Functionality of muscle proteins in gelation mechanisms of structured meat products

Asghar, Ali; Samejima, Kunihiko; Yasui, Tsutomo; Henrickson, R. L.

doi:10.1080/10408398509527408

Cited by 279 publications

(195 citation statements)

References 593 publications

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“…Westphalen et al (2006) suggested that fiber type influenced water-holding capacity to a greater degree than pH. Asghar et al (1985) reported that an influencing factor on the gel strength is the ratio of myosin and actin. Lan et al (1995) observed that differences in gelation properties between species were not consistent at various protein concentrations.…”

Section: Resultsmentioning

confidence: 99%

Effect of Various Amounts of Pork and Chicken Meat on the Sensory and Physicochemical Properties of Chinese-style Meatball (Kung-wan)

Kang

Zou

et al. 2013

FSTR

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The effects of various mixtures of pork leg meat and chicken breast meat, ranging from 0 to 100% on quality attributes of raw meat-emulsion batters and kung-wans were investigated. Increasing the content of chicken breast meat altered the color by increasing lightness and yellowness, increased protein solubility, and increased hardness. Hardness and springiness play important roles in kung-wan, and consumers prefer those having a firmer, harder texture. The emulsion stability changed with different mixtures of pork leg meat and chicken breast meat. With mixtures of meats, the emulsion stabilities were lower. The treatments which containing chicken breast meat had a higher storage modulus than 100% pork leg meat at temperatures higher than 60℃, and so had better texture. The results showed that chicken breast meat, at 50% substitution for pork leg meat, improved the quality of kung-wan.Keywords: kung-wan, emulsion stability, dynamic rheological, protein solubility, texture *To whom correspondence should be addressed. E-mail: xlxu@njau.edu.cn IntroductionEmulsified meats are available in a large range of products that provide the consumer with a wide choice of textures and flavors depending on their method of production. Commonly, different types of specific products originate from individual countries or regions where tradition has played a large part in their development. One such product is the Chinese-style meatball, or kung-wan, which is made primarily from pork and is a popular meat product in Taiwan and related Chinese communities (Hsu and Chung, 1998). It is a typical emulsified meat product, commonly made with pork leg meat and back fat (Hsu and Chung, 1999). Consumers regard texture is an important factor of this product, and in particular, springiness and cohesiveness are two attributes that define this ball-shaped meat product. Springiness is to some extent the result of inclusion of air during the beating method used in their production.These important textural properties are highly dependent not only on the method of fabrication but also upon the properties of the myofibrillar proteins and the characteristics of the muscle tissue. It has been reported for instance that muscle from pork and chicken have different gelation properties (Cofrades et al., 1997;Iwasaki et al., 2006;Kang et al., 2010) which affects the product texture. The salt soluble proteins (SSP) of muscle are the most important functional proteins for the manufacture of emulsified meat products. Muscle is classified by fiber type. Pork leg meat (PLM) is comprised primarily of type IIB fibers, and other is type I and type IIA myofibers (Suzuki et al., 1999), whereas chicken breast meat (CBM) is composed of essentially 100% white muscle fiber (fiber type IIB) (Nakamura et al., 2004). Different muscle types exhibit different the heat-induced gelation properties of SSP (Xiong, 1994).The consumption of chicken meat continues to grow around the world. Chicken meat is viewed as a tastier, healthier, lower in fat-content than pork (McCarthy et ...

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Section: Resultsmentioning

confidence: 99%

Effect of Various Amounts of Pork and Chicken Meat on the Sensory and Physicochemical Properties of Chinese-style Meatball (Kung-wan)

Kang

Zou

et al. 2013

FSTR

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“…Up until the latter half of the 1990s, sarcoplasmic protein (SP), a water-soluble muscle protein, was believed to contribute very little to the texture of meat products (Samejima et al, 1969;Asghar et al, 1985;Ziegler and Foegeding, 1990). However, recently, a number of reports have shown improved texture of meat products by the addition of SP.…”

Section: Introductionmentioning

confidence: 99%

Molecular Interaction Studies Evaluating the Gelation of Myosin B with Glyceraldehyde 3-phosphate Dehydrogenase after Succinylation

Sakamoto

Sasaki

Nakade

et al. 2013

FSTR

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Previously, it was clarified that myofibril gelation was enhanced by the basic protein glyceraldehyde 3-phosphate dehydrogenase (GPD). In this study, the mechanism of the gel-enhancing action of GPD to myosin B was evaluated through the study of the surface properties of GPD. GPD and myosin B were prepared from pork loin. Succinylated GPD (S-GPD) was successfully prepared without any loss of solubility at a weight ratio (succinic anhydrate to GPD) of 1.0. Though gelation of myosin B alone required a minimum protein concentration of 4.0% (w/v), the addition of GPD enhanced the gelation of myosin B at a concentration of 3.5% (w/v). Furthermore, GPD increased the gel strength drastically at concentrations above 4.5% (w/v). On the other hand, the addition of S-GPD did not improve the gelling property of myosin B. SDS-PAGE showed molecular interaction between GPD and myosin B, but not between S-GPD and myosin B. However, in the case of GPD, the GPD band became insoluble under coexistence of GPD with myosin B. Meanwhile, the myosin heavy chain was partially soluble. Furthermore, actin and GPD bands became thicker in the insoluble fraction after mixing of G-actin and GPD. These results indicate that positive charges on the surface of GPD are necessary to enhance the gelation of myosin B.

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“…3) Proteolysis of myosin with trypsin or chymotrypsin produces tail sub fragments such as light meromyosin(LMM) and rods. 4'5) The tail portion of myosin heavy chain (MHC) is composed of repetitive oc-helical sequences that assemble in register with another MHCto form a coiled coil.6'7) The repetitive sequence of myosin tail segments included 28-amino acid repeats of seven-residue units with hydrophobic residues at specific positions.…”

Section: Myosin Solutionsmentioning

confidence: 99%

Involvement of hydrophobic residues in heat-induced gelation of myosin tail subfragments from rabbit skeletal muscle.

Morita

Yasui

1991

Agricultural and Biological Chemistry

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Myosin solutionsform gels when heated under appropriate conditions.1>2) The process of heat-induced gelation of skeletal muscle myosin at high ionic strength was explained as the irreversible aggregation of the globular head segments of myosin molecules and network formation resulting from the unfolding of helical tail segments.3) Proteolysis of myosin with trypsin or chymotrypsin produces tail sub fragments such as light meromyosin(LMM) and rods.4'5) The tail portion of myosin heavy chain (MHC) is composed of repetitive oc-helical sequences that assemble in register with another MHCto form a coiled coil.6'7) The repetitive sequence of myosin tail segments included 28-amino acid repeats of seven-residue units with hydrophobic residues at specific positions. This organization provide a hydrophobic surface for the interaction between the two MHCsubunits.7) Borejdo8) has reported that the binding site for a surface hydrophobic probe was located in the head region but not in the LMM region of skeletal myosin molecule in its native state. Samejima et al.9'10) have reported that the aromatic amino acids of myosin were transferred from a hydrophobicenvironmentto a morepolar environment during thermal treatment, based on their results of fluorescence and difference spectra experiments. However, the relationship between the surface hydrophobicity and the heat-induced gelation of skeletal muscle myosin is still obscure. In this study we examined the changes of hydrophobicity of myosin tail sub fragments from skeletal muscle during the formation of gels on heating. The hydrophobic amino acid residues of the myosin tail sub fragments began to be exposed at 35^40°C, attained the maximum at about 65°C, and decreased at temperatures higher than 65°C. These changes in hydrophobicity of myosin tail sub fragments on heating seem to correspond well to the heat-induced gel forming process of the myosin sub fragments. Fluorescence was measured at 20°C with a Hitachi 650-40 spectrofluorometer in the ratio mode.The wavelengths of excitation and emission for PA fluorescence were 327 nm and 420nm, and those for TNSfluorescence were 333 nm and 445 nm, respectively. In both cases the excitation and emission slits were 2 nm and 8 nm. Fluorescence intensities were expressed relative to that of a protein solution incubated at 20°C for lOmin. Figure 1 shows the changes in helix content and surface hydrophobicity of LMMon heating. The helix content of phosphate buffer (pH 6.0) was raised and then circular dichroism was measured after 20 min (O). The reversibility of helix content was examined at 20°C after keeping the solution at each temperature for 20 min followed by cooling to 20°C and standing for 10min (#). Fluorescence: the solution containing 1jim LMM,0.6m KC1, and 20mM phosphate buffer (pH 6.0) was held at a constant temperature for 20min, cooled to and kept at 20°C for 10 min, and then fluorescence intensity measurements were began 10min after adding of 1 /im PA (A) or 10/iM TNS (å¡)à" Arrows indicate transition points obtained by the...

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Functionality of muscle proteins in gelation mechanisms of structured meat products

Cited by 279 publications

References 593 publications

Effect of Various Amounts of Pork and Chicken Meat on the Sensory and Physicochemical Properties of Chinese-style Meatball (Kung-wan)

Effect of Various Amounts of Pork and Chicken Meat on the Sensory and Physicochemical Properties of Chinese-style Meatball (Kung-wan)

Molecular Interaction Studies Evaluating the Gelation of Myosin B with Glyceraldehyde 3-phosphate Dehydrogenase after Succinylation

Involvement of hydrophobic residues in heat-induced gelation of myosin tail subfragments from rabbit skeletal muscle.

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