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1.
Rev Argent Microbiol ; 46(1): 58-65, 2014.
Article in Spanish | MEDLINE | ID: mdl-24721277

ABSTRACT

There is a great variety of fermented milks containing lactic acid bacteria that present health-promoting properties. Milk proteins are hydrolyzed by the proteolytic system of these microorganisms producing peptides which may also perform other functions in vivo. These peptides are encrypted within the primary structure of proteins and can be released through food processing, either by milk fermentation or enzymatic hydrolysis during gastrointestinal transit. They perform different activities, since they act in the cardiovascular, digestive, endocrine, immune and nervous systems. Bioactive peptides that have an antihypertensive, antithrombotic, antioxidant and hypocholesterolemic effect on the cardiovascular system can reduce the risk factors for chronic disease manifestation and help improve human health. Most studied bioactive peptides are those which exert an antihypertensive effect by inhibiting the angiotensin-converting enzyme (ACE). Recently, the study of these peptides has focused on the implementation of tests to prove that they have an effect on health. This paper focuses on the production of ACEinhibitory antihypertensive peptides from fermented milks, its history, production and in vivo tests on rats and humans, on which its hypotensive effect has been shown.


Subject(s)
Cultured Milk Products , Hypertension/diet therapy , Angiotensin-Converting Enzyme Inhibitors/isolation & purification , Animals , Bifidobacterium/enzymology , Cattle , Cultured Milk Products/enzymology , Cultured Milk Products/microbiology , Humans , Lactobacillus/enzymology , Lactococcus/enzymology , Milk Proteins/metabolism , Peptides/pharmacokinetics , Peptides/pharmacology , Rats , Streptococcus/enzymology
2.
Rev. argent. microbiol ; 46(1): 58-65, mar. 2014. tab
Article in Spanish | BINACIS | ID: bin-131909

ABSTRACT

Existe una gran variedad de leches fermentadas con bacterias lácticas, con propiedades que promueven la salud. Recientemente se ha comunicado que las proteínas de los alimentos pueden, además, ejercer otras funciones in vivo, por medio de sus péptidos con actividad biológica. Estos péptidos se encuentran encriptados dentro de la estructura primaria de las proteínas y pueden ser liberados por fermentación de la leche, hidrólisis enzimática, o bien durante el tránsito gastrointestinal. Las funciones que presentan son diversas, ya que pueden actuar en diferentes sistemas del cuerpo humano: el cardiovascular, el digestivo, el endocrino, el inmune y el nervioso. Los péptidos bioactivos que presentan un efecto en el sistema cardiovascular (antihipertensivo, antitrombótico, antioxidante o hipocolesterolémico) pueden reducir los factores de riesgo para la manifestación de enfermedades crónicas y ayudar a mejorar la salud humana. Los péptidos bioactivos más estudiados son aquellos que ejercen un efecto antihipertensivo a través de la inhibición de la enzima convertidora de angiotensina (ACE). Este documento se enfoca en la producción de péptidos antihipertensivos inhibidores de la ACE en leches fermentadas, en su historia, y en las pruebas in vivo realizadas en ratas y en humanos, donde se ha demostrado su efecto hipotensor.(AU)


There is a great variety of fermented milks containing lactic acid bacteria that present health-promoting properties. Milk proteins are hydrolyzed by the proteolytic system of these microorganisms producing peptides which may also perform other functions in vivo. These peptides are encrypted within the primary structure of proteins and can be released through food processing, either by milk fermentation or enzymatic hydrolysis during gastrointestinal transit. They perform different activities, since they act in the cardiovascular, digestive, endocrine, immune and nervous systems. Bioactive peptides that have an antihypertensive, antithrombotic, antioxidant and hypocholesterolemic effect on the cardiovascular system can reduce the risk factors for chronic disease manifestation and help improve human health. Most studied bioactive peptides are those which exert an antihypertensive effect by inhibiting the angiotensin-converting enzyme (ACE). Recently, the study of these peptides has focused on the implementation of tests to prove that they have an effect on health. This paper focuses on the production of ACEinhibitory antihypertensive peptides from fermented milks, its history, production and in vivo tests on rats and humans, on which its hypotensive effect has been shown.(AU)


Subject(s)
Animals , Cattle , Humans , Rats , Cultured Milk Products , Hypertension/diet therapy , Angiotensin-Converting Enzyme Inhibitors/isolation & purification , Bifidobacterium/enzymology , Cultured Milk Products/enzymology , Cultured Milk Products/microbiology , Lactobacillus/enzymology , Lactococcus/enzymology , Milk Proteins/metabolism , Peptides/pharmacokinetics , Peptides/pharmacology , Streptococcus/enzymology
3.
Rev. argent. microbiol ; 46(1): 58-65, mar. 2014. tab
Article in Spanish | LILACS | ID: lil-708697

ABSTRACT

Existe una gran variedad de leches fermentadas con bacterias lácticas, con propiedades que promueven la salud. Recientemente se ha comunicado que las proteínas de los alimentos pueden, además, ejercer otras funciones in vivo, por medio de sus péptidos con actividad biológica. Estos péptidos se encuentran encriptados dentro de la estructura primaria de las proteínas y pueden ser liberados por fermentación de la leche, hidrólisis enzimática, o bien durante el tránsito gastrointestinal. Las funciones que presentan son diversas, ya que pueden actuar en diferentes sistemas del cuerpo humano: el cardiovascular, el digestivo, el endocrino, el inmune y el nervioso. Los péptidos bioactivos que presentan un efecto en el sistema cardiovascular (antihipertensivo, antitrombótico, antioxidante o hipocolesterolémico) pueden reducir los factores de riesgo para la manifestación de enfermedades crónicas y ayudar a mejorar la salud humana. Los péptidos bioactivos más estudiados son aquellos que ejercen un efecto antihipertensivo a través de la inhibición de la enzima convertidora de angiotensina (ACE). Este documento se enfoca en la producción de péptidos antihipertensivos inhibidores de la ACE en leches fermentadas, en su historia, y en las pruebas in vivo realizadas en ratas y en humanos, donde se ha demostrado su efecto hipotensor.


There is a great variety of fermented milks containing lactic acid bacteria that present health-promoting properties. Milk proteins are hydrolyzed by the proteolytic system of these microorganisms producing peptides which may also perform other functions in vivo. These peptides are encrypted within the primary structure of proteins and can be released through food processing, either by milk fermentation or enzymatic hydrolysis during gastrointestinal transit. They perform different activities, since they act in the cardiovascular, digestive, endocrine, immune and nervous systems. Bioactive peptides that have an antihypertensive, antithrombotic, antioxidant and hypocholesterolemic effect on the cardiovascular system can reduce the risk factors for chronic disease manifestation and help improve human health. Most studied bioactive peptides are those which exert an antihypertensive effect by inhibiting the angiotensin-converting enzyme (ACE). Recently, the study of these peptides has focused on the implementation of tests to prove that they have an effect on health. This paper focuses on the production of ACEinhibitory antihypertensive peptides from fermented milks, its history, production and in vivo tests on rats and humans, on which its hypotensive effect has been shown.


Subject(s)
Animals , Cattle , Humans , Rats , Cultured Milk Products , Hypertension/diet therapy , Angiotensin-Converting Enzyme Inhibitors/isolation & purification , Bifidobacterium/enzymology , Cultured Milk Products/enzymology , Cultured Milk Products/microbiology , Lactobacillus/enzymology , Lactococcus/enzymology , Milk Proteins/metabolism , Peptides/pharmacokinetics , Peptides/pharmacology , Streptococcus/enzymology
4.
Rev. Argent. Microbiol. ; 46(1): 58-65, 2014 Jan-Mar.
Article in Spanish | BINACIS | ID: bin-133710

ABSTRACT

There is a great variety of fermented milks containing lactic acid bacteria that present health-promoting properties. Milk proteins are hydrolyzed by the proteolytic system of these microorganisms producing peptides which may also perform other functions in vivo. These peptides are encrypted within the primary structure of proteins and can be released through food processing, either by milk fermentation or enzymatic hydrolysis during gastrointestinal transit. They perform different activities, since they act in the cardiovascular, digestive, endocrine, immune and nervous systems. Bioactive peptides that have an antihypertensive, antithrombotic, antioxidant and hypocholesterolemic effect on the cardiovascular system can reduce the risk factors for chronic disease manifestation and help improve human health. Most studied bioactive peptides are those which exert an antihypertensive effect by inhibiting the angiotensin-converting enzyme (ACE). Recently, the study of these peptides has focused on the implementation of tests to prove that they have an effect on health. This paper focuses on the production of ACEinhibitory antihypertensive peptides from fermented milks, its history, production and in vivo tests on rats and humans, on which its hypotensive effect has been shown.


Subject(s)
Cultured Milk Products , Hypertension/diet therapy , Angiotensin-Converting Enzyme Inhibitors/isolation & purification , Animals , Bifidobacterium/enzymology , Cattle , Cultured Milk Products/enzymology , Cultured Milk Products/microbiology , Humans , Lactobacillus/enzymology , Lactococcus/enzymology , Milk Proteins/metabolism , Peptides/pharmacokinetics , Peptides/pharmacology , Rats , Streptococcus/enzymology
5.
Anal Bioanal Chem ; 405(11): 3813-22, 2013 Apr.
Article in English | MEDLINE | ID: mdl-23263517

ABSTRACT

A new and simple-to-prepare hypoxanthine biosensor has been developed using xanthine oxidase (XOD) immobilised on carbon electrode surfaces. XOD was immobilised by glutaraldehyde cross-linking on carbon film (CF) electrodes and on carbon nanotube (CNT) modified CF (CNT/CF). A comparison of the performance of the two configurations was carried out by the current response using amperometry at fixed potential; the best characteristics being exhibited by XOD/CNT/CF modified electrodes. The effects of electrolyte pH and applied potential were evaluated, and a proposal is made for the enzyme mechanism of action involving competition between regeneration of flavin adenine dinucleotide and reduction of hydrogen peroxide. Under optimised conditions, the determination of hypoxanthine was carried out at -0.2 V vs. a saturated calomel electrode (SCE) with a detection limit of 0.75 µM on electrodes with CNT and at -0.3 V vs. SCE with a detection limit of 0.77 µM on electrodes without CNT. The applicability of the biosensor was verified by performing an interference study, reproducibility and stability were investigated, and hypoxanthine was successfully determined in sardine and shrimp samples.


Subject(s)
Biosensing Techniques/instrumentation , Cultured Milk Products/enzymology , Enzymes, Immobilized/chemistry , Hypoxanthine/analysis , Nanotubes, Carbon/chemistry , Xanthine Oxidase/chemistry , Carbon/chemistry , Electrodes , Limit of Detection , Models, Molecular
6.
J Dairy Sci ; 93(3): 884-92, 2010 Mar.
Article in English | MEDLINE | ID: mdl-20172208

ABSTRACT

Angiotensin I-converting enzyme (ACE) inhibitory activities in untreated koumiss and koumiss digested with ACE, pepsin, trypsinase, and chymotrypsin were compared and analyzed. Four novel ACE inhibitory peptides (P(I), P(K), P(M), and P(P)) were purified using ultrafiltration and high performance liquid chromatography (HPLC). The classification study showed that these 4 peptides were of the true inhibitor type. The amino acid sequences of these peptides are YQDPRLGPTGELDPATQPIVAVHNPVIV, PKDLREN, LLLAHLL, and NHRNRMMDHVH, respectively. Their individual IC(50) (50% inhibitory concentration) values were as follows: 14.53+/-0.21microM, 9.82+/-0.37microM, 5.19+/-0.18microM, and 13.42+/-0.17microM. From sequence analysis, we determined that P(I) was part of beta-casein in mare's milk. The 3 peptides P(K), P(M), and P(P) did not correspond with any known milk protein. The results suggest that koumiss is rich in ACE inhibitory peptides, and the ACE inhibitors in koumiss are of the pro-drug type or a mixture of the pro-drug type and the true inhibitor type. These results may provide evidence about the beneficial effects of koumiss, especially on cardiovascular health.


Subject(s)
Angiotensin-Converting Enzyme Inhibitors/analysis , Cultured Milk Products/enzymology , Peptides/analysis , Amino Acid Sequence , Angiotensin-Converting Enzyme Inhibitors/chemistry , Animals , Chromatography, Reverse-Phase , Cultured Milk Products/microbiology , Female , Filtration , Horses , Molecular Weight , Peptides/chemistry
7.
Molecules ; 10(10): 1298-306, 2005 Oct 31.
Article in English | MEDLINE | ID: mdl-18007523

ABSTRACT

Synthesis of several pryrazolo[4,3-e][1,2,4]-triazines is described. The absorption spectrum of some 5-substituted derivatives was found to extend to the visible region. These compounds were found to inhibit some enzymes of purine metabolism, like xanthine oxidase or bacterial purine-nucleoside phosphorylase with Ki values in the 10(-3) -10(-5) M range.


Subject(s)
Light , Purines/chemistry , Pyrazoles/chemistry , Triazines/chemistry , Absorption , Animals , Cattle , Cultured Milk Products/enzymology , Drug Evaluation , Enzyme Inhibitors/chemistry , Enzyme Inhibitors/pharmacology , Escherichia coli/enzymology , Guanine Deaminase/antagonists & inhibitors , Guanine Deaminase/metabolism , Models, Biological , Muscles/enzymology , Purine-Nucleoside Phosphorylase/antagonists & inhibitors , Purine-Nucleoside Phosphorylase/metabolism , Purines/metabolism , Purines/pharmacology , Pyrazoles/pharmacology , Rabbits , Triazines/pharmacology , Xanthine Oxidase/antagonists & inhibitors , Xanthine Oxidase/metabolism
8.
Biomacromolecules ; 5(2): 547-52, 2004.
Article in English | MEDLINE | ID: mdl-15003019

ABSTRACT

In this study, the antioxidant property of (+)-catechin-aldehyde polycondensates has been examined. Superoxide anions are one of the most typical reactive oxygen species (ROS) and generated by xanthine oxidase (XO). The measurements of the superoxide anion scavenging and XO inhibition activity showed that catechin had pro-oxidant properties in lower concentrations and little XO inhibition. On the other hand, the polycondensates exhibited much higher effects compared to the catechin monomer, and their physiological activities were greatly affected by the structure of polycondensates. Steady-state analysis of the inhibition against XO showed that the inhibition type of the polycondensate was uncompetitive. Furthermore, the results of the circular dichroism and UV-visible measurements of a mixture of the polycondensate and XO were in good agreement with that of the steady-state analysis; the spectral changes due to the chelation of the polycondensate onto the Fe/S and/or the FAD center of XO were observed. These data strongly suggest that the polycondensates possess a great potential as antioxidant for various applications.


Subject(s)
Antioxidants/metabolism , Catechin/metabolism , Free Radical Scavengers/metabolism , Superoxides/metabolism , Xanthine Oxidase/antagonists & inhibitors , Aldehydes/analysis , Aldehydes/chemistry , Aldehydes/metabolism , Antioxidants/analysis , Antioxidants/chemistry , Catechin/analysis , Catechin/chemistry , Cultured Milk Products/enzymology , Enzyme Inhibitors/analysis , Enzyme Inhibitors/chemistry , Enzyme Inhibitors/metabolism , Free Radical Scavengers/analysis , Free Radical Scavengers/chemistry , Superoxides/analysis , Superoxides/chemistry , Xanthine Oxidase/metabolism
9.
Commun Agric Appl Biol Sci ; 68(2 Pt B): 465-8, 2003.
Article in English | MEDLINE | ID: mdl-24757787

ABSTRACT

The effect of coagulation conditions of raw, skimmed and pasteurized milk on the transfer of commercial enzymatic preparations (Chymogen, Fromase and Hala) to cheese grain, was studied. It was found that the transfer degree of the above preparations was dependent on some coagulation parameters such as milk acidity and temperature. The duration of cheese grain retention did not have a significant effect on the transfer of the analyzed preparations.


Subject(s)
Cheese/analysis , Cultured Milk Products/enzymology , Food Handling/methods , Milk Proteins/metabolism , Animals , Cheese/microbiology , Cultured Milk Products/chemistry , Food-Processing Industry , Hydrogen-Ion Concentration
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