• Proceedings of the Korea Society of Poultry Science Conference
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• 2003.11a
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• pp.129-130
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• 2003

There is growing interest for improving meat quality in chicken. Recently, the proteomics can be used as a valuable tool for identifying candidate proteins. In this study, we investigated the proteins expressed in chicken muscle for obtaining chicken muscle reference two dimensional(2D) map and identifying the proteins in muscle affecting Ginseng diet. A few candidate proteins have been currently characterizing using MALDI-TOF Mass spectrometry. Further investigations of the proteins can be used as valuable markers for selection of better quality chicken meat.

• Animal Bioscience
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• v.35 no.1
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• pp.96-104
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• 2022

Objective: Sarcoplasmic proteins include proteins that play critical roles in biological processes of living organisms. How seasons influence biological processes and meat quality of postmortem muscles through the regulation of protein phosphorylation remain to be investigated. In this study, the phosphorylation of sarcoplasmic proteins in pork longissimus muscle was investigated in four seasons. Methods: Sarcoplasmic proteins were extracted from 40 pork carcasses (10 for each season) and analyzed through ProQ Diamond staining for phosphorylation labeling and Sypro Ruby staining for total protein labeling. The pH of muscle, contents of glycogen and ATP were measured at 45 min, 3 h, and 9 h postmortem and the water (P_2b, P₂₁, and P₂₂) was measured at 3 h and 9 h. Results: A total of 21 bands were detected. Band 8 (heat shock cognate 71 kDa protein; heat shock 70 kDa protein 1B) had higher phosphorylation level in summer than that in other seasons at 45 min postmortem. The phosphorylation levels of 3 Bands were significantly different between fast and normal pH decline groups (p<0.05). The phosphorylation levels of 4 bands showed negative associations with immobilized water (P₂₁) and positive association with free water (P₂₂). Conclusion: The phosphorylation levels of sarcoplasmic proteins involved in energy metabolism and heat stress response at early postmortem time differed depending on the seasons. These proteins include heat shock protein 70, pyruvate kinase, phosphoglucomutase-1, glucose-6-phosphate isomerase, and carbonic anhydrase 3. High temperatures in summer might result in the phosphorylation of those proteins, leading to pH decline and low water holding capacity.

• Korean Journal of Food Science and Technology
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• v.19 no.3
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• pp.257-262
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• 1987

The effects of the substitution of non-meat proteins (Isolated Soy protein, Vital Wheat Gluten, Sodium Caseinate) for pork were evaluated at 0, 10, 20 and 30% levels of pork weight in the restructured product. The increase of the substitution level led to a significant increase in pH but a decrease in cooking loss, whereas it brought only a slight negative effect on color of products. TBA values for all treatments containing non-meat proteins were lower than or similar to the value for control Also, increased levels of non-meat proteins improved or did not affect functional properties of products. Alt three non-meat proteins appeared to be acceptable in terms of physico-chemical and sensory properties up to 20% of the replacement with pork in the restructured product.

• Proceedings of the Korean Society for Food Science of Animal Resources Conference
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• 2004.10a
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• pp.218-222
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• 2004

Low-fat (< 3%)/salt(< 1%) sausages were manufactured with two levels (1, 2%) of milk proteins(whey protein and sodium caseinate) to compensate for the textural problems due to reduced fat and salt(%). The addition of two levels of milk proteins into these meat products did not affect the most physicochemical and textural properties. As compared to regular-fat counterpart, higher expressible moisture of low-fat/salt sausages were observed. In addition, low-fat/salt sausages containing more than 2% of milk proteins reduced the textural hardness and gumminess, resulting in significantly lower these values, as compared to regular-fat counterparts. These results indicated that the low-fat/salt sausages were successfully manufactured with the addition of these milk proteins at the lower than 1% to improve the textural difference, however further research will be performed to improve the water holding capacity in these products.

• Journal of Nutrition and Health
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• v.10 no.2
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• pp.27-34
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• 1977

The present study was carried out to evaluate the nutritional quality of rabbit meat protein. The composition of amino acids contained in rabbit meat was compared with those of other animal meats such as beef, pork and chicken. Also included in this study was the question whether the cooking and storage conditions affect the amino acid composition and the pepsindigestibility of rabbit meat protein. The results are summarized as follows: 1. The large variation observed from sample to sample of EAA (essential amino acid) composition in rabbit meat was found to be an interesting but peculiar property of rabbit meat protein. The most limiting amino acid of rabbit meat protein was phenylalanine, whereas methionine was the first limiting amino acid of both beef and pork proteins. Chemical scores of various meat proteins were 68, 65, 66, and 74 for rabbit meat, beef, pork, and chicken respectively. 2. In pan roasting, the EAA damaged most by heat was methionine (15%). When cooked after two months of frozen storage, lysine decreased most. 3. Higher pepsin digestibility was obtained by cooking rabbit meat after seasoned in alcohol, ginger juice, and other spices compared with various other cooking conditions without seasoning. The pepsin digestibility value was even higher for the seasoned meat than for the raw meat. 4. Among various meats tested the rabbit meat showed the lowest pepsin digestibility. 5. A simple measurement of released methionine could be used to determine relative digestibility instead of measuring $NH_2-N$ content after pepsin digestion. From all the results obtained in this study it can be concluded that rabbit meat is a good Protein food item when used fresh and stored properly to prevent rancidity problems. It is suggested to study further the peroxidation effect of unsaturated fatty acids on protein quality. This study was supported by the Ministry of Science and Technology in Korea.

• Food Science of Animal Resources
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• v.40 no.1
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• pp.1-10
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• 2020

Various processing methods have a great impact on the physiochemical and nutritional properties of meat that are of health concern. Hence, the postmortem processing of meat by different methods is likely to intensify the potential effects on protein oxidation. The influence of meat protein oxidation on the modulation of the systemic redox status and underlying mechanism is well known. However, the effects of processed meat proteins isolated from different sources on gut microbiota, oxidative stress biomarkers, and metabolomic markers associated with metabolic syndromes are of growing interest. The application of advanced methodological approaches based on OMICS, and mass spectrometric technologies has enabled to better understand the molecular basis of the effect of processed meat oxidation on human health and the aging process. Animal studies indicate the involvement of dietary proteins isolated from different sources on health disorders, which emphasizes the impact of processed meat protein on the richness of bacterial taxa such as (Mucispirillum, Oscillibacter), accompanied by increased expression of lipogenic genes. This review explores the most recent evidences on meat processing techniques, meat protein oxidation, underlying mechanisms, and their potential effects on nutritional value, gut microbiota composition and possible implications on human health.

• Korean Journal of Food Science and Technology
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• v.20 no.1
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• pp.34-39
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• 1988

The possibility of using sodium dodecylsulfate-polyacrylamide gel electrophoresis was studied to detect specific proteins and their content in meat products such as beef, pork, fish, soybean, fish paste, ham and fish sausage. Many complicated bands were observed in the total protein fractions of the tested samples. The number of protein bands in the low salt-soluble protein fractions was considerably lesser and showed more specific bands in comparison with total protein fractions. Actone-insoluble fractions of non-meat proteins showed different patterns from meat proteins. A heating procedure seemed to be a cause for the diminished number and quantity of resolved protein bands in sausages. The results suggest that the discgel electrophoresis can be used to detect specific proteins and their content in protein foods, if a selective extraction method is emplyed.

• Food Science of Animal Resources
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• v.41 no.6
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• pp.997-1011
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• 2021

The processing characteristics of freeze-dried pork powder as raw meat for comminuted meat products were compared with those of freeze-thawed pork. The tertiary structural properties, oxidation, and solubility of proteins in the freeze-dried pork powder were investigated. In addition, the properties of the emulsion gels manufactured with freeze-dried pork powder (GFD) and freeze-thawed pork (GFT) at 1.5% and 2.0% NaCl were evaluated. The surface hydrophobicity and intrinsic tryptophan fluorescence intensity of myofibrillar proteins between the freeze-dried pork powder and freeze-thawed pork were similar. However, freeze-dried pork powder had higher carbonyl compounds and lower solubility of sarcoplasmic and myofibrillar proteins than freeze-thawed pork (p<0.05). GFD had higher cooking loss than GFT in 2.0% NaCl, and lower hardness and a^* value of GFD were observed regardless of NaCl level (p<0.05). Moreover, GFD had higher malondialdehyde content than GFT at the two NaCl concentrations (p<0.05). Therefore, our study demonstrated that freeze-dried pork powder has lower functional properties than freeze-thawed pork as raw meat for comminuted meat products.

• Korean Journal of Food Science and Technology
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• v.29 no.6
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• pp.1191-1195
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• 1997

This study was conducted to investigate the proteolytic properties of saewoojeot (salted and fermented shrimp) on various meat proteins. NaCl content was decreased less than 2% by electrodialysis. As electrodialysis time was passed, the protease activity was increased. The proteolytic activity of crude protease on muscle proteins of beef, pork, chicken was analyzed by SDS-PAGE. Crude enzyme easily degradated both heat-denatured and native meat proteins. Protein degradation was rapidly occurred within 5 min and most all myofibrilar protein was disappeared. Heat-denatured chicken meat (100%) was most easily degraded than heat-denatured pork meat (47%) and beef meat (31%).

• Food Science of Animal Resources
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• v.42 no.2
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• pp.266-279
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• 2022

This study was conducted to evaluate the proteolysis trends and change in meat quality during 10 days of cold storage in duck M. pectoralis major (PM) and M. iliotibialis (IL). Duck IL had a higher pH and greater degree of lightness but lower cooking loss than PM (p<0.05). During the 10-day cold storage, the pH value of PM declined significantly (p<0.05), while the meat quality traits of IL were not affected by cold storage (p>0.05). In PM, the redness increased from day 1 to day 5, while cooking loss was lower on day 10 compared to day 5 (p<0.05). There were no significant differences in the activities of cathepsin B and proteasome 20S during cold storage (p>0.05). The activity of calpains declined gradually during 10 days of storage (p<0.05), and the activity of calpains in PM was higher than that in IL (p<0.05). A total of 5,155 peptides were detected and derived from 34 proteins of duck PM muscle, whereas 4,222 peptides derived from 32 proteins were detected from duck IL muscle. Duck PM muscle was composed only of fast type of muscle fiber, whereas IL muscle was composed of both slow and fast types. The proteins responsible for glycolysis or myofibrillar proteins were closely related to changes in meat color or water-holding capacity during cold storage. These results suggest that changes in meat quality characteristics during cold storage are closely related to protein degradation, which is also related to the distribution of muscle fiber types.