• Title/Summary/Keyword: Metmyoglobin

Search Result 58, Processing Time 0.019 seconds

Effects of Supercritical CO2 Treatment on Color, Lipid Oxidation, Heme Iron, Non-Heme Iron and Metmyoglobin Contents in Ground Pork

  • Shirong Huang;Min Tang;Fenfen Chen;Shengnan Zhao;Dongfang Chen
    • Food Science of Animal Resources
    • /
    • v.44 no.2
    • /
    • pp.408-429
    • /
    • 2024
  • The color, lipid oxidation, heme iron (HI) and non-heme iron (NHI) contents, metmyoglobin content and Soret band of myoglobin of ground pork subjected to supercritical CO2 treatment under different conditions, or to heat treatment (40℃, 2 h) and subsequent storage at 4℃ were evaluated during 9-day period. Supercritical CO2 treatment significantly increased CIE L* and CIE b* values of ground pork during subsequent storage, while the HI content was slightly affected. In general, CIE a* value and metmyoglobin content were decreased. Supercritical CO2 treatment for 2 h could increase the thiobarbituric acid-reactive substances (TBARS) value, while treatment for 1 h or less had no effect. The NHI content could be increased only after treatment at above 40℃ or 17.2 MPa for 2 h. The Soret band of myoglobin was shifted to longer wavelength. Increasing treatment temperature from 35℃ to 45℃ could increase CIE L*, CIE a*, CIE b* and TBARS values, HI and NHI contents of the ground pork, while decreasing metmyoglobin content. As the treatment pressure increased from 13.8 MPa to 20.7 MPa, CIE b* and TBARS values were decreased, while the NHI and metmyoglobin contents were increased. However, the other parameters were unchanged. Extending exposure time from 0.5 h to 2 h could increase CIE L*, CIE b* and TBARS values, HI contents, while decreasing CIE a* value and metmyoglobin content. Correlation analysis showed that the TBARS value was significantly and negatively correlated with the HI content or metmyoglobin content in samples treated at 40℃ or above for 2 h.

Analysis of Oxy- and Metmyoglobin in Beef Chuck by Absorption Spectrophotometer and Hunter-Lab (Hunter-Lab와 분광광도계(分光光度計)에 의한 쇠고기의 Oxy-와 Metmyoglobin의 분석(分析))

  • Yeo, Young Keun;Park, Choon Ran
    • Current Research on Agriculture and Life Sciences
    • /
    • v.1
    • /
    • pp.165-167
    • /
    • 1983
  • Oxy - and metmyoglobin concentrations in beef chuck were measured by Hunter-Lab and spectrophotometer. The values of oxymyoglobin by Hunter-Lab got 34.03, 10.40, and 6.50 as average in L, a, and b while the CIE color primaries were 13.33, 11.58, and 9.94 in X, Y, and Z, respectively. The metmyoglobin values recorded 39.10, 13.20, and 10.13 in L, a, and b, of which values were converted to 17.88, 15.29, and 11.40 in X, Y, and Z of the CIE primaries. Absorption spectrum of oxymyoglobin showed 2 peaks which were 0.79 and 0.83 pf extinction coefficient with 530 and 570nm in wavelengh, and that of metmyoglobin appeared on an irregular curve with a summit of 0.58 and 500 in extinction coeffcient ($cm^2$/mg) and wavelength(nm) each.

  • PDF

Effect of Slaughter Age on Beef Color Stability during Display of Four Muscles from Japanese Black Steers

  • Muramoto, T.;Shibata, M.;Nakanishi, N.
    • Asian-Australasian Journal of Animal Sciences
    • /
    • v.16 no.9
    • /
    • pp.1364-1368
    • /
    • 2003
  • Effect of slaughter age (24, 28 and 38 months of age) on beef color stability during display of m. serratus ventralis, m. psoas major, m. semitendinosus and m. longissimus thoracis from Japanese Black steers was studied. Steak samples from muscles were over-wrapped with PVC film and displayed under fluorescent lights at $4^{\circ}C$ for 12 days. Percentages of metmyoglobin of steak samples were determined at days 0, 3, 6, 9 and 12. The percentage of metmyoglobin of m. psoas major at day 3 of display in the 24 months group was lower (p<0.05) than that in the 38 months group. The percentage of metmyoglobin of m. semitendinosus at day 6 of display in the 38 months group was higher (p<0.05) than that in the other groups. The percentage of metmyoglobin of m. longissimus thoracis at day 3 of display in the 24 months group was lower (p<0.01) than that in the other groups. The percentage of metmyoglobin of m. longissimus thoracis at day 6 (p<0.01), 9 (p<0.01) and 12 (p<0.05) of display in the 38 months group were higher than those in the other groups. Crude fat concentration in m. longissimus thoracis increased (p<0.05) after 28 months of age. $\alpha$-Tocopherol concentration in m. serratus ventralis in the 38 months group was higher (p<0.001) than that in the other groups. In m. psoas major the $\alpha$-tocopherol concentration in the 38 months group was higher (p<0.05) than that in the 24 months group. The $\alpha$-tocopherol concentration in m. longissimus thoracis increased (p<0.001) with age. These results suggested that in spite of increase in both the crude fat and the $\alpha$-tocopherol concentrations in m. longissimus thoracis, the beef color stability during display became short with age.

Effects of Gamma Irradiation on Pigments of Beef (감마선 조사가 한우육의 색소에 미치는 영향)

  • Yook, Hong-Sun;Lee, Ju-Woon;Lee, Kyong-Haeng;Kim, Sung;Byun, Myung-Woo
    • Korean Journal of Food Science and Technology
    • /
    • v.30 no.5
    • /
    • pp.1184-1188
    • /
    • 1998
  • Effects of gamma irradiation on pigments of beef was investigated by determination of the Hunter's color values and pigments such as myoglobin, metmyoglobin and oxymyoglobin after gamma irradiation up to 5 kGy in air or vacuum package for 7 days. 'L' and 'b' values increased but 'a' value decreased with the elapse of the storage period. But, 'L', 'a' and 'b' values of irradiated beef were lower than non-irradiated beef. Myoglobin decreased but oxymyoglobin and metmyoglobin increased with the elapse of the storage period. Myoglobin decreased but oxymyoglobin and metmyoglobin increased with gamma irradiation up to 5 kGy. In regard to packaging methods, vacuum package did not affect pigment of the beef as did air package.

  • PDF

Relationships between Muscle α-Tocopherol Concentrations and Metmyoglobin Percentages during Display of Six Muscles of Japanese Black Steers

  • Muramoto, T.;Shibata, M.;Nakanishi, N.
    • Asian-Australasian Journal of Animal Sciences
    • /
    • v.17 no.7
    • /
    • pp.1014-1018
    • /
    • 2004
  • Relationships between muscle $\alpha$-tocopherol oncentrations and metmyoglobin percentages during display of six muscles, m. serratus ventralis (SV), m. psoas major (PM), m. gluteus medius (GM), m. semimembranosus (SM), m. semitendinosus (ST) and m. longissimus lumborum (LL), of Japanese Black steers slaughtered at 28 months of age were studied. Steers were supplemented with 0, 2,000 and 4,000 mg $\alpha$-tocopheryl acetate/head/day for 28 days prior to slaughter in the VE 0, the VE 2,000 and the VE 4,000 groups, respectively. $\alpha$-Tocopherol concentrations in PM, GM, SM, ST and LL of the VE 2,000 and the VE 4,000 groups were significantly (p<0.05) higher than those of the VE 0 group. There were no significant (p>0.05) differences in $\alpha$-tocopherol concentrations in all muscles between the VE 2,000 group and the VE 4,000 group. The muscle $\alpha$-tocopherol concentrations ($\ell$/g meat) which can retard metmyoglobin formation in muscles were estimated to be 5.3 for SV, 4.5 for PM, 4.2 for GM, 4.0 for SM, 3.6 for ST and 3.5 for LL. The equation to predict color-shelf-life of each muscle from the $\alpha$-tocopherol concentration in each muscle could be obtained.

Retail Distribution Temperature and Quality Status of Fried-Frozen Korean Meat Ball Products (조리냉동 완자제품의 유통온도 및 품질 현황)

  • Yun, Sung-Hee;Yoon, Jae-Young;Lee, Su-Rae
    • Korean Journal of Food Science and Technology
    • /
    • v.28 no.4
    • /
    • pp.657-662
    • /
    • 1996
  • In order to investigate the quality status of fried-frozen Korean meat ball products during retail distribution, VBN value, TBA value, pH and metmyoglobin ratio were determined for 117 samples collected in Seoul area during the period of May to September, 1995. Most samples maintained relatively good quality, but one sample of a company showed $32.5mg%$ of VBN value and 0.65mg/kg of TBA value which indicate the early stage of spoilage. Correlation coefficient between metmyoglobin ratio and TBA value was highly significant. Samples closer to shelf-life limit tended to show higher VBN value, TBA value, metmyoglobin ratio and pH. Out of the surveyed samples, 35% were on retail shelves of temperature above $-14^{\circ}C$, while only 18% were being sold at temperature below $-18^{\circ}C$. It is concluded that prepared frozen foods should be stored at the recommended temperature of $-18^{\circ}C$.

  • PDF

QUICK DETERMINATION OF MEAT COLOR, METMYOGLOBIN FORMATION AND LIPID OXIDATION IN BEEF, PORK AND CHICKEN BY NEAR-INFRARED SPECTROSCOPY

  • Mitsumoto, Mitsuru;Sasaki, Keisuke;Murakami, Hitoshi
    • Proceedings of the Korean Society of Near Infrared Spectroscopy Conference
    • /
    • 2001.06a
    • /
    • pp.1259-1259
    • /
    • 2001
  • Meat becomes brown and rancid during storage in the refrigerator and display in the case. Color changes, metmyoglobin formation and lipid oxidation are the important problems in the transportation / distribution of meat and retail display. The freshness of meat is determined by the sense of vision and smell. Since conventional method determining lipid oxidation is time consuming and destructive (it needs to homogenize meat with reagents, filtrate, time for reaction and read optical density using spectroscopy), more rapid and nondestructive technical tools are desired. The objective of this work was to evaluate near-infrared spectroscopy as an analytical tool for determining meat color, metmyoglobin formation and lipid oxidation. in beef, pork and chicken. Semitendinosus and longissimus thoracis muscles from six beef steers, biceps femoris and longissimus thoracis muscles from twelve LWD crossbred pigs, and superficial pectoral muscles from twenty-four broilers were used. About a 5-cm diameter and 1-cm thick sample (20.0g) was cut from the muscle and placed on plastic foam, over-wrapped with PVC film, and displayed under flourescent lights at 4 degrees C. during 10 days for beef and pork or 4 days for chicken. The spectra was measured by NIR systems Model 5500 Spectrophotometer using fiber optic scan at range of 400 - 1100 nm. Data were recorded at 2 nm intervals and 10 scans / 10 sec were averaged for every sample. Data obtained were saved as log 1/Re, where Re is the reflectance energy, and then mathematically transformed to second derivatives to reduce effects of differences in particle size. $L^{*}$, $a^{*}$ and $b^{*}$, and metmyoglobin formation were determined by conventional spectrophotometer using the integrating sphere unit. 2-Thiobarbituric acid reactive substances (TBARS) were measured for lipid oxidation. A multiple linear regression was used to find the equation which would best fit the data. The number of wavelengths used in the equation was selected based on the fewer number compared to the increasing multiple correlation and Decreasing standard error. (omitted)

  • PDF

Lipid Oxidation in Roasted Fish Meat -IV. Changes in Heme Compounds in Roasted and/or Reheated White Muscled fishes- (어육의 배소에 의한 지질산화에 관한 연구 -IV. 백색육어의 배소 및 재가열에 의한 heme 화합물의 변화-)

  • Cho Ho Sung
    • Korean Journal of Fisheries and Aquatic Sciences
    • /
    • v.35 no.2
    • /
    • pp.162-165
    • /
    • 2002
  • To determine changes of heme compounds on lipid oxidation during repeat heating in white muscled fish (yellowfin sole and yellow croaker), myoglobin, metmyoglobin, total iron, nonheme iron and heme iron contents were analysed. Myoglobin content was decreased in the step of repeat heating. Especially, it was decreased the most rapidly roasted at 180$^{\circ}C$ for 20 min in fillet samples. The skinless fillet roasted at the lower temperature resulted in the higher level of metmyoglobin associated with the reduced myoglobin. Regardless of roasted temperature and time, total iron content was not change in contrast of raw meat throughout processing. Nonheme iron content was increased, but heme iron content was decreased during roasted, heated and reheated.

Comparison of Beef Color Stability during Display of Two Muscles between Japanese Shorthorn Steers and Japanese Black Steers

  • Muramoto, T.;Higashiyama, M.;Kondo, T.
    • Asian-Australasian Journal of Animal Sciences
    • /
    • v.17 no.9
    • /
    • pp.1303-1308
    • /
    • 2004
  • The beef color stability during display of two muscles, m. longissimus thoracis and m. semitendinosus, of Japanese Shorthorn steers (n=14) was compared with that of Japanese Black steers (n=14). The beef color of each carcass was evaluated according to the Japanese Grading Standards at 24 h post mortem. Steak samples from muscles were over-wrapped with PVC film and displayed under fluorescent lights at $4^{\circ}C$ for 9 days. Metmyoglobin percentages of steak samples were determined at days 0, 3, 6 and 9. The overall grade of beef color of the carcasses of Japanese Shorthorn steers was significantly (p<0.05) lower than that of Japanese Black steers. The metmyoglobin percentages during the display of two muscles of Japanese Shorthorn steers were significantly (p<0.05) lower than those of Japanese Black steers. These results suggested that though beef color evaluation of the carcasses of Japanese Shorthorn steers was lower than that of Japanese Black steers, the beef color stability during the display of the muscle of Japanese Shorthorn steers was higher than that of Japanese Black steers.

Comparision of the Pressure Denaturation of Metmyoglobin in $H_2O$ and $D_2O$ ($H_2O$$D_2O$ 에서 메트미오글로빈의 압력에 의한 변성의 비교 연구)

  • Keon Kim
    • Journal of the Korean Chemical Society
    • /
    • v.28 no.1
    • /
    • pp.14-19
    • /
    • 1984
  • The stability difference of metmyoglobin in $H_2O$ and $D_2O$ at pH 5.7 and pH 7.0 toward pressure denaturation is studied. Metmyoglobin is denatured in $D_2O$ at smaller pressure than in $H_2O$. The stability difference in $H_2O$ and $D_2O$ is more pronounced at pH 5.7 than at pH 7. The main reasons for the stability difference in $H_2O$ and $D_2O$are the difference in positive charge due to $H^+$and $D^+$ binding to the protein in $H_2O$ and $D_2O$, and the structural change that accompany deuteration.

  • PDF