scholarly journals Amino Acids and Biogenic Amines Evolution during theEstufagemof Fortified Wines

2015 ◽  
Vol 2015 ◽  
pp. 1-9 ◽  
Author(s):  
Vanda Pereira ◽  
Ana C. Pereira ◽  
Juan P. Pérez Trujillo ◽  
Juan Cacho ◽  
José C. Marques

The current study was focused on the impact of accelerated ageing (heating step) on the amino acid and biogenic amine profiles of fortified wines. In this sense, three Madeira wines from two commonly used grape varieties (one red and the other white) were analysed during the heating, at standard (45°C, 3 months) and overheating (70°C, 1 month) conditions, following a precolumn derivatization procedure using iodoacetic acid,o-phthaldialdehyde, and 2-mercaptoethanol, carried out in the injection loop prior to RP-HPLC-FLD detection. Eighteen amino acids were identified, with arginine being the most abundant. An important decrease of the amino acid levels was detected during the standard heating (up to 30%), enhanced up to 61% by the temperature increase. Cysteine, histidine, and asparagine revealed the greatest decreases at 45°C. Conversely, some amino acids, such as asparagine, slightly increased. Four biogenic amines were identified but always in trace amounts. Finally, it was observed that the accelerated ageing did not favour the biogenic amine development. The results also indicate that the heating process promotes the amino acid transformation into new ageing products.

2004 ◽  
Vol 22 (SI - Chem. Reactions in Foods V) ◽  
pp. S287-S289 ◽  
Author(s):  
L. Simon-Sarkadi ◽  
E. Szőke ◽  
A. Kerekes

Comparative study was conducted on the basis of free amino acids and biogenic amines of Hungarian sparkling wines originated from 3 producers (Törley, Hungária, Balaton Boglár). Determination of amino acids and biogenic amines was accomplished by ion-exchange chromatography using an amino acid analyser. The dominant free amino acids in sparkling wines were proline and arginine and the major biogenic amine was spermidine. Based on results of chemometric analyses, free amino acid and biogenic amine contents seemed to be closely related to quality and the technology of sparkling wine making.


Foods ◽  
2020 ◽  
Vol 9 (10) ◽  
pp. 1377
Author(s):  
Lucía Gómez-Limia ◽  
Roxana Cutillas ◽  
Javier Carballo ◽  
Inmaculada Franco ◽  
Sidonia Martínez

This study evaluated the effects of the canning process and different filling media on the free amino acid and biogenic amine contents of eels. The main free amino acids were histidine, taurine and arginine, which constituted 72% of the free amino acids in raw eels. All steps in the canning process significantly altered the free amino acid content of eels, relative to raw samples. The changes were influenced by the step, the composition of the frying or filling medium and the storage time. The biogenic amine contents were very low in all samples. Histamine was not detected in either raw eels or canned eels. The highest values were obtained for 2-phenylethylamine. The step of the canning process, the composition of the frying or filling medium and storage time also determined the changes in the biogenic amine contents. The biogenic amines indices were low, indicating the good quality of canned eels.


Author(s):  
A. Zavala ◽  
M. González ◽  
P. Pino

The objective of this research was to determine the quality of the protein present in sausages fortified with quinoa as a substitute for animal protein, through the identification and quantification of amino acids, using gas chromatography and precolumn derivatization. The amino acid composition found in the analyzed products was predominantly composed of: Threonine (THR) with a concentration of 1046.32µmol / L, aminobutyric acid (ABA) with a concentration of 9685.68 µmol / L and glutamic acid (GLU) with a concentration of 1178.71 µmol / L. These values were found in the treatment with the highest percentage of quinoa flour, establishing a directly proportional relationship between the concentrations of these amino acids and the percentage of quinoa. Gas chromatography was an adequate technique for determining the amino acid profile due to its speed and sensitivity. Keywords: amino acids, sausages, quinoa, derivatization, gas chromatography. RESUMEN La presente investigación tiene por objetivo determinar la calidad de la proteína presente en embutidos fortificados con quinua como sustituyente de la proteína animal, a través de la identificación y cuantificación de aminoácidos mediante la aplicación de cromatografía de gases y la derivatización precolumna. La composición de aminoácidos encontrada en los productos analizados destaca la presencia mayoritaria de: Treonina (THR) con una concentración de 1046,32 µmol/L, ácido aminobutírico (ABA) con una concentración de 9685,68 µmol/L  y ácido glutámico (GLU) con una concentración de 1178,71 µmol/L, todos estos valores se presentaron en el tratamiento con mayor porcentaje de harina de quinua estableciéndose una relación directamente proporcional entre las concentraciones de estos aminoácidos y el porcentaje de adición de quinua en los tratamientos estudiados. Se puede concluir que la cromatografía de gases empleada resultó una técnica adecuada para la determinación del perfil aminoacídico por la rapidez y sensibilidad presentada sobre las muestras estudiadas.  Palabras claves: aminoácidos, embutidos, quinua, derivatización, cromatografía de gases.  


2006 ◽  
Vol 69 (2) ◽  
pp. 397-404 ◽  
Author(s):  
Á. MARCOBAL ◽  
P. J. MARTÍN-ÁLVAREZ ◽  
M. C. POLO ◽  
R. MUÑOZ ◽  
M. V. MORENO-ARRIBAS

Changes in biogenic amines (histamine, methylamine, ethylamine, tyramine, phenylethylamine, putrescine, and cadaver-ine) were monitored during the industrial manufacture of 55 batches of red wine. The origin of these amines in relation to must, alcoholic fermentation, malolactic fermentation, sulfur dioxide addition, and wine aging and the interactions between amines and their corresponding amino acids and pH were statistically evaluated in samples from the same batches throughout the elaboration process. Some amines can be produced in the grape or the musts (e.g., putrescine, cadaverine, and phenylethylamine) or can be formed by yeast during alcoholic fermentation (e.g., ethylamine and phenylethylamine), although quantitatively only very low concentrations are reached in these stages (less than 3 mg/liter). Malolactic fermentation was the main mechanism of biogenic amine formation, especially of histamine, tyramine, and putrescine. During this stage, the increase in these amines was accompanied by a significant decline in their amino acid precursors. Significant correlations between biogenic amine formation and the disappearance of their corresponding amino acids were observed, which clearly supports the hypothesis that malolactic bacteria are responsible for accumulation of these amines in wines. No increase in the concentration of biogenic amines was observed after SO2 addition and during wine aging, indicating that sulfur dioxide prevents amine formation in subsequent stages.


2003 ◽  
Vol 70 (2) ◽  
pp. 249-252 ◽  
Author(s):  
Áine C Curtin ◽  
Paul LH McSweeney

Bacterial decarboxylases and aminotransferases may be involved in the production of flavour or off-flavour compounds from aromatic amino acids during cheese ripening. Transamination is one of the first steps in amino acid catabolism for both lactococci and lactobacilli (Gao et al. 1997; Klein et al. 2001). Biologically active amines, produced by decarboxylation, such as tyramine, phenylethylamine, tryptamine, histamine, cadaverine and putrescine, known as biogenic amines, have been found in cheese and can cause migraine and hypertension in susceptible consumers (McSweeney & Sousa, 2000).


2000 ◽  
Vol 66 (4) ◽  
pp. 1354-1359 ◽  
Author(s):  
Liesbeth Rijnen ◽  
Pascal Courtin ◽  
Jean-Claude Gripon ◽  
Mireille Yvon

ABSTRACT The first step of amino acid degradation in lactococci is a transamination, which requires an α-keto acid as the amino group acceptor. We have previously shown that the level of available α-keto acid in semihard cheese is the first limiting factor for conversion of amino acids to aroma compounds, since aroma formation is greatly enhanced by adding α-ketoglutarate to cheese curd. In this study we introduced a heterologous catabolic glutamate dehydrogenase (GDH) gene into Lactococcus lactis so that this organism could produce α-ketoglutarate from glutamate, which is present at high levels in cheese. Then we evaluated the impact of GDH activity on amino acid conversion in in vitro tests and in a cheese model by using radiolabeled amino acids as tracers. The GDH-producing lactococcal strain degraded amino acids without added α-ketoglutarate to the same extent that the wild-type strain degraded amino acids with added α-ketoglutarate. Interestingly, the GDH-producing lactococcal strain produced a higher proportion of carboxylic acids, which are major aroma compounds. Our results demonstrated that a GDH-producing lactococcal strain could be used instead of adding α-ketoglutarate to improve aroma development in cheese.


2013 ◽  
Vol 110 (6) ◽  
pp. 981-987 ◽  
Author(s):  
Atsushi Kanda ◽  
Kyosuke Nakayama ◽  
Tomoyuki Fukasawa ◽  
Jinichiro Koga ◽  
Minoru Kanegae ◽  
...  

It is well known that ingestion of a protein source is effective in stimulating muscle protein synthesis after exercise. In addition, there are numerous reports on the impact of leucine and leucine-rich whey protein on muscle protein synthesis and mammalian target of rapamycin (mTOR) signalling. However, there is only limited information on the effects of whey protein hydrolysates (WPH) on muscle protein synthesis and mTOR signalling. The aim of the present study was to compare the effects of WPH and amino acids on muscle protein synthesis and the initiation of translation in skeletal muscle during the post-exercise phase. Male Sprague–Dawley rats swam for 2 h to depress muscle protein synthesis. Immediately after exercise, the animals were administered either carbohydrate (CHO), CHO plus an amino acid mixture (AA) or CHO plus WPH. At 1 h after exercise, the supplements containing whey-based protein (AA and WPH) caused a significant increase in the fractional rate of protein synthesis (FSR) compared with CHO. WPH also caused a significant increase in FSR compared with AA. Post-exercise ingestion of WPH caused a significant increase in the phosphorylation of mTOR levels compared with AA or CHO. In addition, WPH caused greater phosphorylation of ribosomal protein S6 kinase and eukaryotic initiation factor 4E-binding protein 1 than AA and CHO. In contrast, there was no difference in plasma amino acid levels following supplementation with either AA or WPH. These results indicate that WPH may include active components that are superior to amino acids for stimulating muscle protein synthesis and initiating translation.


2009 ◽  
Vol 37 (1) ◽  
pp. 248-252 ◽  
Author(s):  
Deborah C.I. Goberdhan ◽  
Margret H. Ögmundsdóttir ◽  
Shubana Kazi ◽  
Bruno Reynolds ◽  
Shivanthy M. Visvalingam ◽  
...  

mTOR (mammalian target of rapamycin) plays a key role in determining how growth factor, nutrient and oxygen levels modulate intracellular events critical for the viability and growth of the cell. This is reflected in the impact of aberrant mTOR signalling on a number of major human diseases and has helped to drive research to understand how TOR (target of rapamycin) is itself regulated. While it is clear that amino acids can affect TOR signalling, how these molecules are sensed by TOR remains controversial, perhaps because cells use different mechanisms as environmental conditions change. Even the question of whether they have an effect inside the cell or at its surface remains unresolved. The present review summarizes current ideas and suggests ways in which some of the models proposed might be unified to produce an amino acid detection system that can adapt to environmental change.


2018 ◽  
Author(s):  
Björn F. Koel ◽  
David F. Burke ◽  
Stefan van der Vliet ◽  
Theo M. Bestebroer ◽  
Guus F. Rimmelzwaan ◽  
...  

AbstractWe previously showed that single amino acid substitutions at seven positions in hemagglutinin determined major antigenic change of influenza H3N2 virus. Here, the impact of two such substitutions was tested in eleven representative H3 hemagglutinins to investigate context-dependence effects. The antigenic effect of substitutions introduced at hemagglutinin position 145 was fully independent of the amino acid context of the representative hemagglutinins. Antigenic change caused by substitutions introduced at hemagglutinin position 155 was variable and context-dependent. Our results suggest that epistatic interactions with contextual amino acids in the hemagglutinin can moderate the magnitude of antigenic change.


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