soybeans on instrumental and sensory textures of soybean curd was investigated. The hardness, gumminess and chewiness of soybean curd prepared with frozen soybeans were about three times as high as those prepared with unfrozen soybeans, while cohesiveness and elasticity were affected little by freezing. Sensory evaluation showed that freezing improved the quality of soybean curd. Instrumental and sensory textures of soybean curd prepared with frozen soybeans were excellent and almost same regardless of the boiling time when the soy slurry was boiled for 2.5 min or 5 min. However, the textures of soybean curd prepared with unfrozen soybeans were deteriorated by reducing the boiling time to 2.5 min. It was postulated that freezing facilitate the heat-denaturation of soyprotein to enhance aggregation of soy proteins and formation of cross-linkage between aggregate and $Ca^{++}$. Frozen soybeans resulted in soybean curd which lower fat content, while protein content of soybean curd was almost he same. Frozen soybeans gave a lower yield of soybean curd, which is supposed to be caused by the more fat loss during whey-off.

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Fabrication, Estimation and Trypsin Digestion Experiment of the Thermally Isolated Micro Teactor for Bio-chemical Reaction

  • Sim, Tae-Seok;Kim, Dae-Weon;Kim, Eun-Mi;Joo, Hwang-Soo;Lee, Kook-Nyung;Kim, Byung-Gee;Kim, Yong-Hyup;Kim, Yong-Kweon
    • JSTS:Journal of Semiconductor Technology and Science
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    • v.5 no.3
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    • pp.149-158
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    • 2005
  • This paper describes design, fabrication, and application of the silicon based temperature controllable micro reactor. In order to achieve fast temperature variation and low energy consumption, reaction chamber of the micro reactor was thermally isolated by etching the highly conductive silicon around the reaction chamber. Compared with the model not having thermally isolated structure, the thermally isolated micro reactor showed enhanced thermal performances such as fast temperature variation and low energy consumption. The performance enhancements of the micro reactor due to etched holes were verified by thermal experiment and numerical analysis. Regarding to 42 percents reduction of the thermal mass achieved by the etched holes, approximately 4 times faster thermal variation and 5 times smaller energy consumption were acquired. The total size of the fabricated micro reactor was $37{\times}30{\times}1mm^{3}$. Microchannel and reaction chamber were formed on the silicon substrate. The openings of channel and chamber were covered by the glass substrate. The Pt electrodes for heater and sensor are fabricated on the backside of silicon substrate below the reaction chamber. The dimension of channel cross section was $200{\times}100{\mu}m^{2}$. The volume of reaction chamber was $4{\mu}l$. The temperature of the micro reactor was controlled and measured simultaneously with NI DAQ PCI-MIO-16E-l board and LabVIEW program. Finally, the fabricated micro reactor and the temperature control system were applied to the thermal denaturation and the trypsin digestion of protein. BSA(bovine serum albumin) was chosen for the test sample. It was successfully shown that BSA was successfully denatured at $75^{\circ}C$ for 1 min and digested by trypsin at $37^{\circ}C$ for 10 min.

Cryoprotective Effect and Mechanism of Corn Starch Enzyme Hydrolysates on Fish Protein 1. Cryoprotective Effect of Corn Starch Enzyme Hydrolysates on Fish Protein (전분가수분해물의 어육단백질 동결변성 방지효과 및 작용기구 1. 옥수수전분가수분해물의 어육단백질에 대한 동결변성 방지효과)

  • LEE Kang-Ho;JUNG Byung-Chun;HONG Byung-Il
    • Korean Journal of Fisheries and Aquatic Sciences
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    • v.31 no.6
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    • pp.823-828
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    • 1998
  • The objective of this study is to investigate cryoprotective effects of corn starch enzyme hydrolysates of nonsweet and low-calories on denaturation of frozen fish protein. The cryoprotective effects of were examined in Alaska pollack actomyosin solution by changes in SDS-PAGE pattern, solubility, and $Ca^{2+}$-ATPase activity. When samples stored for 0 and 30 days were compared on SDS-PAGE patterns, severe changes in all bands were shown on the control sample regardless of storage temperature, especially in myosin heavy chain (MHC). Not much difference no appeared the electrophoretic pattern in case of the samples containing sucrose at any storage temperature during 30 days of storage. The cryoprotective effect of the hydrolysates were markedly dependant on storage temperature and no MHC band was found in the samples stored at $-5^{\circ}C$. The SDS-PAGE patterns of sample stored at $-20^{\circ}C$, however, completely maintained after 30 days or storage. When the samples were stored at $-5^{\circ}C$, the solubility of the sample containing sucrose was retained at $90\%$ after 30 days of storage, whereas dramatically decreased in other samples. The samples including sucrose, D.E. 10, 15, and 20 revealed $90\%$ in solubility when stored at $-20^{\circ}C$. The tendency of remaining $Ca^{2+}$-ATPase activity was almost shown the same as that of solubility.

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Studies on Preservation of Concentrated Milk by Freeze - Flow Process (Freeze - Flow Process 를 이용한 농축우유의 저장에 관한 연구)

  • Lee, Young-Chun;Shin, Dong-Bin
    • Korean Journal of Food Science and Technology
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    • v.17 no.6
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    • pp.500-505
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    • 1985
  • A method to store concentrated milk in the liquid state at $-15^{\circ}C$ was developed, and quality changes during storage of milk were evaluated. Combined cryoprotectants (CCP) suitable for storing concentrated milk in the liquid state at $-15^{\circ}C$ were consisted of 17.74% sucrose, 8.87% glucose, 8.87% fructose, 2% glycerol, 0.25% sodium hexametaphosphate, 0.25% NaCl and 0.02% ascorbic acid. The amount of CCP to be added to concentrated milk to depress freezing point to $-15^{\circ}C$ was 38% by weight. Gelation due to protein denaturation was the most serious quality change during storage, which adversely affected appearance and utilization of the stored product. Gelation was observed after 3 weeks storage in the control, but it was not in milk with CCP throughout 18 weeks storage. Amount of protein precipitated increased in the control during storage, whereas there was no protein precipitated in milk with CCP. Surface color and peroxide value of the control and treatment did not change significantly during storage, and there were no marked differences between the control and treatment. These results indicated that quality of concentrated milk could be preserved, without gelation, by storing milk with CCP in the -liquid state at the frozen storage temperature. Besides, energy required for freezing preservation of milk could be significantly reduced by elimination of phase changes for freezing and thawing, and the stored product could be continuously processed for the final products without long waiting time for thawing.

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