Assessment of the Protein Quality of Beefstock Bone Isolates for Use as an Ingredient in Meat and Poultry Products

Zarkadas, Constantinos G.; Yu, Ziran; Zarkadas, George C.; Minero-Amador, Adolfo

doi:10.1021/jf00049a015

Cited by 20 publications

(13 citation statements)

References 26 publications

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“…In their paper examining the quality of protein in bones from young bulls, Zarkadas et al (1995) reported that the content of total protein of demineralised bone powder varied between 78-80% in dry matter and connective tissue proteins accounted for 72.3-81.1%…”

Section: Resultsmentioning

confidence: 99%

Amino Acid Profile of Protein from Pelvic Limb Long Bones of Broiler Chickens

et al. 2009

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The objective of the study was to determine the amino acid profile in protein from long bones of the pelvic limb (femur, tibiotarsus) in ROSS 308 hybrid broiler chickens, and to examine whether it is sex-dependent.The study material was obtained from 120 Ross 308 broiler chickens (60 males and 60 females) at the end of the fattening (40 days of age). The average weight of birds was 2 694 ± 32.6 g for cockerels and 2 345 ± 23.9 g for pullets. The study birds did not show any clinical signs of leg diseases. The long bones of the right pelvic limbs (femur and tibiotarsus) were collected after bird slaughter and after removal of soft tissues, they were used for laboratory analyses. The crude protein content and the amino acid (AA) composition were determined and the obtained values were recalculated to 100% dry matter. The chemical score (CS) and the essential amino acid index (EAAI) were calculated for each AA. As a standard, the hen egg ovalbumin was used. The crude protein content in 100% dry matter shows that the content of crude protein was significantly higher (P ≤ 0.01) in the femur (405.3 ± 17.21 g/kg) compared to the tibiotarsus (393.5 ± 12.68 g/kg). The same trends were found with regard to sex. Both males and females had significantly (P ≤ 0.01) higher crude protein content in the femur (406.6 ± 19.34 g/kg and 404.1 ± 15.09 g/kg, respectively) than in the tibiotarsus (395.0 ± 12.16 g/kg and 392.1 ± 13.21 g/kg, respectively). Both bones showed the highest contents of Gly, Glu and Pro, and the lowest contents of Met, Tyr and His. The same trends were found with regard to chicken sex. Collagenous protein has lower contents of most AA in comparison to the standard protein -ovalbumin; especially contents of Ser, Val, Met, Ileu and Phe are substantially lower. On the other hand, collagenous protein had higher contents of Gly, Pro, His and Arg. The collagenous protein EAAI for the femur and the tibiotarsus was 59.0% and 57.4%, respectively. The knowledge of amino acid composition in protein from long bones of the pelvic limb in broiler chickens is important because it can help us understand the origin of bone disorders. Femur, tibiotarsus, crude protein, chemical score, essentials amino acid indexBones are predominantly composed of the inorganic mineral hydroxyapatite (Ca 10 (PO 4 ) 6 OH 2 ). Approximately 30% of bone tissue consists of organic compounds of which 90-95% is represented by collagen. The remaining portion is made up of proteins, particularly osteocalcin which is one of the most widespread non-collagen proteins, representing up to 3% of total protein in bones. Collagen is a water-insoluble protein which forms the main part of connective tissue. It represents 30% of total body protein (Mosby 2009). It is a fibrous protein that ensures bone strength and flexibility. It is an important component of a number of other tissues including the skin and tendons. Collagen molecules consist of linear, unbranched sequences of approximately 20 amino acids. The molecule's structure is stabilized by hydroge...

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Section: Resultsmentioning

confidence: 99%

Amino Acid Profile of Protein from Pelvic Limb Long Bones of Broiler Chickens

et al. 2009

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“…Laser-Reuterswä rd (1985). a Data taken from (a) Linder et al (1995a); (b) Eastoe and Leach (1977); (c) Zarkadas et al (1995); (d) Laser-Reuterswä rd (1985); (e) Eggum et al (1989).…”

Section: Protein Quality Indexesmentioning

confidence: 99%

“…They are a potential source of ingredients in various meat products (Laser-Reuterswärd et al, 1982). Data on amino acid composition of meat bone hydrolysates, isolates and meals have not been widely reported (Hegedüs et al, 1983(Hegedüs et al, , 1990Zarkadas et al, 1995).…”

Section: Introductionmentioning

confidence: 99%

Nutritional Value of Veal Bone Hydrolysate

Linder

Rozan

Kossori

et al. 1997

Journal of Food Science

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Industrial veal hydrolysate was produced enzymatically for possible use as a gelatin-replacing ingredient for human consumption. Protein digestibility and nutritional value were determined in vitro and in vivo. Net protein ratio (ϭ 2.65) and true digestibility (ϭ 80.3) were compared with gelatin and caseinate. Protein digestibility was determined by pHstat method and cell dialysis. Amino acid composition including 4-hydroxyproline, allowed determination of connective tissue, amino acid score and protein digestibility corrected amino acid score. High correlation was found between true digestibility and pH-stat method (R 2 ϭ 0.99). Meaty flavor and gelling properties of veal hydrolysate could make it useful for high-quality soups, sauces and gravies.

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“…Actually, there are some commercial collagen-based byproducts for use in the meat processing industry as ingredients in various meat products. Such collagen byproducts include skins (rind) and skin trimmings, tendon, beef shank, sinew residues, and hand or mechanically separated bones from beef, pork, and poultry carcasses (Zarkadas et al, 1995). However, high collagen content in meat products could produce physical defects during the cooking like unstable emulsions, formation of gelatin or fat pockets, or bad peeling (Flores, 1980).…”

Section: Introductionmentioning

confidence: 99%

“…However, high collagen content in meat products could produce physical defects during the cooking like unstable emulsions, formation of gelatin or fat pockets, or bad peeling (Flores, 1980). In addition, the amount of collagen byproducts relates to the final product and nutritional qualities (Flores, 1980;Zarkadas et al, 1995).…”

Section: Introductionmentioning

confidence: 99%