Wangang Zhang

Biochemistry of postmortem muscle - lessons on mechanisms of meat tenderization.

It is certain that meat tenderness is a highly valued consumer trait and thus definition of the multiple processes that influence meat tenderness will provide clues toward improving meat quality and value. The natural process by which meat becomes tender is complex. Tenderness development is dependent on the architecture and the integrity of the skeletal muscle cell and on events that modify those proteins and their interaction. Specifically protein degradation and protein oxidation have been identified as processes that modify proteins as well as the tenderness of meat. The intracellular environment is a major factor that controls these events. Ultimately, the interplay between these events determines the rate and extent of tenderization. Given the intricacy of the structure of the muscle cell, coupled with the complexity of the regulation of protein modification and the ever-changing intracellular environment it is not surprising that this area of research is a very dynamic field. Just as the overall integrity and function of muscle cells does not depend on a single protein, but rather on the coordinated interaction of several proteins, the structural weakening of muscle cells during postmortem aging also must not depend on the degradation of a single myofibrillar or other cytoskeletal protein. The proteins mentioned in this review are located in different regions of the muscle cell, and most have been implicated in some manner as being important in maintaining the structure and function of the muscle cell. Oxidation of myosin heavy chain, a predominant protein in the myofibril, is known to promote aggregation and toughening of meat. Degradation of proteins such as desmin, filamin, dystrophin, and talin (all located at the periphery of the Z-line) may disrupt the lateral register and integrity of the myofibril themselves as well as the attachments of the peripheral layer of myofibril to the sarcolemma. Degradation of the proteins within the myofibril that are associated with the thick and thin filaments may allow lateral movement or breaks to occur within the sarcomeres of postmortem aged samples. Titin, nebulin, and troponin-T, by their ability to directly interact with, or modulate the interaction between, major proteins of the thick and thin filaments and (or) the Z-line, play key roles in muscle cell integrity. Disruption of these proteins, especially titin and nebulin, could initiate further physicochemical and structural changes that result in myofibril fragmentation and loss of muscle cell integrity, and ultimately in tenderization of the muscle. In order to make real progress in this area, the scientific community must have a global appreciation of how both the structural proteins and the key proteases are influenced by the vast changes that occur during the conversion of muscle to meat.

Improving functional value of meat products

In recent years, much attention has been paid to develop meat and meat products with physiological functions to promote health conditions and prevent the risk of diseases. This review focuses on strategies to improve the functional value of meat and meat products. Value improvement can be realized by adding functional compounds including conjugated linoneleic acid, vitamin E, n3 fatty acids and selenium in animal diets to improve animal production, carcass composition and fresh meat quality. In addition, functional ingredients such as vegetable proteins, dietary fibers, herbs and spices, and lactic acid bacteria can be directly incorporated into meat products during processing to improve their functional value for consumers. Functional compounds, especially peptides, can also be generated from meat and meat products during processing such as fermentation, curing and aging, and enzymatic hydrolysis. This review further discusses the current status, consumer acceptance, and market for functional foods from the global viewpoints. Future prospects for functional meat and meat products are also discussed.

Protein Oxidation: Basic Principles and Implications for Meat Quality

The involvement of oxidized proteins to the development of biological diseases has been studied for a few decades, but the effects and the mechanisms of protein oxidation in food systems are largely unknown. Protein oxidation is defined as the covalent modification of a protein induced either by the direct reactions with reactive oxygen species (ROS) or indirect reactions with secondary by-products of oxidative stress. ROS can cause oxidation in both amino acid side chains and protein backbones, resulting in protein fragmentation or protein–protein cross-linkages. Although all amino acids can be modified by ROS, cysteine, and methionine that are the most susceptible to oxidative changes due to high reaction susceptibility of the sulfur group in those amino acids. Oxidative modifications of proteins can change their physical and chemical properties, including conformation, structure, solubility, susceptibility to proteolysis, and enzyme activities. These modifications can be involved in the regulation of fresh meat quality and influence the processing properties of meat products. Oxidative stress occurs when the formation of oxidants exceeds the ability of antioxidant systems to remove the ROS in organisms. Increased levels of protein oxidation have been associated with various biological consequences, including diseases and aging, in humans and other animal species. The basic principles and products of protein oxidation and the implications of protein oxidation in food systems, especially in meat, are discussed in this review.

Contribution of postmortem changes of integrin, desmin and μ-calpain to variation in water holding capacity of pork

The purpose of this study was to examine the relationship between integrin, desmin, μ-calpain and water holding capacity in fresh pork. High levels of intact integrin at one day postmortem were negatively correlated with day 1 (P<0.05) and days 1-5 (cumulative) drip loss (P<0.05). High levels of intact integrin at five days postmortem were negatively correlated with days 1-7 (cumulative) purge loss (P<0.05). Intensity of intact desmin at one day postmortem was positively correlated with days 1-7 purge loss (P<0.01). There were positive correlations between intensity of intact desmin at day 7 and day 1 (P<0.01), days 1-5 drip loss (P<0.01) and days 1-7 purge loss (P<0.05). Autolysis of μ-calpain was associated with the degradation of desmin and drip or purge loss postmortem. Our results indicate that low levels of degradation of integrin and high levels of desmin degradation were associated with low drip loss values in fresh pork.

Consumption of Oxidized Oil Increases Oxidative Stress in Broilers and Affects the Quality of Breast Meat

A total of 120 4-week-old broiler chickens were allotted to 12 pens and fed one of three diets including control, oxidized diet (5% oxidized oil), or antioxidant-added diet (500 IU vitamin E) for 2 weeks. Blood samples were collected at the end of feeding trial, and breast muscles were sampled immediately after slaughter. Breast meats were also collected 24 h after slaughter and used for meat quality measurements. Oxidative stress in blood, lipid and protein oxidation, and sarcoplasmic reticulum Ca²(+)-ATPase (SERCA) activity of breast muscle were determined. The oxidized diet increased oxidative stress in blood and increased carbonyl content in breast meat compared with the other two dietary treatments (P < 0.05). Lipid oxidation of breast muscles with the antioxidant-supplemented diet was lower than that with the oxidized and control diet groups (P < 0.05). Meat from birds fed the oxidized diet showed higher drip loss after 1 and 3 days of storage and greater 0-1 h post-mortem pH decline (P < 0.05). Significant differences in specific SERCA activity in breast muscles from birds fed control and oxidized diets (P < 0.05) were detected. This suggested that dietary oxidized oil induced oxidative stress in live birds and increased lipid and protein oxidation in breast muscle. Decrease in SERCA activity in breast muscles due to oxidative stress in live animals accelerated post-mortem glycolysis, which sped the pH drop after slaughter and increased drip loss, indicating that oxidation of diet can cause PSE-like (pale, soft, and exudative) conditions in broiler breast muscles.

Egg Yolk Phosvitin and Functional Phosphopeptides—Review

Phosphopeptides are among the most interesting biomolecules with characteristic molecular structure and functions. They usually contain clusters of phosphoserines, which can effectively bind calcium and iron, and inhibit formation of insoluble calcium phosphates or iron complexes. Therefore, phosphopeptides can increase calcium or iron bioavailability and prevent lipid oxidation in foods. Milk protein casein has been currently used by industry to produce phosphopeptides. Egg yolk phosvitin is considered as the most phosphorylated protein found in the nature. Phosvitin from egg yolk can be much better source for producing phosphopeptides with varying sizes and functions than casein because it contains much greater number of phosphates in the molecule than casein. However, still phosvitin has not been subjected to considerable attention with regard to bioactive peptides production.

Isolation and identification of antioxidant peptides from jinhua ham.

The antioxidant activities of the peptides extracted from Jinhua ham were evaluated on the basis of hydroxyl radical scavenging activity, DPPH radical scavenging activity, and Fe(2+) chelating ability. The peptide extracts exhibited great hydroxyl radical scavenging activity and DPPH radical scavenging activity as well as Fe(2+) chelating ability at the concentration of 1 mg/mL, which suggested the presence of peptides with antioxidant activity. The peptides were separated using size exclusion chromatography and reversed-phase HPLC. The fraction with highest DPPH radical scavenging activity was further purified and identified using liquid chromatography tandem matrix-assisted laser desorption/ionization time-of-flight/time-of-flight mass spectrometry (HPLC-MALDI-TOF/TOF-MS). The sequence of the antioxidant peptide was identified as Gly-Lys-Phe-Asn-Val. The assessment of fractions indicated that the hydrophobic fractions contributed more to free radical scavenging activities than the hydrophilic peptides. It was concluded that natural peptides extracted and isolated from the Jinhua ham by several chromatographic techniques have antioxidant activities.

Effect of multiple freeze-thaw cycles on the quality of chicken breast meat.

The objective of this study was to determine the effects of repeated freeze-thaw cycles (0-6) on any physico-chemical changes and lipid and protein oxidation in chicken breast. The results showed that meat colour, a(∗) (redness) and b(∗) (yellowness) values decreased while L(∗) values (lightness) increased with increasing cycle numbers. Increasing freeze-thaw cycles resulted in a greater degree of lipid and protein oxidation, as evidenced by higher contents of malondialdehyde and carbonyl compounds, and lower contents of sulfhydryl groups. Differential scanning calorimetry profiles and SDS-PAGE banding patterns of myofibrillar proteins indicated slight denaturation of myosin and actin with repeated freeze-thaw cycles. The structural changes occurring in proteins caused by oxidation directly affected the ability of muscles to retain water, as confirmed by the nuclear magnetic resonance relaxometery profile. In conclusion, multiple freeze-thaw cycles increased lipid and protein oxidation and decreased water holding capacity and colour stability of broiler chicken breast.

China's meat industry revolution: Challenges and opportunities for the future

From a very limited ration of meat only for urban citizens to the worlds largest meat-producing country, from a handful of processing facilities in major cities to thousands of modern meat packing and processing plants throughout the country, the Chinese meat industry has gone through drastic revolutionary changes particularly in the last three decades. Before the national economic reform in the late 1970s, meat production in China was extremely limited; hence, meat was rationed, treated as a highly precious food, and was highly valued. However, new processing technology developments, as related to meat animal production, slaughtering, processing, and distribution have transformed the inefficient Chinese meat industry that prepared only a handful of traditional products into a vast enterprise today that is manufacturing a huge variety of fresh and further processed items enjoyed by the average Chinese household. Along with this evolution, there has been the emergence of mega-scale meat companies and rapid advances in meat science and technology that address many aspects of meat. This review will highlight some milestone changes of the Chinese meat industry and discuss challenges and opportunities ahead in the global market for China.

Effects of diet, packaging, and irradiation on protein oxidation, lipid oxidation, and color of raw broiler thigh meat during refrigerated storage

This study was designed to evaluate the effects of dietary treatment, packaging, and irradiation singly or in combination on the oxidative stability of broiler chicken thigh meat. A total of 120 four-week-old chickens were divided into 12 pens (10 birds/pen), and 4 pens of broilers were randomly assigned to a control oxidized diet (5% oxidized oil) or an antioxidant-added diet [500 IU of vitamin E + 200 mg/kg of butylated hydroxyanisole (BHA)] and fed for 2 wk. After slaughter, thigh meats were separated, ground, packaged in either oxygen-permeable or oxygen-impermeable vacuum bags, and irradiated at 0 or 3 kGy. Lipid oxidation (TBA-reactive substances), protein oxidation (carbonyl), and color of the meat were measured at 1, 4, and 7 d of refrigerated storage. The lipid and protein oxidation of thigh meats from birds fed the diet supplemented with antioxidants (vitamin E + BHA) was significantly lower than the lipid and protein oxidation of birds fed the control diet, whereas the lipid and protein oxidation of broilers fed the oxidized oil diet was higher than that of birds fed the control diet. Vacuum packaging slowed, but irradiation accelerated, the lipid and protein oxidation of thigh meat during storage. Dietary antioxidants (vitamin E + BHA) and irradiation treatments showed a stronger effect on lipid oxidation than on protein oxidation. A significant correlation between lipid and protein oxidation in meat was found during storage. Dietary supplementation of vitamin E + BHA and the irradiation treatment increased the lightness and redness of thigh meat, respectively. It is suggested that appropriate use of dietary antioxidants in combination with packaging could be effective in minimizing oxidative changes in irradiated raw chicken thigh meat.