Quantitative determination of the myofibrillar proteins and connective tissue content in selected porcine skeletal muscles

Zarkadas, Constantinos G.; Karatzas, C.N.; Khalili, Ali D.; Khanizadeh, Shahrokh; Morin, G.

doi:10.1021/jf00084a004

Cited by 36 publications

(14 citation statements)

References 65 publications

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“…The exceptions were asparagine and histidine, with increases during processing of only 0.1 and 0.2 mmol/100 g DM, respectively, and also tryptophan, which reached a final concentration of approximately 800 times that found in raw pork. The increase of histidine, asparagine, and arginine in the fully ripened ham was lower than expected, according to their ratio in muscle proteins from pig (Zarkadas et al, 1988). These three amino acids are characterized by their intense reaction with reducing compounds in the Maillard condensations (Ashoor and Zent, 1984; Wong and Stanton, 1989).…”

Section: Resultsmentioning

confidence: 73%

“…On the other hand, the 800-fold increase for tryptophan is partially due to its low concentration in the free form found in raw pork, given that its overall increase throughout the ripening process is lower than that of most amino acids (Figure 1). On the other hand, the low ratio at which tryptophan has been reported in proteins from porcine skeletal muscle (Zarkadas et al, 1988) suggests that the released amount of this amino acid exceeds expectations. The explanation for this unexpected increase during ripening could come from a specific tryptophan aminopeptidase activity.…”

Section: Resultsmentioning

confidence: 89%

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Evolution of free amino acids and amines during ripening of Iberian cured ham

Córdoba¹,

Antequera²,

Garcı́a³

et al. 1994

J. Agric. Food Chem.

128

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Fifty-eight hams were obtained from Iberian pigs and were traditionally processed into dry cured products. Free amino acids and amines from semimembranosus and biceps femoris muscles were detected and quantified by HPLC. The larger increases of free amino acids took place in the drying cycle. Glutamic acid, alanine, leucine, and glycine were the free amino acids present in higher quantities in the final product. The amines with higher concentrations were not in the toxic range. Most amino acids increased according to their proportion in porcine skeletal muscle, except for some basic amino acids that may be involved in the formation of volatile compounds and amines.

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Section: Resultsmentioning

confidence: 73%

Section: Resultsmentioning

confidence: 89%

Evolution of free amino acids and amines during ripening of Iberian cured ham

Córdoba¹,

Antequera²,

Garcı́a³

et al. 1994

J. Agric. Food Chem.

128

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show abstract

“…9860) test tubes (18 X 150 mm) under vacuum (below 10 mmHg) with triple-glass-distilled constant-boiling HC1 (6.0 M) containing 0.2% (v/v) phenol at 110 ± 0.5 °C for periods of 24, 48, 72, and 96 h with the usual precautions described by Zarkadas et al (1988c). Analyses of individual acid hydrolysates were performed on the clear filtrate in duplicate by methods described previously (Zarkadas et al, 1986(Zarkadas et al, ,1988b.…”

Section: Methodsmentioning

confidence: 99%

Comparison of the protein-bound and free amino acid contents of two northern adapted soybean cultivars

Zarkadas¹,

Yu²,

Voldeng³

et al. 1994

J. Agric. Food Chem.

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“…The M procedure could break more effectively the meat gel structure formed during the processing of the dry-cured hams than the S one. In fact, other authors [ 29 , 30 ] observed a difficulty of protein extraction during the processing of Iberian hams, even using solutions with high ionic strength for their extraction. The observed suitability of the M in the extraction procedures for the analyses of these compounds could be related to the combined movement of the grinding jars with the balls, which results in an intensive mixing of the ham sample with the solvent.…”

Section: Resultsmentioning

confidence: 99%

A Rapid and Accurate Extraction Procedure for Analysing Free Amino Acids in Meat Samples by GC-MS

Pérez‐Palacios

Barroso

Ruiz

et al. 2015

International Journal of Analytical Chemistry

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This study evaluated the use of a mixer mill as the homogenization tool for the extraction of free amino acids in meat samples, with the main goal of analyzing a large number of samples in the shortest time and minimizing sample amount and solvent volume. Ground samples (0.2 g) were mixed with 1.5 mL HCl 0.1 M and homogenized in the mixer mill. The final biphasic system was separated by centrifugation. The supernatant was deproteinized, derivatized and analyzed by gas chromatography. This procedure showed a high extracting ability, especially in samples with high free amino acid content (recovery = 88.73–104.94%). It also showed a low limit of detection and quantification (3.8 · 10−4–6.6 · 10−4 μg μL−1 and 1.3 · 10−3–2.2 · 10−2 μg μL−1, resp.) for most amino acids, an adequate precision (2.15–20.15% for run-to-run), and a linear response for all amino acids (R 2 = 0.741–0.998) in the range of 1–100 µg mL−1. Moreover, it takes less time and requires lower amount of sample and solvent than conventional techniques. Thus, this is a cost and time efficient tool for homogenizing in the extraction procedure of free amino acids from meat samples, being an adequate option for routine analysis.

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Quantitative determination of the myofibrillar proteins and connective tissue content in selected porcine skeletal muscles

Cited by 36 publications

References 65 publications

Evolution of free amino acids and amines during ripening of Iberian cured ham

Evolution of free amino acids and amines during ripening of Iberian cured ham

Comparison of the protein-bound and free amino acid contents of two northern adapted soybean cultivars

A Rapid and Accurate Extraction Procedure for Analysing Free Amino Acids in Meat Samples by GC-MS

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