Free amino acids profile and quality properties of Turkish pastırma cured with potassium lactate and sodium chloride combinations

Author(s):  
Ebru Erdemir
2019 ◽  
Vol 48 (1) ◽  
pp. 22-33 ◽  
Author(s):  
Igor Palčić ◽  
Ana-Marija Jagatić Korenika ◽  
Snježana Jakobović ◽  
Igor Pasković ◽  
Nikola Major ◽  
...  

2018 ◽  
Vol 16 (1) ◽  
pp. 833-841 ◽  
Author(s):  
Magdalena Dziągwa-Becker ◽  
Ryszard Weber ◽  
Olga Zajączkowska ◽  
Wiesław Oleszek

AbstractThe purpose of this study was to establish the free amino acids profile of Viola tricolor collected from different habitats in Poland. Viola tricolor (heartsease) is a very popular plant found worldwide, classified both as weed and medicinal plant. Based on a validated method, the following nineteen free amino acids were analyzed using liquid chromatography-electrospray ionization coupled to a triple quadrupole mass spectrometer (LC-ESI-MS/MS):alanine, glycine, leucine, valine, isoleucine, proline, phenylalanine, tryptophan, tyrosine, serine, threonine, methionine, asparagine, glutamine, lysine, arginine, histidine, aspartic acid, glutamic acid. The total free amino acids (TAA) ranged from 9938.0 to 11393.8 mg/kg of fresh weight. The variability of the investigated amino acids with respect to different habitat conditions was statistically assessed using the method of discriminant and cluster analysis. Alanine, valine, glutamine and aspartic acid were the most abundant free amino acids present in both localizations. The ratio of total essential amino acids (EAA) to TAA was 0.27 and 0.11 in Zagródki and Wrocław, respectively. Discriminant analysis has demonstrated that the investigated habitats significantly differentiated the free amino acids content of Viola tricolor. Only methionine showed a similar concentration in both Viola tricolor populations.


2003 ◽  
Vol 51 (17) ◽  
pp. 5079-5087 ◽  
Author(s):  
Pablo M. Cometto ◽  
Pablo F. Faye ◽  
Romina D. Di Paola Naranjo ◽  
Miguel A. Rubio ◽  
Mario A. J. Aldao

2007 ◽  
Vol 30 (9-10) ◽  
pp. 1371-1383 ◽  
Author(s):  
B. M. Silva ◽  
L. R. Silva ◽  
P. Valentão ◽  
R. M. Seabra ◽  
P. B. Andrade ◽  
...  

2013 ◽  
Vol 141 (3) ◽  
pp. 3207-3214 ◽  
Author(s):  
M. Gratacós-Cubarsí ◽  
C. Sárraga ◽  
M. Castellari ◽  
A. Valero ◽  
J.A. García Regueiro ◽  
...  

Author(s):  
Anna Visy ◽  
Karina Ilona Hidas ◽  
Annamária Barkó ◽  
Lien Le Phuong Nguyen ◽  
László Friedrich ◽  
...  

Abstract Consuming enough protein is a very important part of a balanced and healthy diet. Complete proteins are those in which all essential amino acids are present. In meat products, like hams, many different reactions occur during ageing and storage. For example, the production of free amino acids or the production of biogenic amines is formed by decarboxylation. In this study, the presence of these amino acids and biogenic amines, as well as the quality properties of cured hams during curing and ageing, were investigated. The meat samples were immersed into 100 g L−1 NaCl brine. The curing took 20 days, followed by smoking and ageing for 35 days (12 °C, 75% RH). The wet-cured ham samples were analysed for changes in NaCl concentration (at 3 parts: surface, core, bottom layer). Moreover, color, water activity, denaturation temperature and enthalpy (Differential Scanning Calorimetry), free amino acids (FAAs) and biogenic amines (BAs) were also evaluated.


1959 ◽  
Vol 16 (5) ◽  
pp. 747-754
Author(s):  
E. Bilinski ◽  
H. Fougère

The rate of proteolysis and the deamination of free amino acids in cod muscle treated with 4, 8, 12 and 16% sodium chloride varies with the sodium chloride content and temperature. Proteolysis of the fish muscle protein is completely inhibited at concentrations of 16 and 12% sodium chloride. Trimethylamine formation is inhibited by 16% sodium chloride for at least 15 days. Both inhibitions take place at either 15 or 25 °C. In salted muscle deamination can occur in the absence of trimethylamine formation. The reaction appears to be hardly influenced by salt. Indole formation is completely inhibited by 8% salt at either 15 or 25 °C.


2020 ◽  
Vol 23 ◽  
Author(s):  
María del Rosario Brunetto ◽  
Máximo Gallignani ◽  
Wendy Orozco ◽  
Sabrina Clavijo ◽  
Yelitza Delgado ◽  
...  

Abstract The development of cocoa flavor and aroma is a complex phenomenon that depends on how the fermentation and roasting processes are carried out. During fermentation, the formation of some compounds so-called “aroma and flavor precursors” takes place, which are finally expressed during the roasting stage. Therefore, the evaluation of aroma precursors such as the amino acids formed during fermentation is crucial in order to determine the quality of the cocoa. In this context, we developed and validated a method for the study of these compounds in cocoa samples. The amino acids were quantitatively converted into their trimethylsilyl derivatives before their determination by gas chromatography with mass spectrometry detection. The results were verified performing precision and accuracy studies. The inter and intra assay coefficients of variation (C.V, n = 5) were lower than 4.7% and 4%, respectively. The analytical recoveries (95% to 108% with C.V < 4.2, n = 5) demonstrated the high performance of the extraction procedure. The method was successfully applied to the analysis of the amino acids in 110 samples of Venezuelan Criollo cocoa during the three days of fermentation and roasting (110 °C for 25 min). All samples had an appreciable content of free amino acids ranging between 3.87 and 5.97 g/kg in the absence of fermentation. We observed degradation of the acidic amino acids during the first day of fermentation, while the rest of amino acids increased progressively during the fermentation process with a predominance of the hydrophobic ones, mainly leucine, phenylalanine, valine, alanine and isoleucine. Additionally, during the roasting stage a fraction of the amino acids, especially the hydrophobic ones, was partially degraded through Maillard reaction to form the compounds associated with the cocoa aroma and flavor.


1993 ◽  
Vol 264 (6) ◽  
pp. R1164-R1179 ◽  
Author(s):  
J. J. Bedford ◽  
J. P. Leader

Rats were exposed to osmotic stress either acutely, over periods of 1 or 4 h, or chronically, over several days. In acute experiments, hyposmolality was induced by intraperitoneal infusion of dilute glucose or mannitol solutions, whereas hyperosmolality was induced by use of sodium chloride, concentrated glucose or mannitol solutions, or urea. Chronic hypernatremia was induced by daily administration of sodium chloride to water-deprived animals; chronic hyponatremia was induced by daily injection of antidiuretic hormone supplemented with glucose. Animals were made hyperglycemic using streptozotocin or uremic by ureteral ligation. Where appropriate, animals were anesthetized with thiobutabarbital (Inaktin) or ether. In acute experiments, analysis of the composition of the cardiac ventricle, diaphragm, liver, and renal cortex showed no evidence of cell volume regulatory processes involving transmembrane movement of potassium ions. There was a small but significant increase in free amino acids [measured as ninhydrin-positive substance (NPS)] in cardiac muscle exposed to hypertonic solutions of sodium chloride and glucose but not when plasma osmolality was raised using mannitol. In cerebral cortical tissue, after 4 h of exposure to acute hypertonicity by infusion of sodium chloride or glucose, there was a significant increase in tissue potassium content and a slight increase in NPS content. In chronic experiments, tissue analysis revealed good evidence for cellular volume readjustment only in cerebral cortex and heart. In the cortex, levels of free amino acids, principally taurine and glutamate (plus glutamine), showed large increases during hypernatremia and hyperglycemia and corresponding decreases during hyposmolality. In heart the principal amino acid present was taurine, and it, together with aspartate and glutamate (plus glutamine), showed large changes under osmotic stress. Other tissues analyzed showed only small changes in composition.


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