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Animal Frontiers - AMSA Perspectives

Meat: the edible flesh from mammals only or does it include poultry, fish, and seafood?


This article in

  1. Vol. 7 No. 4, p. 12-18
    Published: September 21, 2017

    * Corresponding author(s):
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  1. Xue Zhang,
  2. Casey M. Owens and
  3. M. Wes Schilling *
  1.  Department of Food Science, Nutrition, and Health Promotion, Mississippi State University, Mississippi State, MS
     Department of Poultry Science, University of Arkansas, Fayetteville, AR


  • Historically, meat science research has been focused on the edible flesh from mammals. Though differences exist between edible flesh from mammals, poultry, and fish, there are also many similarities with respect to muscle fiber type, rigor mortis, and quality problems associated with these muscle foods.

  • Different entities provide variable definitions for what constitutes meat. Since many companies in the United States utilize multiple species in processed food products, there is an emphasis on including poultry in the definition of meat and meat science research. This paper does not attempt to define meat, but does discuss similarities and differences between muscle foods that may be defined as meat.

  • All types of fresh meat products are susceptible to quality defects. Muscles with higher concentrations of red fibers are susceptible to long-term stress and the production of dark, firm, and dry (DFD) meat. Muscles with greater concentrations of white fibers are susceptible to short-term stress and the production of pale, soft, and exudative (PSE) meat. In recent years, genetic selection of broilers for high breast yield has introduced white striping and woody breast meat defects that are partially attributed to both genetics and nutrition.

Definition of Meat

The definition of meat varies according to source. For example, Webster’s Dictionary defines meat as “the flesh of an animal (especially a mammal) as food” (Merriam-Webster, 2017). The American Meat Science Association defines meat as red meat (beef, pork, and lamb), poultry, fish/seafood, and meat from other managed species (AMSA, 2017). The journal Meat Science does not provide a specific definition for meat but states the following purpose of the journal: “to provide an appropriate medium for the dissemination of interdisciplinary and international knowledge on all the factors which influence the properties of meat. The journal is predominantly concerned with the flesh of mammals; however, contributions on poultry will only be considered, if they demonstrate that they would increase the overall understanding of the relationship between the nature of muscle and the quality of the meat which muscles become post mortem” (Elsevier, 2017).

Historically, the field of meat science has been associated with beef, pork, lamb, and goat. Poultry meat, seafood, and aquaculture have been considered muscle foods but have been differentiated from the edible flesh of mammals.

This paper gives a brief discussion of similarities and differences between meat from mammals and meat from poultry, seafood, and other aquatic species with respect to live muscle, muscle fiber type, rigor mortis, meat quality, and quality defects.

Muscle Foods

Animals with backbones are in the phylum Chordata and include mammals, birds, and fish as three of the five classes in this phylum. Other muscle foods such as crabs, lobster, crayfish, and shrimp are in the phylum Arthropoda, and mollusks, oysters, and clams are in the phylum Mollusca. Skeletal muscles are used to facilitate movement by applying force to bones and joints via contraction and consist of a heterogeneous population of fibers that differ in their molecular, structural, contractile, and metabolic features. Differences in fiber type influence the growth rate and postmortem characteristics such as onset of rigor mortis, pH decline, color, water-holding capacity, tenderness, and ultimately, the functional properties of meat.

Muscle Fiber Classification

Muscle fibers have been classified according to:

  1. biochemical studies on glycolytic and oxidative enzymes,

  2. histochemistry of myosin ATPases,

  3. fast- and slow-twitch muscles determined using electron microscopy, and

  4. correlation between histochemical and physiological studies of myofibers (Schiaffino and Reggiani, 2011) (Table 1).

1 Reactions of aerobic oxidative capacity; succinate dehydrogenase (SDH) activity is the reference enzyme Red Gauthier, 1969
2 Sensitivity of myofibrillar ATPase (mATPase) activity after exposure to either high or low pH Type I Brooke and Kaiser, 1970; Gorza, 1990
Type IIA
Type IIB/C
Type IIX/D
3 The Combination of oxidative SDH staining and ATPase activity beta-R, ATPase acido-stabile and oxidative Ashmore and Doerr, 1971
alpha-R, acido-labile and oxidative
alpha-W, ATPase acido-labile and glycolytic
4 The combination of histochemical stains for the oxidative enzyme NADH tetrazolium reductase and ATPase Slow-twitch oxidative (SO) Peter et al., 1972
Fast-twitch oxidative glycolytic (FOG)
Fast-twitch glycolytic (FG)
5 Myosin heavy chain isoforms MyHC I Schiaffino and Reggiani, 1996
MyHC IId/x

Isoforms of MyHC I, MyHC IIa, MyHC IIb, and MyHC IId/x correspond to Type I, Type IIA, Type IIB/C, and Type IID/X fibers, respectively (Carani et al., 2006). However, hybrid fibers can contain several MyHC isoforms simultaneously (Choi and Kim, 2009) since fibers can switch from one type to another based on the following pathway: I ↔ I/IIA ↔ IIA ↔ IIA/IIX ↔ IIX ↔ IIX/IIB ↔ IIB. The characteristics of four main types of muscle fibers are summarized in Table 2.

a. Very low mATPase activity a. Medium mATPase activity a. High mATPase activity a. Very high mATPase activity
b. Very high oxidative and very low glycolytic metabolism b. High oxidative and glycolytic metabolism b. Low oxidative and high glycolytic metabolism b. Very low oxidative and very high glycolytic metabolism
c. Very slow contraction speed c. Medium contraction speed c. Rapid contraction speed c. Very rapid contraction speed
d. Small size d. Small size d. Large size d. Very large size
e. Very dense capillary network e. Dense capillary network e. Sparse capillary network e. Sparser capillary network
f. Very high levels of intracellular myoglobin f. High levels of intracellular myoglobin f. Low levels of intracellular myoglobin f. Very low levels of intracellular myoglobin
g. Very high resistance to fatigue g. High resistance to fatigue g. Low resistance to fatigue g. Very low resistance to fatigue
h. Very high mitochondrial density h. High mitochondrial density h. Low mitochondrial density h. Very low mitochondrial density
i. Red color i. Intermediate color i. White color i. White color
Source: Gerrard and Grant, 2003; Lefaucheur, 2010.

Muscle Fiber Composition of Different Meat Species

Mammalian animals

In most mammalian animals, the four major types of muscle fibers coexist, and muscle differences are mainly due to variability in the relative concentration of Type I, IIA, IIX, and IIB fibers. There are marked differences in histochemical characteristics both between and within muscles that are influenced by genotype, sex, age, feed, management, etc. (Vestergaard et al., 2000).


Type I fibers are grouped in clusters in the center of the muscle and are immediately surrounded by IIA and IIB fibers. The deeper muscle area has a greater proportion of Type I fibers and a higher oxidative capacity compared with the outward area portion of the muscle. Porcine muscles, such as the longissimus dorsi (LD), gluteus medius, rectus femoris, biceps femoris, and semimembranosus contain a high concentration of Type IIB fibers while muscles such as the masseter, trapezius, vastus intermedius, triceps brachii, infraspinatus, and spinam, contain a greater concentration of Type I and IIA fibers (Karlsson et al., 1999). In general, porcine LD muscle contains approximately 10% Type I, 10% IIA, 25% IIX, and 55% IIB fibers (Listrat et al., 2016).


On average, bovine LD muscle contains 30% Type I, 18% IIA, and 52% IIX fibers, which is more Type I, less Type IIX, and no Type IIB fibers compared with porcine muscle. Type IIB fibers have rarely been detected in bovine muscles. Bovine limb flexor digitorum, membri thoracic muscle is mainly composed of Type I, IIA fibers and a small proportion of hybrid types, I+IIA and IIAX, but pure Type IIX fibers were not detected. The psoas major (PM) had a balanced proportion of Type I, IIA, and IIX pure fiber types, and a reduced number of hybrid fibers (Waritthitham et al., 2010).

Sheep and goats

The proportion of red, intermediate, and white fibers in ovine muscle is approximately 10–15, 31–35, and 50–55%, respectively. Type I, IIA, and total muscle fiber numbers in LD muscle were similar between lambs of different breeds, but Type IIB muscle fiber numbers in LD from Morkaraman lambs were greater than those from other breeds (Şirin et al., 2017).

Goat limb semitendinosus consists of 40% Type I, 2% Type I + IIA, 23% IIA, 21% IIAX, 14% IIX, and no Type IIB (Argüello et al., 2001). There was 21% of hybrid IIAX fiber phenotype in goat semitendinosus compared with 8% in bovine semitendinosus. The proportion of different types of muscle fibers impacts muscle mass. Sheep and goats have less white muscle fibers (Type IIX and IIB) than pigs or cattle. In analogical muscles with the same total number of fibers obtained from different animals, a greater content of white fibers results in greater muscle mass since white fibers are characterized by a larger diameter (Wieslaw and David, 2015).

Source: © rostyle



Most commercial poultry breast muscles (broilers and turkeys) typically have a higher proportion of fast-twitch, glycolytic (white) fibers than muscles from mammalian species. In broilers and turkeys, the breast meat is predominantly made up of white breast fibers, and the leg meat consists of predominantly red muscle fibers. The five distinct fiber types in chicken skeletal muscles include Type I slow-contracting “red” fibers, Type IIA and IIB fast-contracting “white” fibers, and Type IIIA and IIIB slow, tonic “intermediate” fibers. A greater concentration of Type I muscle fibers are in the soleus muscle, which is used for walking and standing. Type IIA fibers are found in muscles that are fast-moving and repetitive in action and do not fatigue as easily as Type IIB glycolytic fibers. Type IIB fibers are found primarily in the pectoral muscle and the posterior latisimus dorsi. Type IIIA and IIIB slow-tonic fibers are not found in mammals but are present in the plantaris and anterior latissimus dorsi of avian species that remain contracted much of the time since their function is to keep the wings back against the body (McKee, 2004). Duck breast has a greater content of muscle fiber Type IIA, more redness and less lightness when compared with the chicken breast to help them fly for sustained periods of time (Ali et al., 2008). One of the largest differences between muscle growth from poultry and mammals is postnatal skeletal muscle growth. Accumulation of DNA is directly proportional to skeletal muscle size. Greater than 94% of total muscle DNA accumulates postnatally in chicken while substantially less (50–90% DNA) accumulates postnatally in mammals. More information on similarities and differences between muscle accretion and growth in poultry and mammals can be found in Smith and Doumit (1999).

Source: © soleg



Most fish have 90–95% fast-twitch muscle (high glycolytic and anaerobic) that allows them to dart away from predators, whereas terrestrial herbivores, such as cows, have a large proportion of slow-twitch muscle, facilitating the sustained load bearing necessitated by their grazing lifestyle (Jackson and Ingham, 2013). The majority of fish species never cease to grow and, therefore, can increase the size and number of their muscle cells throughout their life span.

Mammalian and poultry muscle are typically heterogeneous. In fish, muscle fiber types are organized into large, homogeneous, and anatomically separate regions at the macroscopic scale as three main types of muscle: a major white muscle, a superficial red muscle (along the skin), and an intermediate pink muscle. In trout, fast fibers (similar to mammalian IIB fibers) are in the center of a cross-sectional body area, and slow fibers (similar to the mammalian Type I) are at the periphery, along with a longitudinal line under the skin. In addition to these two main fiber types, minor types, such as the intermediate type (e.g., the pink fiber type, comparable to the Type IIA) can be found in certain species or at certain stages of development. The two main types of white and red fibers have been associated with the expression of fast and slow MyHC (Lampila, 1990; Rescan et al., 2001). However, it is difficult to systematically match a MyHC isoform with a fiber type due to the presence of several MyHCs within the same fiber. In crustacean shellfish, such as shrimp, crab, and lobster, muscles are attached to the inner walls of their shells. In crabs, the majority of edible flesh comes from the legs and claws. There are two types of muscle in Crustacea, the slow, tonic fiber, and the fast phasic fiber, which are likely similar to Type IIA and Type IIB fibers, respectively (Factor, 1995).

Rigor Mortis

The development of rigor mortis depends on meat species, muscle type, carcass size and weight, slaughter, processing, and chilling conditions. Muscles throughout the carcass vary in their rates of temperature and pH decline, due to inherent metabolic differences and muscle size (Jacob and Hopkins, 2014). Rates of pH and temperature decline during rigor development are important post-mortem factors that affect meat quality in terms of color, water-holding capacity (WHC) and tenderness.

The rate of rigor onset is different for avian and mammalian species. Broiler muscle undergoes rigor development at a very rapid rate due to its relatively smaller size and younger age. Broiler meat is sufficiently tender when deboned at least within 4 to 6 h after slaughter, allowing for rigor completion. In contrast, rigor onset in beef occurs between 6 and 12 h postmortem, and beef is typically aged at least 14 d to optimize tenderness (Smith and Doumit, 1999).

The pH of live muscle is approximately 7.0 for mammals, poultry, and fish. Although the pH of all muscles declines after slaughter, the ultimate pH varies among species and among muscles within species. Poultry muscle has an ultimate pH of 5.6–6.0 for breast meat and 6.0–6.4 for thigh meat, whereas beef muscle pH ranges approximately 5.3–5.8 (Smith and Doumit, 1999). Fish muscle pH may drop to 6.1–6.5 in cod and 5.8–6.0 in large mackerel. Fish muscle contains less glycogen than mammalian muscle, which generally leads to the production of less lactic acid in fish. Within a species, white muscles have a lower ultimate pH than red muscles. For example, turkey breast and thigh meat have ultimate pH values of 5.8 and 6.2, respectively (Debut et al., 2003). Muscle pH has a large influence on product quality since it affects water-holding and textural properties of the products due to the influence of pH on protein solubility and functionality. The isoelectric point of myofibrillar proteins (myosin and actin) are approximately 5.0. The further the proteins are away from this point, the greater WHC of the myofibers and the sarcomere structure. Pork muscle undergoes a more rapid postmortem pH decline than muscle from other mammalian species because pork contains more glycolytic Type IIB fibers. Therefore, it is more likely to experience elevated temperatures during the onset phase of rigor.

Fish may begin the rigor mortis process within an hour after being killed although onset may be delayed by as much as 7 h if fish are chilled with ice as soon as they are killed and maintained in a chilled storage environment. This extends the time that fish remain fresh, since bacterial spoilage commences only after rigor mortis has passed. The resolution of rigor mortis makes the fish muscle flexible but not as elastic as before rigor mortis (Delbarre-Ladrat et al., 2006).

Meat Quality Measurements


Rapid discoloration occurs in muscles that contain greater relative proportions of Type I and Type IIA muscle fibers due to higher oxygen consumption rate and higher concentrations of myoglobin during cold storage (Jeong et al., 2009). Therefore, beef and lamb are more susceptible to color deterioration than pork, chicken, and fish. Often under retail settings, color degradation ends the product shelf life for beef and lamb, whereas chicken becomes unacceptable due to bacterial growth and fish become unacceptable due to texture degradation, bacterial growth, and/or lipid oxidation.

Red meat with a greater concentration of Type I muscles, for example the beef psoas major, contains more oxidative muscle fibers and has less color stability than meat cuts with relatively greater concentrations of Type IIX or Type IIB muscles, for example, the beef LD and semimembranosus (Jeong et al., 2009).

Poultry and fish meat have less pigmentation than meat from mammals. Poultry has less myoglobin than red meat due to more Type IIB fibers and a younger age at the time of harvest when compared with mammals. In fish, the muscle color is primarily related to the muscle fiber type composition. The red superficial lateral muscle is rich in myoglobin and exhibits a less desirable brown color, and the white muscle is almost translucent. The color of fish muscle also depends on the depth and diving habits of the fish, indicating the need for greater oxygen storage. The lateral muscle in salmon has a unique orange-red color due to the presence of a carotenoid pigment, astaxanthin. Fish myoglobin contains a cysteine residue, which is not present in mammals. Therefore, fish myoglobin can react with sulfhydryl compounds in the presence of trimethylamine oxide to cause green discoloration (Venugopal and Shahidi, 1996).

Water-holding capacity

The composition of fast-twitch glycolytic (IIB) fibers in pork muscle is related to greater lightness and less WHC (Kim et al., 2013). Therefore, excessive drip loss is prevalent in pork that contains a greater relative proportion of Type II muscle fibers compared with beef or lamb. In cattle and lambs, an increased proportion of Type I fibers is associated with improved meat WHC, juiciness, and flavor, which can be partially attributed to the high phospholipid content and high capillary density in Type I fibers (Table 2). However, the high content of polyunsaturated fatty acids in phospholipids increases the susceptibility to oxidation during storage time, which contributes to the development of rancid off-flavors. Meat flavor and juiciness are also positively correlated with intramuscular fat content and proportion of Type I fibers in the muscle (Joo et al., 2013).

Poultry thighs and drumsticks have higher cooking losses compared with breast meat. Poultry thighs and drumsticks have more Type I fibers, more fat, and more connective tissue. Meat with a greater amount of fat will have higher cooking loss because of the percentage of fat lost during cooking. Also, there is proportionately less functional protein available for water binding. Because poultry thigh and drumsticks have more oxidative type fibers, they also have more myoglobin and mitochondria. The myoglobin is a heme protein containing iron. Poultry thighs and drumsticks have a stronger flavor compared with the breast muscle, which is largely attributed to the iron content of the muscle and fat composition (McKee, 2004).


For beef, muscles with greater concentrations of non-degenerative Type II muscle are more tender than “red” or Type I fibers. Slow-twitch muscles (Type I) have been reported to contain more collagen, which binds muscle fibers, resulting in less tender meat (Joo et al., 2013). However, in cattle breeds with faster glycolytic metabolism, the most tender meat muscles are the most oxidative (Type I), which is partially explained by the higher protein turnover and associated proteolytic activity in the oxidative fibers (Picard et al., 2014). In cattle, increasing the proportion of slow-twitch Type I fibers improved tenderness. Similarly, a high content of the MyHC slow isoform (Type I) was associated with tender pork, beef, and lamb, whereas a high ratio of MyHC fast/slow isoforms (Type II) was associated with less tender meat (Hwang et al., 2010).

In general, the mean diameter of muscle fibers is negatively correlated with flesh firmness in fish. Fish red muscle contains more lipids, a larger quantity of myoglobin, more collagen, and greater glycogen content than white muscle. As tuna cooking temperature increases, the shear force of red muscle became progressively greater than that of white muscle even though the mechanical resistance of collagen decreased. In contrast, trout red muscle had less mechanical resistance than white muscle after cooking, suggesting variability among species (Xiong et al., 1999). In fresh and smoked Atlantic salmon and in fresh brown trout, firmness decreases as fiber size increased and fiber density decreased (Bugeon et al., 2003; Johnson et al., 2004).

Source: © Amy Radunz


Meat Quality Defects

Pork defects

Pale, soft, and exudative (PSE) meat.

Swine with a greater concentration of white fast-twitch Type II fibers (Type IIX and IIB) are more stress susceptible than swine with different fiber type distributions. The former has a higher concentration of lactate and subsequent rapid pH decline in the early postmortem period due to their higher glycolytic capacity, which increases the incidence of PSE pork production (Ryu and Kim, 2005). Pork that is PSE results from a rapid pH decline during rigor mortis while the muscle temperature is still high. It has increased drip loss and a lighter color when compared with normal pork. Also, pigs that are susceptible to stress have more Type II anaerobic fibers than other non-susceptible breeds (McKee, 2004).

Cold shortening.

Cold shortening results from the rapid chilling of carcasses immediately after slaughter before the glycogen in the muscle has been converted to lactic acid. Cold shortening occurs due to the inability of the sarcoplasmic reticulum to sequester Ca2+ at low temperatures (0–5°C). The inability of sarcoplasmic reticulum and mitochondria to bind Ca2+ results in calcium entering the sarcoplasm and cold shortening due to muscle contraction, leading to tough meat. Red meat is more susceptible to cold shortening than meat with predominantly white muscle fibers (Savell et al., 2005). Because white muscle fibers tend to have higher amounts of glycogen, they experience a more rapid drop in pH earlier in the rigor process. This is especially relevant with pork. For pork, because of the impact of high muscle temperatures and low pH on the development of PSE pork, a more rapid chilling process is needed to reduce the incidence of PSE meat with the recommended internal muscle temperature of 10°C at 12 h and 2–4°C at 24 h. Rapid or blast chilling is effective at reducing the incidence of PSE pork, but extreme chilling systems may cause cold shortening and toughness due to differences between the cold temperatures on the outside of the carcass (darker color) when compared with the warm muscle temperatures within the carcass (lighter color) (Choi and Oh, 2016).

Beef quality defects

Dark, firm, and dry meat (DFD).

Meat that is DFD is produced from animals that have experienced a period of sustained stress that has depleted its muscle glycogen. As a result, less lactic acid is formed during postmortem anaerobic glycolysis, and the ultimate pH ( > 6.0 in beef) is greater than that of normal meat. Meats that are DFD have firm texture, darker color, and sometimes an off-flavor (Wulf et al., 2002). They are more likely to occur in beef and lamb compared with other species due to their greater proportion of Type I and IIA muscle fibers. Kim et al. (2014) indicated that Type I, IIA, and IIAX fibers were greater in the DFD group, which had a darker color and less drip loss.

Poultry meat defects

PSE meat.

Broilers and turkeys have proportionally more Type II fibers thereby influencing rigor mortis development and their susceptibility to stress. In stress susceptible birds, ultimate pH values (5.4–5.8) of breast meat can be observed as early as 20 min post-mortem. Since muscles reach an acidic pH while the carcass temperatures are still high, extensive protein denaturation occurs that results in the production of PSE meat in breast meat but not in leg meat. Post-mortem glycolysis takes place more rapidly in white muscles such as breast meat compared with red muscles from the legs since white muscles are highly glycolytic (Feiner, 2006).

Pink color.

A pink color defect can occur in fully cooked uncured (no nitrate or nitrite is added) chicken and turkey breast meat. The interaction of myoglobin with ligands and small biomolecules have been considered as major endogenous factors that contribute to the pink color defect, but water contamination can also be the cause of this defect (Joseph et al., 2011). The greater thermostability of turkey myoglobin and the high pH of turkey meat compared with mammalian animals contribute to the pink color defect.

White striping.

White striping occurs due to variability in the thickness of myosepta that contain different amounts of lipid. White striping appears as white striations that are parallel to muscle fibers on the surface of the pectoralis major muscle. Broiler breast meat with white striping has greater drip and cooking loss and less marinade absorption (Petracci et al., 2013a) and leads to decreased consumer acceptability at the time of purchase (Kuttappan et al., 2016).

Woody breast.

Woody breast meat is a more recently identified myopathy that is characterized in broilers as hardened areas with pale ridge-like bulges at both the caudal and cranial regions of the breast that is often accompanied by white striping (Sihvo et al., 2014; Tijare et al., 2016). Woody breast meat has less marinade uptake, greater cook loss, reduced yields, and lighter color than normal meat. It is expressed as severe fiber hypertrophy with an increased proportion of large and abnormal fibers (Petracci et al., 2013b).

Fish meat quality defects


Gaping refers to the partial disruption of the myosepta or the fiber/myosepta interface. This is due to strong rigor tensions and stress or handling of the fish or meat that cause the intervening threads of connective tissue to break, which causes slits or holes to appear in the fillet. Some species are more susceptible to gaping than others. Round fish like cod (Gadhus morhua), and salmon (Salmo salar) generally gape more than flat fish. Some species, such as catfish never gape. Size also influences susceptibility to gaping; smaller fish seem to gape more because the connective tissue is thicker and more developed in larger fish (Borderías and Sánchez-Alonso, 2011).

Red color.

Environmental temperatures greater than 32°C and handling stress including capture, transport, and killing leads to the production of an undesirable reddish color in catfish fillets with soft and exudative texture, sometimes called RSE (red, soft, exudative) meat. The redness is theorized to occur due to the depletion of glycogen prior to harvest, muscle protein denaturation, and hemolysis (Bosworth et al., 2004).


There are both similarities and differences between edible flesh from mammals, poultry, and fish with respect to muscle fiber type, rigor mortis, meat quality, and quality defects that occur. Some of these differences are more related to muscle fiber type than actual species. There are many other differences and similarities that we would have liked to discuss, including calpains and cathepsins, processed meats, sensory differences, etc. Though this paper did not make a clear and final distinction on the definition of meat, the differences in muscle fibers alone and the impact that they have on meat quality and our eating experience is remarkable. The amount of knowledge that is known about all of these food animals and the edible flesh that they produce is also vast and continuing to increase. It is a privilege to conduct research on any or all of these animals and food products.

Mrs. Xue Zhang is a Ph.D. candidate in the department of Food Science, Nutrition, and Health Promotion at Mississippi State University. Zhang received her B.S. and M.S. from the Northeast Agricultural University in China. Her research interests include meat processing, sensory and microbiological qualities of meat products, fermented meat products, meat/muscle proteome, animal gut microbiota, and the safety of meat and meat products.

Dr. Casey Owens is Professor of Poultry Processing and Products and holds the Novus International Professorship of Poultry Science at the University of Arkansas. Owens conducts research to evaluate the effects of preslaughter environmental conditions and processing techniques on muscle metabolism and meat quality of poultry. Her research has a strong emphasis on evaluating production and processing factors affecting poultry meat quality, including tenderness, water-holding capacity, color, and sensory attributes. Her recent research has focused on quality of meat from broilers in big bird market programs, including muscle defects such as white striping and woody breast and issues with meat texture.

Dr. Wes Schilling is a Professor of meat science, sensory science, and food chemistry at Mississippi State University in the Department of Food Science, Nutrition, and Health Promotion. Since coming to Mississippi State University, he has developed five courses that focus on hands-on experiences and real-world examples that he has experienced through interaction with food companies. Real-world examples are related to topics taught through food chemistry, instrumental analysis, and sensory testing principles. His research focuses on sensory science, meat processing (poultry, beef, pork, and catfish), meat quality, flavor chemistry, proteomics, and statistical methods.




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