• Title/Summary/Keyword: myoglobin

Search Result 169, Processing Time 0.025 seconds

Mechanism of Lipid Peroxidation in Meat and Meat Products -A Review

  • Min, B.;Ahn, D.U.
    • Food Science and Biotechnology
    • /
    • v.14 no.1
    • /
    • pp.152-163
    • /
    • 2005
  • Lipid peroxidation is a primary cause of quality deterioration in meat and meat products. Free radical chain reaction is the mechanism of lipid peroxidation and reactive oxygen species (ROS) such as hydroxyl radical and hydroperoxyl radical are the major initiators of the chain reaction. Lipid peroxyl radical and alkoxyl radical formed from the initial reactions are also capable of abstracting a hydrogen atom from lipid molecules to initiate the chain reaction and propagating the chain reaction. Much attention has been paid to the role of iron as a primary catalyst of lipid peroxidation. Especially, heme proteins such as myoglobin and hemoglobin and "free" iron have been regarded as major catalysts for initiation, and iron-oxygen complexes (ferryl and perferryl radical) are even considered as initiators of lipid peroxidation in meat and meat products. Yet, which iron type and how iron is involved in lipid peroxidation in meat are still debatable. This review is focused on the potential roles of ROS and iron as primary initiators and a major catalyst, respectively, on the development of lipid peroxidation in meat and meat products. Effects of various other factors such as meat species, muscle type, fat content, oxygen availability, cooking, storage temperature, the presence of salt that affect lipid peroxidation in meat and meat products are also discussed.

Synthesis of Muscle Proteins During the Differentiation of Cultured Chicken Pectoralis Muscle Cells (培養 鷄胚 筋細胞의 分化에 따른 筋特異 蛋白質의 合成과 젖산탈수소 효소의 活性에 관하여)

  • Ha, Doo-Bong;Im, Wook-Bin;Yoo, Byoung-Je
    • The Korean Journal of Zoology
    • /
    • v.24 no.4
    • /
    • pp.173-188
    • /
    • 1981
  • 근세포의 분화에 있어서의 근특이 단백질의 합성 순서를 구명하기 위하여 계배 근세포를 2$\\sim$9일간 배양하면서 단백질합성야상을 SDS-polyacrylamide 겔전기 영동법, 등전점초점2차원 전기영동법 및 방사자기법으로 분석하였다. Actin은 분화의 초기부터 활발히 합성되어 그 양이 다량으로 축적되나, myosin은 배양 3일째부터 대량 합성되기 시작하였다. Myosin의 대량합성시기는 배양 근원세포가 융합을 활발히 일으키는 시기와 거의 같았다. Myoglobin은 분화초기부터 서서히 합성축적되기 시작하여 배양 5일에서 최대치에 달하였다. Creatine phosphokinase는 배양 3일만에, 그리고 glyceraldehyde dehydrogenase는 6일만에 전기영동상에 검출되었다. Tropomyosin $\\alpha$와 $\\beta$, 그리고 troponin C는 분화초기부터 비교적 다량 합성되고 있었다. 젖산탈수소효소의 활성은 배양 2$\\sim$5일 사이에서 급격히 증가하고 이후 거의 변화가 없었다. 이 효소의 동위효소 조성은 초기 근원세포에서는 $H_4$와 $H_3M$형이 많으나 분화가 진행됨에 따라 $HM_3 와 M_4$형이 서서히 출현하였다. 그리고 배양 5일만에 5종의 동위효소가 모두 검출되었다.

  • PDF

An Amber Force Field for S-Nitrosoethanethiol That Is Transferable to S-Nitrosocysteine

  • Han, Sang-Hwa
    • Bulletin of the Korean Chemical Society
    • /
    • v.31 no.10
    • /
    • pp.2903-2908
    • /
    • 2010
  • Protein S-nitrosation is common in cells under nitrosative stress. In order to model proteins with S-nitrosocysteine (CysSNO) residues, we first developed an Amber force field for S-nitrosoethanethiol (EtSNO) and then transferred it to CysSNO. Partial atomic charges for EtSNO and CysSNO were obtained by a restrained electrostatic potential approach to be compatible with the Amber-99 force field. The force field parameters for bonds and angles in EtSNO were obtained from a generalized Amber force field (GAFF) by running the Antechamber module of the Amber software package. The GAFF parameters for the CC-SN and CS-NO dihedrals were not accurate and thus determined anew. The CC-SN and CS-NO torsional energy profiles of EtSNO were calculated quantum mechanically at the level of B3LYP/cc-pVTZ//HF/6-$31G^*$. Torsional force constants were obtained by fitting the theoretical torsional energies with those obtained from molecular mechanics energy minimization. These parameters for EtSNO reproduced, to a reasonable accuracy, the corresponding torsional energy profiles of the capped tripeptide ACE-CysSNO-NME as well as their structures obtained from quantum mechanical geometry optimization. A molecular dynamics simulation of myoglobin with a CysSNO residue produced a well-behaved trajectory demonstrating that the parameters may be used in modeling other S-nitrosated proteins.

Artificial Metalloproteases with Broad Substrate Selectivity Constructed on Polystyrene

  • Ko, Eun-Hwa;Suh, Jung-Hun
    • Bulletin of the Korean Chemical Society
    • /
    • v.25 no.12
    • /
    • pp.1917-1923
    • /
    • 2004
  • Although the proteolytic activity of the Cu(II) complex of cyclen (Cyc) is greatly enhanced upon attachment to a cross-linked polystyrene (PS), the Cu(II)Cyc-containing PS derivatives reported previously hydrolyzed only a very limited number of proteins. The PS-based artificial metalloproteases can overcome thermal, mechanical, and chemical instabilities of natural proteases, but the narrow substrate selectivity of the artificial metalloproteases limits their industrial application. In the present study, artificial metalloproteases exhibiting broad substrate selectivity were synthesized by attaching Cu(II)Cyc to a PS derivative using linkers with various structures in an attempt to facilitate the interaction of various protein substrates with the PS surface. The new artificial metalloproteases hydrolyzed all of the four protein substrates (albumin, myoglobin, ${\gamma}$-globulin, and lysozyme) examined, manifesting $k_{cat}/K_m$ values of 28-1500 $h_{-1}M_{-1}$ at 50 $^{\circ}C$. The improvement in substrate selectivity is attributed to steric and/or polar interaction between the bound protein and the PS surface as well as the hydrophobicity of the microenvironment of the catalytic centers.

Identification of the Proteins Expressed at Optimum Marbling in Hanwoo Loin (한우육의 육질에 중요 영향을 미치는 근내지방축적 최적기에 발현되는 단백질 동정)

  • 임진규
    • Journal of the Korean Society of Food Science and Nutrition
    • /
    • v.28 no.3
    • /
    • pp.579-585
    • /
    • 1999
  • Proteins from the loin tissues age ranged from 0 to 24 months of ten Korean cattle were extracted, separated and compared on two dimensional(2 D) gels to identify the proteins whose expression is highly correlated to marbling. We also compared the difference of loin proteins between castrated and non castrated bull cows on two dimensional gels. As the marbling in the loin of the cattle is optimized at 18 to 24 months, eight proteins expressed significantly higher level in 24 month than in 0 or 6 month were selected in terms of isoelectric points(pIs) and molecular weights. Using these values, we searched the Swiss Prot database via the ExPASy molecular biology server with TagIdent program. The proteins with the nearest molecular weights and isoelectric points were selected from the lists. These possible candidates were confirmed by N terminal microsequencing of the eight selected proteins. Three proteins, myoglobin, hemoglobin and ATPase, whose N termini were not blocked could be microsequenced and found to be exactly matched to the selected candidates. It is suggested that the proteins increasingly expressed in marbling periods can be involved in meat color, lipid transport and flavor improvement.

  • PDF

Functional Properties of Mechanically Deboned Chicken Meat from Various Chicken Parts (부위별로 제조된 기계발골 계육의 가공적성에 관한 연구)

  • 이성기;김희주;김용재;조규석;김종원
    • Korean Journal of Poultry Science
    • /
    • v.21 no.4
    • /
    • pp.277-284
    • /
    • 1994
  • The functional properties of mechanically deboned chicken meat(MDCM) from whole carcass, whole carcass without exsanguination, neck without skin, leg hone, and upper back and rib were studied. Also, the effects of adding different levels of gelatin and MDCM to the comminuted meats were investigated. Proximate composition values of MDCM ranged from 54.2 to 68.6% moisture, 14.5 to 19.7% protein, 12.3 to 30.1% fat, and 1.1 to 1.3% ash. The MDCM from leg hone had a higher content of fat, and a lower contents of moisture and protein. The MDCM from neck without skin tended to be opposite to the MDCM from leg hone. The total pigment and myoglobin levels were highest in MDCM from whole carcass without exsanguination such as 3.83 and 0.29 rng /g, and those from the other parts were 1.58~2.93 mg /g and 0. 17~0.31 mg /g, respectively. The emulsifying capacity and water holding capacity were highest in MDCM from neck without skin which contained lower levels of fat, collagen and hydroxyproline, but a higher level of salt soluble protein. The emulsifying capacity of comminuted meat decreased as gelatin content increased. The extractability of hydroxyproline from gelatin showed a higher solubility in acidic solution. The MDCM could he added up to 20% level without detrimentally affecting functional properties of comminuted meats although they had less water holding capacity and cooking loss as the proportion of MDCM increased.

  • PDF

Studies on the Preservation of Raw Beef by Gamma Radiation (감마선 조사에 의한 우육의 저장에 관한 연구)

  • Kim, Yun-Jin;Park, Yong-Kun;Kong, Un-Young
    • Korean Journal of Food Science and Technology
    • /
    • v.4 no.2
    • /
    • pp.95-99
    • /
    • 1972
  • Studies were made to investigate the influence of vacuum packing after irradiating mean doses of gamma ray at freezing temperature $(-20^{\circ}C)$ on the keeping quality and color of raw beef. Fresh round steaks were packaged anaerobically in aluminum foil, and irradiated with 0.25 and 0.5 Mrad followed by storage at $5^{\circ}C$. The shelf life of beef irradiated with 0.5 Mrad could be extended about 10 days longer than unirradiated, and the off-odors was not developed. The discoloration by irradiation was shown, but soon reverted to about 90 percentage myoglobin in 20 hours.

  • PDF

A Study of the Retention Behavior of Proteins in High-Performance Liquid Chromatography(Ⅰ): The Effect of Solvent and Temperature on Retention Behavior of Proteins in Reversed-Phase Chromatography

  • Dai Woon Lee;Byung Yun Cho
    • Bulletin of the Korean Chemical Society
    • /
    • v.14 no.4
    • /
    • pp.510-514
    • /
    • 1993
  • The retention behavior of proteins was investigated by using reversed-phase chromatography (RPC), comparing to the retention behavior of small molecules in RPC. The evaluation was carried out on a SynChropak RP-P($C_{18}$) column with 0.1% aq. TFA-organic solvent modifier such as acetonitrile, isopropanol, and ethanol. The Z value (the number of solvent molecules required to displace the solute from the surface) was a general index for the characterization of protein retention as a function of organic concentration over a range of temperature between 5 and 70$^{\circ}C$. Van't Hoff plots provided the basis for evaluating the enthalpic and entropic changes associated with the interaction between protein and the stationary phase. Z values did not change significantly at the range of temperature showing the consistent ${\Delta}H^{\circ}$ and ${\Delta}S^{\circ}$ values. From these investigation, it was concluded that the retention behavior of proteins in RPC was able to be predicted by the retention parameters applied to small molecules. Furthermore, myoglobin and hemoglobin in RPC as stated above showed a similar retention behavior regardless of their molecular weights.

Level Optimization of Beet Powder and Caramel Color for Beef Color Simulation in Meat Analogs before and after Cooking

  • Seonmin Lee;Kyung Jo;Seul-Ki-Chan Jeong;Yun-Sang Choi;Samooel Jung
    • Food Science of Animal Resources
    • /
    • v.43 no.5
    • /
    • pp.889-900
    • /
    • 2023
  • In this study, concentration levels of beet powder (BP) and caramel color (CC) were optimized to simulate beef color in meat analogs before and after cooking. The central composite design of response surface methodology (RSM) was used to set the levels of BP and CC, and the CIE L*, CIE a*, and CIE b* were selected as the responses for RSM. After optimization, myoglobin-free beef patties were prepared with three optimized levels of BP and CC. When raw, all the patties had the same color as natural beef; however, CIE L*, CIE a*, and CIE b* were statistically different from those of beef after cooking (p<0.05). Moreover, the use of BP and CC induced "browning" after the cooking process, with no excessive yellow color. Therefore, based on the overall desirability in the color optimization using RSM, the combination of BP (1.32%) and CC (1.08%) with the highest overall desirability can be used to simulate the color change of beef in meat analogs.

Effects of cold water immersion and compression garment use after eccentric exercise on recovery

  • Maruyama, Tatsuhiro;Mizuno, Sahiro;Goto, Kazushige
    • Korean Journal of Exercise Nutrition
    • /
    • v.23 no.1
    • /
    • pp.48-54
    • /
    • 2019
  • [Purpose] The combined effect of different types of post-exercise treatment has not been fully explored. We investigated the effect of combined cold water immersion (CWI) and compression garment (CG) use after maximal eccentric exercise on maximal muscle strength, indirect muscle damage markers in the blood, muscle thickness, and muscle soreness score 24 h after exercise. [Methods] Ten men performed two trials (CWI + CG and CON) in random order. In the CWI + CG trial, the subjects performed 15 min of CWI (15℃), followed by wearing of a lower-body CG for 24 h after exercise. In the CON trial, there was no post-exercise treatment. The exercise consisted of 6 × 10 maximal isokinetic (60°·s-1) eccentric knee extensions using one lower limb. The maximal voluntary contraction (MVC) and maximal isokinetic (60°·s-1) strength during knee extension, as well as the indirect muscle damage markers, were evaluated before exercise and 24 h after exercise. [Results] The maximal muscle strength decreased in both trials (p < 0.001), with no difference between them. The exercise-induced elevation in the myoglobin concentration tended to be lower in the CWI + CG trial than in the CON trial (p = 0.060). The difference in the MVC, maximal isokinetic strength, muscle thickness, and muscle soreness score between the trials was not significant. [Conclusion] CWI followed by wearing of a CG after maximal eccentric exercise tended to attenuate the exercise-induced elevation of indirect muscle damage markers in the blood.