Collagen cross-linking in porcine m. longissimus lumborum: Absence of a relationship with variation in texture at pork weight

Avery, Nicholas C.; Sims, Trevor J.; Warkup, C C; Bailey, Allen J.

doi:10.1016/0309-1740(95)00021-6

Cited by 57 publications

(37 citation statements)

References 17 publications

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“…Cooked CHM had the lowest moisture value, followed sequentially by the uncooked, cooked fresh tissue and finally, by the fresh tissue samples. As pointed out in Avery et al (1996), collagen denatures upon cooking and shrinks. Resistance from the denatured muscle proteins leads to a tension that squeezes the water out, making the meat tougher, particularly in mature animals.…”

Section: Resultsmentioning

confidence: 92%

“…Samples of 150-200g were vacuum packed and cooked in a water bath until 75-78 o C internal temperature as measured by a Hanna thermocouple, model HI 8313, (Co. City, State) USA. Samples were cooled to room temperature and the meat surface was dried with absorbent paper (Avery et al, 1996). Moisture, ash, protein and lipid were determined according to AOAC (1995) methods.…”

Section: Methodsmentioning

confidence: 99%

“…Indeed, hydroxylysinoketonorleucine (HLKNL), the main form of collagen crosslinking in an immature animal decreases with aging (Shimokomaki et al, 1972) and is replaced by hydroxylysylpyridinium (HP) (Fujimoto et al, 1977;Eyre and Oguchi, 1980). HP has been shown to be related to increased toughness (Nakano et al, 1991;Bosselman et al;Coro et al, 2002) although this relationship has been questioned (Avery et al, 1996). In this work, we report the measurement of tenderness and its relationship to both HP concentration and moisture throughout the processing.…”

Section: Introductionmentioning

confidence: 95%

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Chemical basis for beef charqui meat texture

Youssef

Garcia

Yamashita

et al. 2007

Braz. arch. biol. technol.

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Section: Resultsmentioning

confidence: 92%

Section: Methodsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 95%

See 1 more Smart Citation

Chemical basis for beef charqui meat texture

Youssef

Garcia

Yamashita

et al. 2007

Braz. arch. biol. technol.

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“…The amount of collagen was determined by multiplying the colour intensity to 8.0 (Kolar, 1980). HP was analyzed by HPLC (Avery, et al, 1996). It consisted essentially in removing myofibrillar proteins with a 0.06M KCl treatment, centrifugation, and the precipitate was collected and dialyzed against several distilled water changes and finally lyophilised.…”

Section: Animalsmentioning

confidence: 99%

Comparison of proximate chemical composition and texture of cupim, Rhomboideus m. and lombo, Longissimus dorsi m. of Nelore (Bos indicus)

Pedrão

Lassance

Souza

et al. 2009

Braz. arch. biol. technol.

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“…As the proportion of IMCT increases, IMF also correspondingly increases. The relationship between IMF and tenderness in pork is controversial; some researchers reported a marked correlation whereas others found none (Avery et al, 1996;Van Laack et al, 2001). Pork with different IMCT levels may have originated from pigs with different genetic backgrounds.…”

Section: Discussionmentioning

confidence: 99%

Histological characteristics of longissimus dorsi muscle and their correlation with restriction fragment polymorphisms of calpastatin gene in F2 Jinghua × Piétrain crossbred pigs

Liu

2007

Animal

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In order to evaluate the genotype of the calpastatin (CAST) gene and its relationship to muscle histology and other post mortem traits in the Jinhua 3 Pié train F 2 pig family, 158 barrows and gilts were electrically stunned and exsanguinated. Both blood and muscle samples were collected, and both post mortem traits and meat qualities were recorded. Restriction fragment length polymorphism (RFLP) analysis, the periodic acid Schiff reaction (PAS) and myosin heavy-chain immunohistochemistry were employed to explore the relationship between genotype and muscle histology. Based on PAS reactivity, muscle fibres can be classified into three types: PAS (2), PAS (1) and PAS (11). Myosin heavy-chain immunohistochemistry can differentiate muscle fibres into either slow or fast fibres; the proportion of slow and fast fibres were 6% and 94%, respectively. When the amplification products of the CAST gene were digested with MspI, HinfI and RsaI, two different cleavage patterns could be discriminated from the endonuclease map detected using each enzyme. The results showed that the polymorphisms detected using these three endonucleases are identical. Only three genotypes (AA/CC/EE, AB/CD/EF and BB/DD/FF) were distinguished. Their frequencies were 0.1835, 0.5823 and 0.2342, respectively. Different genotypes had significant association with area and pH 45m value of loin muscle, while showing no significant association with the water-holding capacity and conductivity of loin muscle. The results also revealed that the genotypes had a significant correlation with diameter, area, circularity and the aspect ratio of muscle fibres. It was also presented that the genotypes significantly correlated with the percentage of intramuscular connective tissue.

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Collagen cross-linking in porcine m. longissimus lumborum: Absence of a relationship with variation in texture at pork weight

Cited by 57 publications

References 17 publications

Chemical basis for beef charqui meat texture

Chemical basis for beef charqui meat texture

Comparison of proximate chemical composition and texture of cupim, Rhomboideus m. and lombo, Longissimus dorsi m. of Nelore (Bos indicus)

Histological characteristics of longissimus dorsi muscle and their correlation with restriction fragment polymorphisms of calpastatin gene in F2 Jinghua × Piétrain crossbred pigs

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