ABSTRACT
Advanced glycation end products (AGEs) are potentially-hazardous chemical compounds, produced by the Maillard reaction between reducing sugars and Lysine side-chain amino groups in proteins. AGEs are strongly associated with diabetes, Alzheimer's disease and atherosclerosis. Pyrraline, a sugar derivative of Lysine, is a major AGE and an established marker for the presence of dietary AGEs. In this study, the effects of NaCl and different dipeptide and tripeptide structures were compared on the formation of pyrraline-containing peptides and the glucose derivative 3-deoxyglucosone in the presence of glucose and at different NaCl concentrations. The physicochemical properties (polarizability, dipole moment, molecular volume and dissociation constant) and the thermodynamic properties of the peptides were determined. The amount of the pyrraline decreased significantly in the following order of peptides (at the same concentrations): Lys-Phe > Lys-Ala > Lys-Gly; Lys-Gly-Phe > Lys-Gly-Ala > Lys-Gly-Gly. The highest levels of both pyrraline and 3-deoxyglucosone occurred at 0.2 mol/L Na+. Sodium ions appear to alter the intramolecular electron density and charge distribution of the peptides and facilitate the reaction by stabilizing some of the intermediates in the reaction sequence.
ABSTRACT
ABSTRACT: Vibrio cholerae can cause pandemic cholera in humans. The bacterium resides in aquatic environments worldwide. Continuous testing of V. cholerae contamination in water and aquatic products is imperative for food safety control and human health. In this study, a rapid and visualized method was developed for the first time based on loop-mediated isothermal amplification (LAMP) for detection of the important virulence-related genes ace, zot, cri, and nanH for toxins and the infectious process of V. cholerae. Three pairs of molecular probes targeting each of these genes were designed and synthesized. The one-step LAMP reaction was conducted at 65°C for 40 min. Positive results were inspected by the production of a light green color under visible light or green fluorescence under UV light (302 nm). Limit of detection of the LAMP method ranged from 1.85 to 2.06 pg per reaction of genomic DNA or 2.50 × 100 to 4.00 × 102 CFU per reaction for target genes of cell culture of V. cholerae, which was more sensitive than standard PCR. Inclusivity and exclusivity of the LAMP method were 100% for all target genes. The method showed similar high efficiency to a certain extent in rapid testing of spiked or collected specimens of water and aquatic products. Target genes were detected by absence from all water samples from various sources. However, high occurrences of the nanH gene were observed in intestinal samples derived from four species of fish and one species of shellfish, indicating a risk of potentially toxic V. cholerae in commonly consumed aquatic products. The results in this study provide a potential tool for rapid and visualized detection of V. cholerae in water and aquatic products.
Subject(s)
Vibrio cholerae , Animals , Molecular Diagnostic Techniques , Nucleic Acid Amplification Techniques/methods , Sensitivity and Specificity , Vibrio cholerae/genetics , Virulence , WaterABSTRACT
Amino acids are the structural units (monomers) that make up proteins and play many critical roles in human diets with or without food processing. In this study, corn starch (CS) mixed with Lys, Ser, Ala, or Asp were subjected to heat moisture treatment (HMT) or annealing (ANN). We evaluated the morphological properties, swelling power, pasting properties, thermal properties, crystallinity structure, and in vitro digestibility of CS and CS-AA complexes. HMT increased the gelatinization temperatures and retarded the retrogradation for CS with or without AAs, while ANN had little impact on gelatinization temperature and promoted the recrystallization. Generally, HMT samples were more enzyme resistant than the ANN samples. For the uncooked samples, the addition of Ser, Ala, and Asp decreased rapidly digestible starch (RDS) and slowly digestible starch (SDS) contents, but increased resistant starch (RS) content. Compared with the control (CS without AA), CS-AA complexes had lower contents of RDS following HMT. Under ANN, CS-AAs had higher content of RDS compared with the control. In all groups (physically mixed, HMT, and ANN) with cooked samples, the addition of different AAs decreased the contents of RDS and increased RS contents to varying degrees.
Subject(s)
Amino Acids/chemistry , Starch/chemistry , TemperatureABSTRACT
Advanced glycation end products (AGEs), which are closely associated with various chronic diseases, are formed through the Maillard reaction when aldehydes react with amines in heated foods or in living organisms. The fate of dietary AGEs after oral intake plays a crucial role in regulating the association between dietary AGEs and their biological effects. However, the complexity and diversity of dietary AGEs make their fate ambiguous. Glycated modifications can impair the digestion, transport and uptake of dietary AGEs. High and low molecular weight AGEs may exhibit individual differences in their distribution, metabolism and excretion. Approximately 50-60% of free AGEs are excreted after dietary intake, whereas protein-bound AGEs exhibit a limited excretion rate. In this article, we summarize several AGE classification criteria and their abundance in foods, and in the body. A standardized static in vitro digestion method is strongly recommended to obtain comparable results of AGE digestibility. Sophisticated hypotheses regarding the intestinal transportation and absorption of drugs, as well as calculated physicochemical parameters, are expected to alleviate the difficulties determining the digestion, transport and uptake of dietary AGEs. Orally supplied AGEs with low or high molecular weights must be supported by well-defined amounts in investigations of excretion. Furthermore, unequivocal evidence should be obtained regarding the degradation and metabolism products of dietary AGEs.
Subject(s)
Diet , Glycation End Products, Advanced , Food , Maillard ReactionABSTRACT
Amino acids (AAs) are increasingly applied as nutrient supplements and played a crucial role in human nutrition and health maintenance. The objectives were to evaluate the effects of different AAs on the physicochemical and digestive properties of potato starch (PS); and investigate whether heat moisture treatment (HMT) or annealing (ANN) had different impacts on the complexes between starch and AAs. PS mixed with different AAs, represented by Lys, Ser, Ala, and Asp, were modified by HMT and ANN. Both different AAs addition and hydrothermal treatments significantly increased the pasting and gelatinization temperatures, and decreased swelling power, peak viscosity and enthalpy change for physically mixed samples. In general, different AAs retarded the recrystallization of PS, while hydrothermal treatments promoted retrogradation of PS. The addition of different AAs decreased the RDS and increased RS contents for all cooked samples. Electrostatic interactions between PS with phosphate-monoester derivatives and different charge-carrying AAs formed during hydrothermal treatments, resulting in modify physicochemical and digestive properties of PS. HMT showed greater influence on physicochemical and digestive properties of PS-AA complexes than ANN. This study will enrich interaction theory between starch and AAs, and improve the nutritional values of PS-based products during food thermal processing.
Subject(s)
Amino Acids/chemistry , Digestion , Solanum tuberosum/chemistry , Starch/chemistry , Food Handling/methods , Gelatin/chemistry , Hot Temperature , Power, Psychological , Temperature , Thermodynamics , Viscosity , Water , X-Ray DiffractionABSTRACT
Advanced glycation end products (AGEs), which are present in heat-processed foods, have been associated with several chronic diseases. Sodium chloride (NaCl) modulates the formation of furfurals and acrylamide in the Maillard reaction; however, the effects of NaCl on AGE formation are inconsistent. In this study, we investigated the effects of NaCl on pyrraline formation using glucose-lysine model systems. NaCl, especially at 0.50%, promoted Maillard browning and pyrraline formation, with a simultaneous increase in the 3-deoxyglucosone concentration. To reduce the rate of pyrraline formation, NaCl coated with different gums and starches were used. The results showed that NaCl encapsulation is an effective approach to mitigate pyrraline and 3-deoxyglucosone formation. The content of NaCl in the microparticles were 284 ± 12, 269 ± 6, 258 ± 8, 247 ± 10, 273 ± 16, and 288 ± 15 mg/g (coated with waxy maize starch, normal maize starch, HYLON VII high amylose maize starch, gelatinized resistant starch, xanthan gum, and gum arabic, respectively). The heat resistance of the coating material was negatively correlated with the pyrraline and 3-deoxyglucosone formation, whereas the solubility of the coating material had the opposite results. Coating the material with gum had little effects on the reduction of pyrraline and 3-deoxyglucosone.
Subject(s)
Glucose/genetics , Glycation End Products, Advanced/genetics , Norleucine/analogs & derivatives , Pyrroles/chemistry , Sodium Chloride/chemistry , Amylose/chemistry , Amylose/genetics , Deoxyglucose/analogs & derivatives , Deoxyglucose/chemistry , Deoxyglucose/genetics , Glucose/chemistry , Glycation End Products, Advanced/chemistry , Hot Temperature , Lysine/chemistry , Lysine/genetics , Maillard Reaction , Norleucine/chemistry , Norleucine/metabolism , Pyrroles/metabolism , Sodium Chloride/metabolism , Zea mays/geneticsABSTRACT
Interactions among food components during food processing play important role in starch digestibility. The objective of this study was to investigate the effects of heat moisture treatment on the structural, physicochemical, and digestibility properties of starch-soybean peptide complexes. Corn and potato starch mixed with different amounts of soybean peptide were subjected to heat moisture treatment. The addition of soybean peptide increased pasting temperature, while decreased peak viscosity and swelling power in both starch samples under heat moisture treatment. Thermal analysis showed that soybean peptide retarded starch gelatinization, and heat moisture treatment contributed to a more stable crystalline structure. Lower RDS contents and higher RS contents were associated with higher soybean peptide amounts. Potato starch was more sensitive to heat moisture treatment than corn starch. The results will enrich the interaction theory between starch and protein, and will be important for the development of carbohydrate-restricted diet and protein-based functional foods.
Subject(s)
Soybean Proteins/chemistry , Soybean Proteins/pharmacokinetics , Starch/chemistry , Starch/pharmacokinetics , Digestion , Food Handling/methods , Hot Temperature , Peptides/chemistry , Peptides/pharmacokinetics , Solanum tuberosum/chemistry , Viscosity , Zea mays/chemistryABSTRACT
The objective of this study was to investigate the porcine pancreatic α-amylase (PPA) inhibitory activity of botanical food proteins, represented by soy protein isolate (SPI) and wheat gluten protein (WGP). The half maximal inhibitory concentration (IC50) was determined, and the kinetics of inhibition were investigated using Dixon, Cornish-Bowden, and Lineweaver-Burk plots. The results showed WGP functioned as mixed-type inhibitors with both competitive and uncompetitive inhibitory characteristics, while SPI showed competitive inhibitory effects on α-amylase. The competitive inhibition constants (Kic) of WGP and SPI were 5.753 and 30.212â¯mg/mL, respectively, and the uncompetitive inhibition constants (Kiu) of WGP was 45.110â¯mg/mL, respectively. The IC50 values of WGP and SPI were 3.086 and 33.899â¯mg/mL, respectively. For WGP, the lower Kic vs. Kiu for mixed-type inhibitors suggested that they bound more tightly to free PPA than the PPA-starch complex. Compared with SPI, WGP displayed a stronger inhibitory effect on α-amylase. These results indicated that SPI and WGP may delay the digestion of starchy foods by inhibiting starch hydrolytic enzymes, which may be of relevance in vivo during gastrointestinal digestion. The findings are also of important practical value for the development of carbohydrate-restricted diet and protein-based functional foods.
Subject(s)
Enzyme Inhibitors/pharmacology , Glutens/pharmacology , Soybean Proteins/isolation & purification , Soybean Proteins/pharmacology , Triticum/chemistry , alpha-Amylases/antagonists & inhibitors , Hydrolysis/drug effects , Kinetics , Starch/metabolism , Zea mays/chemistryABSTRACT
LW-1 is a collagen-linked blue fluorophore whose skin levels increase with age, diabetes and end-stage renal disease (ESRD), and correlate with the long-term progression of microvascular disease and indices of subclinical cardiovascular disease in type 1 diabetes. The chemical structure of LW-1 is still elusive, but earlier NMR analyses showed it has a lysine residue in an aromatic ring coupled to a sugar molecule reminiscent of advanced glycation end-products (AGEs). We hypothesized and demonstrate here that the unknown sugar is a N-linked glucuronic acid. LW-1 was extracted and highly purified from ~99 g insoluble skin collagen obtained at autopsy from patients with diabetes/ESRD using multiple rounds of proteolytic digestion and purification by liquid chromatography (LC). Advanced NMR techniques (1H-NMR, 13C-NMR, 1H-13C HSQC, 1H-1H TOCSY, 1H-13C HMBC) together with LC-mass spectrometry (MS) revealed a loss of 176 amu (atomic mass unit) unequivocally point to the presence of a glucuronic acid moiety in LW-1. To confirm this data, LW-1 was incubated with ß-glycosidases (glucosidase, galactosidase, glucuronidase) and products were analyzed by LC-MS. Only glucuronidase could cleave the sugar from the parent molecule. These results establish LW-1 as a glucuronide, now named glucuronidine, and for the first time raise the possible existence of a "glucuronidation pathway of diabetic complications". Future research is needed to rigorously probe this concept and elucidate the molecular origin and biological source of a circulating glucuronidine aglycone.
Subject(s)
Collagen/metabolism , Diabetes Complications/metabolism , Glucuronic Acid/metabolism , Adult , Aged , Aged, 80 and over , Collagen/chemistry , Glycation End Products, Advanced/metabolism , Humans , Middle Aged , Skin/metabolismABSTRACT
Pyrraline, an advanced glycation end product (AGE), is related to some chronic diseases and can be employed as an indicator for heat damage in food processing. In this study, the impact of changing the reactant concentration and ratio on the kinetic parameters describing peptide-bound pyrraline (pep-pyr) formation and elimination was evaluated in the Lys-Gly/glucose model systems, with microwave heating treatment ranging from 120 to 200 °C. The maximum pep-pyr concentration increased as follows: 200 °C Ë 180 °C Ë 160 °C Ë 120 °C Ë 140 °C. First, the pep-pyr formation and elimination was modeled by using a single-response modelling. The formation rate constant (kF ) of pep-pyr was independent of the initial concentration of the reactants and ratios. However, the elimination rate constant of pep-pyr (kE ) increased with increasing reactant concentrations. Second, a multiresponse modelling was performed to illustrate the pathways of pep-pyr formation and elimination. Two adapted models can fit to the experimental data with the goodness-of-fit ranging from 0.663 to 0.920. Glucose-to-fructose isomerization rather than glucose-to-mannose epimerization was detected in an equimolar model system and the model system with an excess of any of the reactants. The caramelization reaction was negligible in the equimolar systems and the model systems with an excess of peptide. The reaction rate constant of glucose-to-fructose isomerization was independent of the initial reactant ratios. It was more difficult for pep-pyr elimination in the model system with an excess of peptide than that in the other 2 model systems (the equimolar system and the system with an excess of glucose), whereas a reverse result in pep-pyr formation was obtained.
Subject(s)
Cooking/methods , Glucose/chemistry , Hot Temperature , Maillard Reaction , Norleucine/analogs & derivatives , Peptides/chemistry , Pyrroles/chemistry , Dipeptides/chemistry , Fructose/chemistry , Glycation End Products, Advanced , Humans , Kinetics , Mannose/chemistry , Microwaves , Models, Chemical , Norleucine/chemistryABSTRACT
Pyrraline, a causative factor for the recent epidemics of diabetes and cardiovascular disease, is also employed as an indicator to evaluate heat damage and formation of advanced glycation end-products (AGEs) in foods. Peptide-enriched drinks (PEDs) are broadly consumed worldwide due to rapid rate of absorption and perceived health effects. It can be hypothesized that PED is an important source of pyrraline, especially peptide bound pyrraline (Pep-Pyr). In this study we determined free-form pyrraline (Free-Pyr) and Pep-Pyr in drinks enriched with whey protein hydrolysate (WPH), soy protein hydrolysate (SPH) and collagen protein hydrolysate (CPH). A detection method was developed using ultrahigh-performance liquid chromatography with UV-visible detector coupled with tandem mass spectrometry after solid-phase extraction (SPE). The SPE led to excellent recovery rates ranging between 93.2% and 98.5% and a high reproducibility with relative standard deviations (RSD) of <5%. The limits of detection and quantification obtained were 30.4 and 70.3 ng/mL, respectively. Pep-Pyr was identified as the most abundant form (above 96 percent) of total pyrraline, whereas Free-Pyr was present in a small proportion (less than four percent) of total pyrraline. The results indicate that PED is an important extrinsic source of pyrraline, especially Pep-Pyr. As compared with CPH- and SPH-enriched drinks, WPH-enriched drinks contained high content of Pep-Pyr. The Pep-Pyr content is associated with the distribution of peptide lengths and the amino acid compositions of protein in PEDs.
Subject(s)
Beverages/analysis , Glycation End Products, Advanced/analysis , Norleucine/analogs & derivatives , Peptides/metabolism , Pyrroles/metabolism , Tandem Mass Spectrometry , Chromatography, High Pressure Liquid , Glycation End Products, Advanced/isolation & purification , Norleucine/chemistry , Norleucine/metabolism , Peptides/chemistry , Pyrroles/chemistry , Solid Phase ExtractionABSTRACT
Peptide-bound advanced glycation end-products (peptide-bound AGEs) can be formed when peptides are heated with reducing saccharides. Pyrraline is the one of most commonly studied AGEs in foods, but the relative importance of the precursor peptide structure is uncertain. In the present study, model systems were prepared by heating peptides with glucose from 60 °C to 220 °C for up to 65 min, and the amounts of peptide-bound pyrraline formed were monitored to evaluate the effect of the neighboring amino acids on the peptide-bound pyrraline formation. The physico-chemical properties were introduced to explore the quantitative structure-reactivity relationships between physicochemical properties and peptide bound formation. 3-DG content in dipeptide-glucose model system was higher than that in the corresponding tripeptide-glucose model systems. Dipeptides produced higher amounts of peptide-bound pyrraline than the corresponding tripeptides. The peptide-bound pyrraline and 3-DG production were influenced by the physico-chemical properties of the side chain of amino acids adjacent to Lys in the following order: Lys-Leu/glucose > Lys-Ile/glucose > Lys-Val/ glucose > Lys-Thr/glucose > Lys-Ser/glucose > Lys-Ala/ glucose > Lys-Gly/glucose; Lys-Leu-Gly/glucose > Lys-Ile-Gly/glucose > Lys-Val-Gly/glucose > Lys-Thr-Gly/glucose > Lys-Ser-Gly/glucose > Lys-Ala-Gly/glucose > Lys-Gly-Gly/glucose. For the side chain of amino acids adjacent to Lys in dipeptides, residue volume, polarizability, molecular volume and localized electrical effect were positively related to the yield of peptide bound pyrraline, while hydrophobicity and pKb were negatively related to the yield of peptide bound pyrraline. In terms of side chain of amino acid adjacent to Lys in tripeptides, a similar result was observed, except hydrophobicity was positively related to the yield of peptide bound pyrraline.
Subject(s)
Dipeptides/chemistry , Glucose/chemistry , Norleucine/analogs & derivatives , Peptides/chemistry , Pyrroles/chemistry , Amino Acid Sequence , Amino Acids/chemistry , Glycation End Products, Advanced/chemistry , Maillard Reaction , Models, Molecular , Norleucine/chemistry , Peptide Fragments/chemistry , Protein Binding , Quantitative Structure-Activity RelationshipABSTRACT
BACKGROUND: Pyrraline, a causative factor for various kinds of disease, is also used as a food contaminant to evaluate the formation of advanced glycation end-products (AGEs) in diet foods. In this study, model systems consisting of lysine and different saccharides were heated at different times, temperatures and initial molar ratios of saccharide to lysine under microwave heating conditions in order to investigate the formation of pyrraline. RESULTS: Increase in initial molar ratio of saccharide to lysine could significantly promote the formation of pyrraline. Specifically, the pyrraline formation rate was influenced by the structure of saccharides involved in the reaction, and decreased in the following order: lactose > fructose > glucose > sucrose; the highest pyrraline was generated in lactose-lysine models. The maximum pyrraline was formed at 140 °C. Moreover, saccharides and lysine had different effects on the stability of pyrraline. Among the reactants, lysine was the major factor for the instability of pyrraline; a dipyrraline and a crosslink by pyrraline reacting with lysine could be formed. CONCLUSION: Pyrraline formation by the saccharide-lysine model system was a dynamic reaction, consisting not only of the pyrraline formation, but also pyrraline elimination with some formation of crosslinks. © 2015 Society of Chemical Industry.
Subject(s)
Carbohydrates/chemistry , Lysine/chemistry , Maillard Reaction , Norleucine/analogs & derivatives , Pyrroles/chemistry , Hot Temperature , Molecular Structure , Norleucine/chemistry , Time FactorsABSTRACT
BACKGROUND: Bovine serum albumin (BSA) contains high affinity binding sites for several endogenous and exogenous compounds and has been used to replace human serum albumin (HSA), as these two compounds share a similar structure. Naringin palmitate is a modified product of naringin that is produced by an acylation reaction with palmitic acid, which is considered to be an effective substance for enhancing naringin lipophilicity. In this study, the interaction of naringin palmitate with BSA was characterised by spectroscopic and molecular docking techniques. METHODOLOGY/PRINCIPAL FINDINGS: The goal of this study was to investigate the interactions between naringin palmitate and BSA under physiological conditions, and differences in naringin and naringin palmitate affinities for BSA were further compared and analysed. The formation of naringin palmitate-BSA was revealed by fluorescence quenching, and the Stern-Volmer quenching constant (KSV ) was found to decrease with increasing temperature, suggesting that a static quenching mechanism was involved. The changes in enthalpy (ΔH) and entropy (ΔS) for the interaction were detected at -4.11 ± 0.18 kJ·mol(-1) and -76.59 ± 0.32 J·mol(-1)·K(-1), respectively, which indicated that the naringin palmitate-BSA interaction occurred mainly through van der Waals forces and hydrogen bond formation. The negative free energy change (ΔG) values of naringin palmitate at different temperatures suggested a spontaneous interaction. Circular dichroism studies revealed that the α-helical content of BSA decreased after interacting with naringin palmitate. Displacement studies suggested that naringin palmitate was partially bound to site I (subdomain IIA) of the BSA, which was also substantiated by the molecular docking studies. CONCLUSIONS/SIGNIFICANCE: In conclusion, naringin palmitate was transported by BSA and was easily removed afterwards. As a consequence, an extension of naringin applications for use in food, cosmetic and medicinal preparations may be clinically and practically significant, especially in the design of new naringin palmitate-inspired drugs.
Subject(s)
Flavanones/chemistry , Palmitates/chemistry , Serum Albumin, Bovine/chemistry , Animals , Binding Sites , Binding, Competitive , Carbohydrate Conformation , Cattle , Flavanones/metabolism , Kinetics , Molecular Docking Simulation , Protein Binding , Protein Conformation , Serum Albumin, Bovine/metabolism , Spectrometry, Fluorescence , Spectroscopy, Fourier Transform Infrared , ThermodynamicsABSTRACT
Thermal behavior of palm stearin (PS) and palm olein (PO) was explored by monitoring peak temperature transitions by differential scanning calorimetry (DSC). The fatty acid composition (FAC), isothermal crystallization kinetics studied by pulsed Nuclear Magnetic Resonance (pNMR) and isothermal microstructure were also compared. The results indicated that the fatty acid composition had an important influence on the crystallization process. PS and PO both exhibited more multiple endotherms than exotherms which showed irregular peak shapes. An increasing in cooling rate, generally, was associated with an increase in peak size. Application of the Avaimi equation to isothermal crystallization of PS and PO revealed different nucleation and growth mechanisms based on the Avrami exponents. PS quickly reached the end of crystallization because of more saturated triacylglycerol (TAG). The Avrami index of PS were the same as PO under the same isothermal condition at lower temperatrue, indicating that the crystallization mechanism of the two samples based on super-cooling state were the same. According to the polarized light microscope (PLM) images, crystal morphology of PS and PO was different. With the temperature increased, the structure of crystal network of both PS and PO gradually loosened.
Subject(s)
Fatty Acids/chemistry , Plant Oils/chemistry , Calorimetry, Differential Scanning , Crystallization , Kinetics , Liquid-Liquid Extraction , Magnetic Resonance Spectroscopy , Palm Oil , Phase Transition , Transition TemperatureABSTRACT
N(ε)-(carboxymethyl) lysine (CML) is the most abundant advanced glycation end product (AGE), and frequently selected as an AGEs marker in laboratory studies. In this paper, the formation and inhibition of N(ε)-(carboxymethyl)lysine in saccharide-lysine model systems during microwave heating have been studied. The microwave heating treatment significantly promoted the formation of CML during Maillard reactions, which was related to the reaction temperature, time and type of saccharide. The order of CML formation for different saccharides was lactose > glucose > sucrose. Then, the inhibition effect on CML by five inhibitors was further examined. According to the results, ascorbic acid and tocopherol did not affect inhibition of CML, in contrast, thiamin, rutin and quercetin inhibited CML formation, and the inhibitory effects were concentration dependent.
Subject(s)
Glucose/analogs & derivatives , Glucose/chemistry , Glycation End Products, Advanced/chemical synthesis , Lysine/analogs & derivatives , Microwaves , Antioxidants/chemistry , Ascorbic Acid/chemistry , Glycation End Products, Advanced/chemistry , Lysine/chemical synthesis , Lysine/chemistry , Quercetin/chemistry , Rutin/chemistry , Thiamine/chemistry , Tocopherols/chemistryABSTRACT
Coesite nanocrystals have been synthesized from periodic mesoporous organosilica (PMO) with (CH(2))(2) bridges heated at 300 °C for 150 min and 12 GPa. The crystals are not sintered, single crystalline, and have diameters of ca. 100-300 nm. Below 300 °C, an amorphous non-porous organosilica glass was obtained. Heating above 300 °C at 12 GPa results in the rapid crystal growth and micron size coesite crystals were formed.