Your browser doesn't support javascript.
loading
Show: 20 | 50 | 100
Results 1 - 20 de 64
Filter
1.
Am J Clin Nutr ; 116(4): 855-861, 2022 10 06.
Article in English | MEDLINE | ID: mdl-35820048

ABSTRACT

The global population is expected to reach 11 billion people by the year 2100 and will require sustainable sources of dietary protein. Most dietary protein originates from animal and terrestrial plant agriculture, which leads to deforestation, water pollution, and greenhouse gas emissions. Discovering alternative protein sources that are nutritionally adequate for the human diet without harmful environmental effects is imperative. Seaweeds are a promising option as they produce abundant protein with a low carbon footprint. Experimental evidence shows that seaweeds contain high concentrations of the essential amino acids (EAAs) necessary for human consumption, but seaweeds have yet to be evaluated with standardized metrics to compare their nutritional value to other protein sources. In this technical note, independent literature describing the EAA content and protein digestibility of 3 commonly consumed species of seaweeds was evaluated alongside traditional protein sources using a novel hybrid protein quality (HPQ) metric. HPQ is derived from the protein digestibility-corrected amino acid score and digestibility indispensable amino acid score but includes modifications to address the lack of in vivo digestibility data for seaweeds. Seaweed proteins are similar in quality to common plant protein sources such as peas, soy, and tree nuts. Furthermore, seaweed proteins from different species have complementary EAA profiles and can be mixed to form protein blends that are nutritionally on par with animal products such as milk and whey. Thus, seaweeds may be viable protein sources with a reduced footprint that provide beneficial ecosystem services.


Subject(s)
Diet , Plant Proteins, Dietary , Seaweed , Amino Acids, Essential/chemistry , Humans , Plant Proteins, Dietary/chemistry , Seaweed/chemistry , Vegetables/chemistry
2.
Molecules ; 26(16)2021 Aug 21.
Article in English | MEDLINE | ID: mdl-34443659

ABSTRACT

The content of protein, moisture content and essential amino acids in conventional and genetically modified soybean grain and selected soybean products (soybean pâté, soybean drink, soybean dessert, tofu) was analyzed in this paper. The following comparative analysis of these products has not yet been carried out. No differences were observed in the amino acid profiles of soybeans and soybean products. The presence of essential amino acids was confirmed except for tryptophan. Its absence, however, may be due not to its absence in the raw material, but to its decomposition as a result of the acid hydrolysis of the sample occurring during its preparation for amino acid determination. Regardless of the type of soybean grain, the content of protein, moisture content and essential amino acids was similar (statistically insignificant difference). Thus, the type of raw material did not determine these parameters. There was a significant imbalance in the quantitative composition of essential amino acids in individual soybean products. Only statistically significant variation was found in genetically modified and conventional soybean pâté. Moreover, in each soy product their amount was lower irrespective of the raw material from which they were manufactured. Therefore, the authors indicate the necessity of enriching soybean products with complete protein to increase their nutritional value.


Subject(s)
Amino Acids, Essential/chemistry , Edible Grain/chemistry , Glycine max/chemistry , Soybean Proteins/chemistry , Amino Acids , Humans , Nutrients/chemistry , Nutritive Value , Soy Foods/analysis
3.
Nat Prod Res ; 35(3): 399-406, 2021 Feb.
Article in English | MEDLINE | ID: mdl-31250667

ABSTRACT

The aim of this study is to prompt the recovery of industrial by-products through the production of new functional foods; it takes advantage from new throughput technologies with low environmental impact and high economic sustainability. In the field of fish processing, in order to recover the worthy protein-rich fish waste, residues from the production of Anchovies (Engraulis encrasicolus) have been converted into hydrolysate through enzymatic treatment. The obtained hydrolysate product showed a promising biological and nutritional content made by differently sized peptides and free amino acids endowed with assessed benefic effects. The study showed the possibility to produce a dry powder with an activity water (aw) of 0.3-0.5 and an essential amino acids (EAA) fraction of 42.0% over the total amino acids (TAAs). These results pave the way to the smart recovery of commercial products featured by high nutritional value, either as stand-alone items or as components of functional foods.


Subject(s)
Fish Proteins/chemistry , Protein Hydrolysates/chemistry , Protein Hydrolysates/isolation & purification , Waste Products , Amino Acids, Essential/analysis , Amino Acids, Essential/chemistry , Animals , Chromatography, High Pressure Liquid , Fishes , Food-Processing Industry , Magnetic Resonance Spectroscopy , Mass Spectrometry/methods , Nutritive Value , Peptides/chemistry , Powders
4.
Food Chem ; 333: 127503, 2020 Dec 15.
Article in English | MEDLINE | ID: mdl-32683258

ABSTRACT

Protein isolates were prepared from wet heat processed (APIp) and unprocessed alfalfa seeds (APIc) and characterized for composition and functionality at different pH. APIc and APIp exhibited high content of all the essential amino acids. Antinutrient content of APIp was lower in comparison to APIc and marked reduction in the trypsin inhibitor (85.97%) and lectin activity (100%) was observed. Processing did not cause much reduction of bioactive constituents and antioxidant activity of APIp. Alfalfa protein isolates exhibited complex polypeptide banding ranging from molecular weight of 11-75 kDa. APIp exhibited change in the conformation of protein discerned as alteration in interrelated nuances of ATR-FTIR spectra, XRD-pattern, morphology, charge on proteins and reduced solubility in comparison to APIc due to processing. APIp exhibited marked improvement in the functional properties in comparison to APIc discerned as improved hydration, surface active and gelation properties. Highest hydration and surface active properties were exhibited at pH 9.0, even though APIp at pH 7.0 showed fairly similar functional properties as APIc and APIp at pH 9.0. APIp exhibited reduced least gelation concentration in comparison to APIc at pH 7.0 and also engendered gelation at pH 4.0 and 9.0 contrary to APIc.


Subject(s)
Amino Acids, Essential/chemistry , Medicago sativa/chemistry , Plant Proteins/chemistry , Hydrogen-Ion Concentration , Medicago sativa/drug effects , Molecular Weight , Plant Proteins/isolation & purification , Solubility , Trypsin Inhibitors/chemistry
5.
J Agric Food Chem ; 68(14): 4109-4115, 2020 Apr 08.
Article in English | MEDLINE | ID: mdl-32133854

ABSTRACT

Algae products are attracting growing interest due to their pleasant taste and their high contents in protein, essential amino acids, vitamins, and minerals. Specifically, spirulina products are widely promoted for their high vitamin B12 content. So far, knowledge regarding the contamination with cyanotoxins, heavy metals, pesticides, or polycyclic aromatic hydrocarbons (PAHs) is scarce, although some studies reported high contaminant levels in spirulina products. The regular intake of spirulina, and very likely other algae products as well, as a dietary supplement in the gram range demands a closer monitoring of potentially harmful constituents.


Subject(s)
Complex Mixtures/chemistry , Nutrients/chemistry , Spirulina/chemistry , Amino Acids, Essential/chemistry , Animals , Dietary Supplements , Food Contamination , Humans , Metals, Heavy/chemistry , Minerals/chemistry , Pesticides/chemistry , Polycyclic Aromatic Hydrocarbons/chemistry , Vitamins/chemistry
6.
Food Funct ; 11(1): 493-507, 2020 Jan 29.
Article in English | MEDLINE | ID: mdl-31833513

ABSTRACT

This study investigated the effects of modulation of the amino acid profile on growth performance and gut health in weaned pigs fed an antibiotic-free, low-protein diet. In experiment 1, 5 treatments were included: a control diet with antibiotics; a low-protein diet with antibiotics; a low-protein diet without antibiotics (LP); a LP diet with 10% more dietary essential amino acids (LP110); and an LP110 diet with 12% more dietary Met + Cys, Thr and Trp. The intestinal digestive enzyme activity and morphology were improved with the increase in dietary essential amino acid levels, while the growth performance was decreased, indicating that the dietary amino acid level was too high. In experiment 2, all 5 treatments of experiment 1 were included, plus a LP diet with 5% more dietary essential amino acids (LP105) and an LP105 diet with 6% more dietary Met + Cys, Thr and Trp. The LP105 treatment showed optimal feed efficiency, a reduced plasma endotoxin concentration, and an increased fecal lactate concentration and increased abundances of Prevotellaceae and Roseburia bacteria. Our results demonstrate that the optimal amino acid profile in an antibiotic-free, low-protein diet can efficiently improve growth performance and gut health and modulate the fecal microbial structure in weaned pigs.


Subject(s)
Amino Acids, Essential/metabolism , Animal Feed/analysis , Gastrointestinal Microbiome , Swine/growth & development , Swine/metabolism , Amino Acids, Essential/chemistry , Animals , Anti-Bacterial Agents/analysis , Bacteria/classification , Bacteria/genetics , Bacteria/isolation & purification , Diet/veterinary , Diet, Protein-Restricted/veterinary , Ileum/metabolism , Ileum/microbiology , Swine/microbiology , Weaning
7.
Mar Drugs ; 17(8)2019 Aug 01.
Article in English | MEDLINE | ID: mdl-31374944

ABSTRACT

Microalgae are considered as excellent candidates for bioactive compounds, yet microalgal residues remaining after the extraction of one or two compounds are usually discarded, which is not economical. This study demonstrates the alkaline extraction of proteins from Chlorella pyrenoidosa residue after lipid and pigment extractions, and their functional properties. Single-factor experiments and response surface methodology were used to obtain the optimal conditions for protein extraction. Based on our results, a maximum protein yield of 722.70 mg/g, was obtained under the following extraction conditions: sodium hydroxide concentration 7.90%, extraction temperature 70.00 °C, extraction time 34.80 min, and microalgal residue concentration 8.20 mg/mL. The molecular weight of microalgal residue protein isolate (MRPI) was mainly distributed at the regions of 0.18-0.50 kDa, 0.50-1.50 kDa, and 1.50-5.00 kDa. The essential amino acid content was greater than the values recommended by FAO/WHO standards; a high essential amino acid index value (1.49) was another good indication that MRPI is suitable for human consumption. Moreover, MRPI exhibited excellent emulsifying properties and antioxidant activity, which suggests it may be useful as an emulsifying agent and antioxidant. These findings could improve the extraction methods of functional protein from microalgal residue and add value to microalgae-based bioactive compound production processes.


Subject(s)
Chlorella/chemistry , Microalgae/chemistry , Plant Extracts/pharmacology , Plant Proteins/pharmacology , Amino Acid Sequence , Amino Acids, Essential/chemistry , Antioxidants/chemistry , Antioxidants/isolation & purification , Antioxidants/pharmacology , Emulsifying Agents/chemistry , Emulsifying Agents/isolation & purification , Emulsifying Agents/pharmacology , Functional Food , Lipids/isolation & purification , Molecular Weight , Oxidative Stress/drug effects , Pigments, Biological/isolation & purification , Plant Extracts/chemistry , Plant Extracts/isolation & purification , Plant Proteins/chemistry , Plant Proteins/isolation & purification , Sodium Hydroxide/chemistry , Temperature
8.
J Nutr Sci Vitaminol (Tokyo) ; 65(3): 219-223, 2019.
Article in English | MEDLINE | ID: mdl-31257261

ABSTRACT

The amino acid composition table (AACT) plays a pivotal role in examining the association between dietary amino acid intake and physical conditions. The updated version, AACT 2015, has been markedly expanded; however, most additions are not based on analytical values. The Food and Agriculture Organization (FAO) of the United Nations and the World Health Organization (WHO) recommend that protein contents be calculated as the sum of amino acid residues (PROTCAA). However, due to the lack of a validated AACT, protein content calculated as reference nitrogen multiplied by a nitrogen to protein conversion factor (PROTRN) is still commonly used. In this study, validity of the estimated dietary amino acid values via the AACT 2015 was examined by comparing differences between the estimated and analytical values, for 14 consecutive days' meals provided in an elder care facility. There were no major differences between the analytical and estimated values over the 14 d; however, noticeable daily differences sometimes emerged. These results indicate that the AACT 2015 may contain accidental errors, but allows the estimation of habitual amino acid intake. In the near future, PROTCAA will become the international standard. It will be necessary to convert PROTRN values to PROTCAA to refer to past reports and data; we have determined a correction factor (0.896) for this conversion.


Subject(s)
Amino Acids, Essential , Dietary Proteins , Food Analysis , Amino Acids, Essential/analysis , Amino Acids, Essential/chemistry , Dietary Proteins/analysis , Dietary Proteins/chemistry , Food Analysis/methods , Food Analysis/standards , Humans , Meals , Nitrogen/analysis , Reproducibility of Results
9.
Isotopes Environ Health Stud ; 55(4): 366-384, 2019 Aug.
Article in English | MEDLINE | ID: mdl-31185743

ABSTRACT

Benthic invertebrates are a crucial trophic link in Arctic marine food webs. However, estimates of the contribution of different primary production sources sustaining these organisms are not well characterised. We measured the stable carbon isotope values (δ13C) of essential amino acids (EAAs) in muscle tissue from two common bivalve genera (Macoma spp. and Astarte spp.) collected in Hanna Shoal in the northeastern Chukchi Sea. Mixing models comparing the δ13CEAA fingerprints of the bivalves to a suite of primary production endmembers revealed relatively high contributions of EAAs from phytoplankton and bacteria in both species. We also examined whether δ13CEAA fingerprints could be produced from the EAAs preserved in bivalve shells, which could allow primary production sources to be estimated from ancient bivalve shells. The δ13CEAA fingerprints from a suite of paired modern bivalve shells and muscle from Macoma calcarea from across the Chukchi Sea revealed a correspondence between the estimates of the dominant primary production source of EAAs derived from analyses of these two tissue types. Our findings indicate that δ13CEAA fingerprinting of marine bivalves can be used to examine dominant organic matter sources in the Arctic marine benthos in recent years as well as in deeper time.


Subject(s)
Amino Acids, Essential/metabolism , Bivalvia/metabolism , Carbon Isotopes/analysis , Food Chain , Amino Acids, Essential/chemistry , Animal Shells/chemistry , Animals , Arctic Regions , Bivalvia/chemistry , Environmental Monitoring/methods , Models, Biological , Muscles/chemistry , Muscles/metabolism , Phytoplankton/chemistry , Phytoplankton/metabolism , Seaweed/chemistry , Seaweed/metabolism
10.
Vopr Pitan ; 87(5): 95-101, 2018.
Article in Russian | MEDLINE | ID: mdl-30592895

ABSTRACT

Almost all currently used technologies for the food production are related to the melanoidinformation reaction, which has a significant effect on appearance, taste, nutritional value and consumer properties of the foodstuffs. To assess the effect of heat treatment of food products on their nutritional value, food model systems protein hydrolyzate - glucose, hydrolyzate protein - xylose, hydrolyzate protein - fructose (1:5) have been investigated. The influence of the presence of reducing sugars, the temperature and the duration of heating on the content of amino acids and the extinction of solutions of model food systems have been studied. Linear dependences of the decrease in the total amino acid content in model food systems on the duration of the melanoidin formation reaction have been found. The loss of the total amino acid content when heating to 120 °C for 120 min was 23.9%; at the same time the content of essential amino acids reduced by 15.5-24.6%. The addition of xylose intensified the process of destruction of amino acids in the model system by 12.7%, at the same time glucose provoked the destruction of amino acids by only 2.3%. It has been established that amino acids threonine, isoleucine and histidine were unstable to destruction, regardless of the type of added sugar. When white wheat bread was heated, the loss of its nutritional value was established by reducing the content of such essential acids as threonine (by 26.5%), methionine (by 21.2%), lysine (by 13.3%) and valine (by 12,1%). It was noted that at the same temperature with increasing time of the melanoidin formation reaction, the content of amino acids in the system decreased with simultaneous intensification of the staining of the solutions. Extinction of model food systems varied according to the following equations: hydrolyzate-glucose - y = 0.0022x, hydrolyzate-xylose - y = 0.0028x, hydrolyzate-fructose - y = 0.0032x.


Subject(s)
Food Handling , Food, Formulated/analysis , Maillard Reaction , Nutritive Value , Polymers , Amino Acids, Essential/chemistry , Dietary Carbohydrates/analysis , Polymers/analysis , Polymers/chemistry , Protein Hydrolysates/analysis , Protein Hydrolysates/chemistry
11.
Int J Mol Sci ; 19(11)2018 Nov 04.
Article in English | MEDLINE | ID: mdl-30400369

ABSTRACT

Diacylglycerol acyltransferase (DGAT) is a rate-limiting enzyme in the synthesis of triacylglycerol (TAG), the most important form of energy storage in plants. Some residues have previously been proven to be crucial for DGAT1 activity. In this study, we used site-directed mutagenesis of the CeDGAT1 gene from Chlorella ellipsoidea to alter 16 amino acids to investigate effects on DGAT1 function. Of the 16 residues (L482R, E542R, Y553A, G577R, R579D, Y582R, R596D, H603D, H609D, A624R, F629R, S632A, W650R, A651R, Q658H, and P660R), we newly identified 5 (L482, R579, H603, A651, and P660) as being essential for DGAT1 function and 7 (E542, G577, R596, H609, A624, S632, and Q658) that significantly affect DGAT1 function to different degrees, as revealed by heterologous expression of the mutants in yeast strain INVSc1. Importantly, compared with CeDGAT1, expression of the mutant CeDGAT1Y553A significantly increased the total fatty acid and TAG contents of INVSc1. Comparison among CeDGAT1Y553A, GmDGAT1Y341A, AtDGAT1Y364A, BnDGAT1Y347A, and BoDGAT1Y352A, in which tyrosine at the position corresponding to the 553rd residue in CeDGAT1 is changed into alanine, indicated that the impact of changing Y to A at position 553 is specific for CeDGAT1. Overall, the results provide novel insight into the structure and function of DGAT1, as well as a mutant gene with high potential for lipid improvement in microalgae and plants.


Subject(s)
Algal Proteins/genetics , Amino Acids, Essential/metabolism , Chlorella/genetics , Diacylglycerol O-Acyltransferase/genetics , Triglycerides/biosynthesis , Algal Proteins/chemistry , Algal Proteins/metabolism , Amino Acid Sequence , Amino Acids, Essential/chemistry , Chlorella/enzymology , Cloning, Molecular , Diacylglycerol O-Acyltransferase/chemistry , Diacylglycerol O-Acyltransferase/metabolism , Fatty Acids/biosynthesis , Gene Expression , Genetic Vectors/chemistry , Genetic Vectors/metabolism , Lipid Metabolism/genetics , Mutagenesis, Site-Directed , Mutation , Recombinant Proteins/chemistry , Recombinant Proteins/genetics , Recombinant Proteins/metabolism , Saccharomyces cerevisiae/genetics , Saccharomyces cerevisiae/metabolism , Sequence Alignment , Sequence Homology, Amino Acid , Structure-Activity Relationship , Triglycerides/genetics
12.
Am J Clin Nutr ; 107(6): 984-991, 2018 06 01.
Article in English | MEDLINE | ID: mdl-29771297

ABSTRACT

Background: Recent evaluations of the risk of dietary protein deficiency have indicated that protein digestibility may be a key limiting factor in the provision of indispensable amino acids (IAAs), particularly for vulnerable populations living in challenging environments where intestinal dysfunction may exist. Since the digestion of protein occurs only in the small intestine, and the metabolic activity of colonic bacteria confounds measurements at the fecal level, there is a need to develop noninvasive protein digestibility measurements at the ileal level. Objective: We used a dual-tracer method with stable isotopes to characterize the digestibility of uniformly labeled [13C]-spirulina protein as a standard protein, in comparison to a mixture of 2H-labeled crystalline amino acids, and then demonstrated the use of this standard protein to measure the digestibility of selected legumes (chick pea and mung bean) through the use of proteins that were intrinsically labeled with 2H. Design: The digestibility of uniformly labeled [13C]-spirulina was first measured in 6 healthy volunteers (3 males and 3 females) by feeding it along with a standard mixture of 2H-labeled amino acids, in a dual-tracer, plateau-fed test meal approach. Next, intrinsically labeled legume protein digestibility was studied with a similar dual-tracer approach, with uniformly labeled [13C]-spirulina as the standard, when processed differently before consumption. Results: The average digestibility of IAA in spirulina protein was 85.2%. The average IAA digestibility of intrinsically 2H-labeled chick pea and mung bean protein was 56.6% and 57.7%, respectively. Dehulling of mung bean before ingestion increased the average IAA digestibility by 9.9% in comparison to whole mung bean digestibility. Conclusions: An innovative, minimally invasive "dual-stable-isotope" method was developed to measure protein digestibility, in which the ingestion of an intrinsically 2H-labeled test protein along with a 13C-labeled standard protein of known digestibility allows for an accurate measure of digestion and absorption of the intrinsically labeled protein. This minimally invasive method is critical to redefining protein quality and will aid in revisiting human protein requirements in different settings and in vulnerable populations. This trial was registered at Clinical Trials Registry-India as CTRI/2017/11/010468.


Subject(s)
Amino Acids, Essential/metabolism , Dietary Proteins/metabolism , Digestion/physiology , Plant Proteins/metabolism , Amino Acids, Essential/chemistry , Dietary Proteins/analysis , Female , Humans , Male , Spirulina/chemistry , Vigna/chemistry , Young Adult
13.
Clin Nutr ; 37(6 Pt A): 2076-2083, 2018 12.
Article in English | MEDLINE | ID: mdl-29066101

ABSTRACT

BACKGROUND & AIMS: It has been demonstrated that the relative content and profile of essential amino acids (EAA) play a determining role for stimulation of muscle protein synthesis (MPS) following intake of pure EAA or protein alone. METHODS: To test if this also holds in the context of mixed meals at both whole body and muscle levels, twelve older subjects (57-74 yrs) received primed continuous infusion of L-[ring-2H5]phenylalanine and L-[ring-2H2]tyrosine over a 9-h experimental period to determine whole body protein kinetics and MPS in the fasted state and following consumption of egg-based (EGG) or cereal-based (CEREAL) isocaloric and isonitrogenous breakfast. A standardized lunch, primarily consisting of beef protein was also consumed by each group. Whole body protein kinetics [protein synthesis (PS), breakdown (PB), and net balance (NB)] were expressed as changes from basal fasted period. RESULTS: We found that EGG breakfast resulted in a greater NB through a greater suppression of PB compared with the CEREAL breakfast. The greater NB during the post-breakfast period with the EGG was normalized following the standard lunch despite the sustained elevations in plasma EAA concentrations. However, the EGG breakfast stimulated both PS and PB compared with the CEREAL breakfast during the post-lunch period. MPS was not different between meals despite larges differences in the plasma EAA responses. CONCLUSIONS: We conclude that in the context of mixed meals, quality of protein affects NB through changes in protein breakdown and affects protein turnover following subsequent meal intake.


Subject(s)
Amino Acids, Essential , Breakfast/physiology , Dietary Proteins/metabolism , Aged , Amino Acids, Essential/blood , Amino Acids, Essential/chemistry , Amino Acids, Essential/metabolism , Amino Acids, Essential/pharmacokinetics , Blood Glucose/metabolism , Egg Proteins/metabolism , Female , Humans , Insulin/blood , Isotope Labeling , Male , Middle Aged , Plant Proteins, Dietary/metabolism , Tyrosine/chemistry , Tyrosine/metabolism , Tyrosine/pharmacokinetics
14.
Plant Foods Hum Nutr ; 72(4): 345-352, 2017 Dec.
Article in English | MEDLINE | ID: mdl-28900797

ABSTRACT

Chia (Salvia hispanica L.) plant is native from southern Mexico and northern Guatemala. Their seeds are a rich source of bioactive compounds which protect consumers against chronic diseases. Germination improves functionality of the seeds due to the increase in the bioactive compounds and associated antioxidant activity. The purpose of this study was to obtain functional flour from germinated chia seeds under optimized conditions with increased antioxidant activity, phenolic compounds, GABA, essential amino acids, and dietary fiber with respect to un-germinated chia seeds. The effect of germination temperature and time (GT = 20-35 °C, Gt = 10-300 h) on protein, lipid, and total phenolic contents (PC, LC, TPC, respectively), and antioxidant activity (AoxA) was analyzed by response surface methodology as optimization tool. Chia seeds were germinated inside plastic trays with absorbent paper moisturized with 50 mL of 100 ppm sodium hypochlorite dissolution. The sprouts were dried (50 °C/8 h) and ground to obtain germinated chia flours (GCF). The prediction models developed for PC, LC, TPC, and AoxA showed high coefficients of determination, demonstrating their adequacy to explain the variations in experimental data. The highest values of PC, LC, TPC, and AoxA were obtained at two different optimal conditions (GT = 21 °C/Gt = 157 h; GT = 33 °C/Gt = 126 h). Optimized germinated chia flours (OGCF) had higher PC, TPC, AoxA, GABA, essential amino acids, calculated protein efficiency ratio (C-PER), and total dietary fiber (TDF) than un-germinated chia seed flour. The OGCF could be utilized as a natural source of proteins, dietary fiber, GABA, and antioxidants in the development of new functional beverages and foods.


Subject(s)
Antioxidants/chemistry , Food Handling/methods , Germination/physiology , Salvia/chemistry , Seeds/chemistry , Amino Acids, Essential/chemistry , Antioxidants/analysis , Antioxidants/metabolism , Dietary Fiber/analysis , Flour/analysis , Food, Fortified/analysis , Lipids/analysis , Models, Theoretical , Nutritive Value , Plant Proteins/analysis , Salvia/growth & development , Salvia/metabolism , Seeds/growth & development , gamma-Aminobutyric Acid/chemistry , gamma-Aminobutyric Acid/metabolism
15.
J Biomol Struct Dyn ; 34(1): 1-14, 2016.
Article in English | MEDLINE | ID: mdl-25565373

ABSTRACT

Aspartate-semialdehyde dehydrogenase (ASADH; EC 1.2.1.11) is a key enzyme in the biosynthesis of essential amino acids in prokaryotes and fungi, inhibition of ASADH leads to the development of novel antitubercular agents. In the present work, a combined structure and ligand-based pharmacophore modeling, molecular docking, and molecular dynamics (MD) approaches were employed to identify potent inhibitors of mycobacterium tuberculosis (Mtb)-ASADH. The structure-based pharmacophore hypothesis consists of three hydrogen bond acceptor (HBA), two negatively ionizable, and one positively ionizable center, while ligand-based pharmacophore consists of additional one HBA and one hydrogen bond donor features. The validated pharmacophore models were used to screen the chemical databases (ZINC and NCI). The screened hits were subjected to ADME and toxicity filters, and subsequently to the molecular docking analysis. Best-docked 25 compounds carry the characteristics of highly electronegative functional groups (-COOH and -NO2) on both sides and exhibited the H-bonding interactions with highly conserved residues Arg99, Arg249, and His256. For further validation of docking results, MD simulation studies were carried out on two representative compounds NSC51108 and ZINC04203124. Both the compounds remain bound to the key active residues of Mtb-ASADH during the MD simulations. These identified hits can be further used for lead optimization and in the design more potent inhibitors against Mtb-ASADH.


Subject(s)
Amino Acids, Essential/chemistry , Aspartate-Semialdehyde Dehydrogenase/chemistry , Enzyme Inhibitors/chemistry , Mycobacterium tuberculosis/enzymology , Amino Acids, Essential/biosynthesis , Aspartate-Semialdehyde Dehydrogenase/genetics , Aspartate-Semialdehyde Dehydrogenase/metabolism , Hydrogen Bonding , Ligands , Molecular Docking Simulation , Molecular Dynamics Simulation , Mycobacterium tuberculosis/drug effects , Prokaryotic Cells/enzymology , Protein Conformation , Structure-Activity Relationship
16.
Chemphyschem ; 16(12): 2571-81, 2015 Aug 24.
Article in English | MEDLINE | ID: mdl-26175003

ABSTRACT

In this work we undertake a pioneer information-theoretical analysis of 18 selected amino acids extracted from a natural protein, bacteriorhodopsin (1C3W). The conformational structures of each amino acid are analyzed by use of various quantum chemistry methodologies at high levels of theory: HF, M062X and CISD(Full). The Shannon entropy, Fisher information and disequilibrium are determined to grasp the spatial spreading features of delocalizability, order and uniformity of the optimized structures. These three entropic measures uniquely characterize all amino acids through a predominant information-theoretic quality scheme (PIQS), which gathers all chemical families by means of three major spreading features: delocalization, narrowness and uniformity. This scheme recognizes four major chemical families: aliphatic (delocalized), aromatic (delocalized), electro-attractive (narrowed) and tiny (uniform). All chemical families recognized by the existing energy-based classifications are embraced by this entropic scheme. Finally, novel chemical patterns are shown in the information planes associated with the PIQS entropic measures.


Subject(s)
Amino Acids, Essential/chemistry , Information Theory , Bacteriorhodopsins/chemistry
17.
Biomed Res Int ; 2014: 359754, 2014.
Article in English | MEDLINE | ID: mdl-24605325

ABSTRACT

The effective atomic number and effective electron density in amino acids are of significant interest due to their use in various applications. The energy absorption buildup factors, exposure buildup factors, effective atomic numbers, and electron densities of essential amino acids such as Leucine (C6H13NO2), Lysine (C6H14N2O2), Methionine (C5H11NO2S), Phenylalanine (C9H11NO2), Threonine (C4H9NO3), Tryptophan (C11H12N2O2), Valine (C5H11NO2), Arginine (C6H14N4O2), and Histidine (C6H9N3O2) were determined theoretically in the energy range 0.015-15 MeV.


Subject(s)
Absorption, Physicochemical , Amino Acids, Essential/chemistry , Molecular Weight , Photons , Thermodynamics
18.
Molecules ; 19(1): 1047-59, 2014 Jan 16.
Article in English | MEDLINE | ID: mdl-24441654

ABSTRACT

Goat "sarapatel" is a product made from blood and viscera. For the first time, the microbiological and nutritional quality of "sarapatel" samples (n=48) sold under different conditions (in street markets, butcher shops, and supermarkets under refrigeration, frozen or at room temperature) was evaluated. Goat "sarapatel" is a nutritive food, with each 100 g providing, on average, 72 g of moisture, 2 g of ash, 18 g of protein, 9 g of lipids, 2 g of carbohydrates, 282 mg of cholesterol, and high amounts of unsaturated fatty acids and essential amino acids. The analysis of the "sarapatel" samples shows that none of them contain Salmonella spp. or L. monocytogenes. High counts (>104) of total coliforms, thermotolerant coliforms, and sulfite-reducing Clostridium were detected, and coagulase-positive Staphylococcus was found in 31.25% of samples. The storage conditions evaluated (refrigeration, frozen or at room temperature) did not affect the physicochemical quality of the "sarapatel"; however, the unsatisfactory microbiological quality indicates that it is necessary to improve the health-sanitary aspects of the processing and sale of this product.


Subject(s)
Food Microbiology , Meat Products/microbiology , Amino Acids, Essential/analysis , Amino Acids, Essential/chemistry , Animals , Cholesterol/analysis , Cholesterol/chemistry , Clostridium/isolation & purification , Dietary Proteins/analysis , Dietary Proteins/chemistry , Fatty Acids, Unsaturated/analysis , Fatty Acids, Unsaturated/chemistry , Food Storage , Goats , Humans , Listeria monocytogenes/isolation & purification , Meat Products/analysis , Salmonella/isolation & purification , Staphylococcus/isolation & purification
19.
Adv Exp Med Biol ; 788: 25-33, 2013.
Article in English | MEDLINE | ID: mdl-23835954

ABSTRACT

Exposure to cigarette smoke (CS) and cigarette smoking have been shown to promote catabolism of skeletal muscle. Previous studies and recent findings from our laboratory have demonstrated the involvement of the ubiquitin proteasome system and the muscle-specific E3 ubiquitin ligases MAFbx/atrogin-1 and MuRF1 in CS induced skeletal muscle catabolism. The essential amino acid leucine is a known anticatabolic agent that improves skeletal muscle metabolism in various atrophic conditions. To examine the protective effect of leucine and proteasome inhibition in CS induced muscle catabolism, C2 myotubes, from an in vitro skeletal muscle cell line, were exposed to CS in the presence or absence of leucine and a proteasome inhibitor, MG132. Diameter of myotubes, levels of the main contractile proteins - myosin heavy chain and actin, expression of MAFbx/atrogin-1 and MuRF1 were studied by microscopy, Western blotting, and qPCR. Leucine pretreatment prevented the CS-induced reduction in diameter of myotubes and degradation of myosin heavy chain by suppressing the upregulation of MAFbx/atrogin-1 and MuRF1. MG132 also attenuated the CS-induced decrease in diameter of myotubes and degradation of myosin heavy chain. Our findings demonstrate that supplementation with the essential amino acid leucine and inhibition of the proteasome may protect skeletal muscle from CS induced catabolism.


Subject(s)
Amino Acids, Essential/chemistry , Leucine/chemistry , Leupeptins/pharmacology , Muscle Fibers, Skeletal/drug effects , Proteasome Inhibitors/pharmacology , Smoke/adverse effects , Animals , Cell Line , Gene Expression Regulation , Metabolism , Mice , Myosin Heavy Chains/metabolism , Proteasome Endopeptidase Complex/metabolism , Tobacco Products/adverse effects
20.
Oecologia ; 173(1): 1-12, 2013 Sep.
Article in English | MEDLINE | ID: mdl-23297046

ABSTRACT

The nutritional value of alternative host plants for leaf-feeding insects such as caterpillars is commonly measured in terms of protein quantity. However, nutritional value might also depend on the quality of the foliar protein [i.e., the composition of essential amino acids (EAAs)]. A lack of comparative work on the EAA compositions of herbivores and their host plants has hampered the testing of this hypothesis. We tested the "protein quality hypothesis" using the tree-feeding caterpillars of Lymantria dispar (gypsy moth) and two taxonomically unrelated host plants, red oak (Quercus rubra) and sugar maple (Acer saccharum). Because L. dispar has higher fitness on oak than on maple, support for the hypothesis would be found if protein were of higher quality from oak than from maple. The whole-body EAA composition of L. dispar larvae was measured to estimate its optimum dietary protein composition, which was compared with the EAA compositions of oak and maple leaves. Contrary to the protein quality hypothesis, the EAA compositions of oak and maple were not significantly different in the spring. The growth-limiting EAAs in both tree species were histidine and methionine. Similar results were observed in the summer, with the exception that the histidine composition of oak was between 10 and 15 % greater than in maple leaves. The two main factors that affected the nutritional value of protein from the tree species were the quantities of EAAs, which were consistently higher in oak, and the efficiency of EAA utilization, which decreased from 80 % in May to <50 % in August. We conclude that the relative nutritional value of red oak and sugar maple for L. dispar is more strongly affected by protein quantity than quality. Surveys of many wild herbaceous species also suggest that leaf-feeding insects would be unlikely to specialize on plants based on protein quality.


Subject(s)
Acer/metabolism , Amino Acids, Essential/metabolism , Moths/physiology , Nutritive Value , Plant Proteins/metabolism , Quercus/metabolism , Acer/chemistry , Amino Acids, Essential/chemistry , Animals , Body Size , Feeding Behavior , Larva/growth & development , Larva/metabolism , Moths/growth & development , Moths/metabolism , Plant Leaves/chemistry , Plant Leaves/metabolism , Quercus/chemistry
SELECTION OF CITATIONS
SEARCH DETAIL