The useful biological properties of sucrose esters: Opportunities for the development of new functional foods.

Sucrose esters have been deployed as surfactants in many food products since the 1950s. In addition to their useful physical characteristics, sucrose esters also have interesting biological properties that enhance their utility. This review critically examines the broad suite of biological activities that has been attributed to both synthetically-derived and naturally-occurring sucrose esters. These include insecticidal, molluscicidal, plant growth-regulating, anti-microbial, anti-tumor, anti-oxidant, anti-depressive, neuro-protective, anti-inflammatory and anti-plasmodial effects. In addition to providing a summary of the structure-activity profiles of sucrose esters, the various known mechanisms-of action of these compounds are also discussed. Furthermore, since sucrose esters are well-known surfactants, the potential to advantageously apply their industrially desirable physical characteristics in combination with their biological properties is considered. Recent advances in synthetic chemistry that have facilitated the deployment of biologically active sucrose esters as food additives are also described.

Sucrose fatty acid esters: synthesis, emulsifying capacities, biological activities and structure-property profiles.

The notable physical and chemical properties of sucrose fatty acid esters have prompted their use in the chemical industry, especially as surfactants, since 1939. Recently, their now well-recognized value as nutraceuticals and as additives in cosmetics has significantly increased demand for ready access to them. As such a review of current methods for the preparation of sucrose fatty acid esters by both chemical and enzymatic means is warranted and is presented here together with an account of the historical development of these compounds as surfactants (emulsifiers). The somewhat belated recognition of the antimicrobial, anticancer and insecticidal activities of sucrose esters is also discussed along with a commentary on their structure-property profiles.

High-Pressure-Promoted and Facially Selective Diels-Alder Reactions of Enzymatically Derived cis-1,2-Dihydrocatechols and Their Acetonide Derivatives: Enantiodivergent Routes to Homochiral and Polyfunctionalized Bicyclo[2.2.2]octenes.

cis-1,2-Dihydrocatechols 5 (X = Me and Cl), which are available in the homochiral form through the whole-cell biotransformation of toluene and chlorobenzene, respectively, undergo Diels-Alder cycloaddition reactions with a range of electron-deficient dienophiles at 19 kbar (1.9 GPa). The favored products of such reactions are adducts of the general form 7 and that arise through the operation of a contrasteric or syn-addition pathway. In contrast, the acetonide derivatives of metabolites 5 undergo anti-selective addition reactions under the same conditions and so producing adducts of the general form 11. Bicyclo[2.2.2]octenes 7 and 11, which embody carbocyclic frameworks of opposite enantiomeric form, are useful scaffolds for chemical synthesis. Computational studies reveal that syn-adduct formation is kinetically and normally thermodynamically favored over anti-adduct formation when the free diols 5 are involved, but the reverse is so when the corresponding acetonides participate as the 4π-addend. Furthermore, the reactions become more exothermic as pressure increases while, concurrently, the activation barrier diminishes and at 6 GPa (60 kbar) almost vanishes.

Solasodine suppress MCF7 breast cancer stem-like cells via targeting Hedgehog/Gli1.

BACKGROUND: Recently, a novel therapy to treat cancer has been to target cancer stem-like cells (CSCs). The aim of this study was to investigate the effect of solasodine, a steroidal alkaloid isolated from Solanum incanum L., on MCF7 CSCs and to understand the compound's underlying mechanism of action. METHOD: A tumorsphere formation assay was used to evaluate the effects of solasodine on the proliferation and self-renewal ability of MCF7 CSCs. The level of expression of proteins associated with cancer stemness markers and Hh signaling mediators was determined. The interaction between solasodine and Gli1 was calculated by molecular docking and further demonstrated by cellular thermal shift assay. RESULTS: Solasodine significantly decreased the proliferation of MCF7 tumorspheres and showed a stronger cytotoxicity on breast cancer cells with higher levels of Gli1 expression. The results showed that the levels of CD44 and ALDH1 expression were suppressed. Furthermore, expression of CD24 was enhanced by solasodine, via a mechanism that involved dampening Gli1 expression and blocking the nuclear translocation of this protein in MCF7 tumorspheres. Computational studies predicted that solasodine showed a high affinity with the Gli1 zinc finger domain that resulted from hydrogen-bonds to the THR243 and ASP216 amino acids residues. In addition, solasodine specifically bound with Gli1 and enhanced Gli1 protein stability in MCF7 cells. CONCLUSION: Here, our findings indicated that solasodine can directly suppresses Hh/Gli1 signaling, and is a novel anticancer candidate that targets CSCs.

Emulsifying Properties of an Homologous Series of Medium- and Long-Chain d-Maltotriose Esters and their Impacts on the Viabilities of Selected Cell Lines.

The development of functional as well as nutritional surfactants for the food industry remains a matter of great interest. In the present study, a series of 6″-O-acylmaltotriose monoesters bearing alkyl side chains of 10-18 carbons was prepared by enzymatic means. The emulsions derived from those monoesters incorporating palmitoyl, stearoyl, and oleoyl side chains generally displayed advantageous shelf-lives, superior resistance to environmental variations, and more favorable droplet size distributions as well as stronger cytotoxic effects against various cancer cell lines. Ester 6 was shown to significantly inhibit the proliferation of MCF-7 breast cancer cells by inducing G1 phase arrest. Specifically, the levels of the G1 phase-related markers cyclin D1 and cyclin E as well as the cycle-dependent kinase 4 were suppressed by this particular ester. This study thus reveals that maltotriose esters can not only serve as novel functional food emulsifiers but also act, in vitro, as notable cytotoxic agents through a well-defined mechanism-of-action.

Structural Modifications of a Flaxseed Lignan in Pursuit of Higher Liposolubility: Evaluation of the Antioxidant and Permeability Properties of the Resulting Derivatives.

While lignans and their biogenetic precursors can have various health benefits, the poor liposolubilities of such phenolic systems have restricted their application as antioxidants in the food industry. The research reported here was aimed at addressing these matters through derivatizing certain forms of such compounds and then assessing their properties as potential nutraceuticals. In particular, crude flaxseed lignan was purified to afford secoisolariciresinol diglucoside (SDG, 1) that was then subjected to structural modification. By such means, the SDG long-chain fatty acid esters 4-9 and 11-13, the fully acetylated SDG 10, secoisolariciresinol (SECO, 2), and anhydrosecoisolariciresinol (ASECO, 14) were obtained. The antioxidant activities of these derivatives were determined while their permeability properties were evaluated. Such studies revealed that certain SDG derivatives possessing useful liposolubilities also retained their antioxidative properties, as well as being capable of permeating Caco-2 cell monolayers while being nontoxic to them. SDG fatty acid esters 4-9 and 11-13 could be developed into emulsifiers with enhanced health benefits, especially considering their improved antioxidative (ca. <11 000 µmol Trolox/g) and permeability properties. This study thus highlights strategies for the structural modification of SDG so as to generate derivatives with superior properties in terms of their utility in the food and pharmaceutical industries.

Influence of glycosylation of deamidated wheat gliadin on its interaction mechanism with resveratrol.

Gliadin is a main composition of wheat storage protein with unique characteristics. Polyphenol with health benefits tends to form complex with protein. In this study, glycosylation of deamidated wheat gliadin (gliadin) was carried out. Fluorescence quenching was applied to evaluate their binding mechanisms with resveratrol. Results showed that glycosylation could increase the solubility and decrease the surface hydrophobicity of gliadin. Both gliadin and glycosylated gliadin have strong affinity with resveratrol. The thermodynamic parameters of binding process indicated that complexation of resveratrol with gliadin was mainly driven by hydrophobic interaction, while by hydrogen bonds with glycosylated gliadin. The hydrosolubility of resveratrol was dramatically increased especially in the presence of glycosylated gliadin. This was consistent with the higher binding constant of glycosylated gliadin with resveratrol. Therefore, gliadin and glycosylated gliadin are both effective to carry resveratrol or other bioactive compounds, and their binding mechanisms are different due to structural difference.

Self-assembled colloidal complexes of polyphenol-gelatin and their stabilizing effects on emulsions.

This research studies the in-depth characteristics including the binding interactions and morphological structure of tannic acid (TA)/grape seed proanthocyanidins (GSP) and gelatin (GLT) colloidal complexes, and evaluated the stability and lipid oxidation of emulsions formed by the colloidal complexes. Polyphenol and GLT (1.2 wt%) self-assembled complexes were fabricated by varying the mass ratio (1 : 16, 1 : 8 and 1 : 4) and pH in the range of 3-7. TA and GSP can form stable colloidal complexes with GLT at the nanoscale at pH 6, as shown by the particle size results, and the complexes exhibited a spherical morphology as seen by transmission electron microscopy. Hydrogen bonding was the main binding force for the interaction between polyphenols and GLT. The antioxidant activity of GLT was greatly improved after complexing with polyphenols. The oil/water emulsion formed by the complexes had a smaller droplet size and higher lipid oxidation stability during storage. This was largely due to the physical barrier formed by polyphenol-GLT colloidal complexes at the oil-water interface, which can prevent the pro-oxidant from penetrating into oil. These results clarified the structural, morphological and antioxidant properties of polyphenol-gelatin non-covalent complexes, which is of great value for their application in food solutions as well as in emulsion systems.

Simultaneous and selective decarboxylation of L-serine and deamination of L-phenylalanine in an amino acid mixture--a means of separating amino acids for synthesizing biobased chemicals.

Amino acids (AAs) obtained from the hydrolysis of biomass-derived proteins are interesting feedstocks for the chemical industry. They can be prepared from the byproduct of biofuel production and agricultural wastes. They are rich in functionalities needed in petrochemicals, providing the opportunity to save energy, reagents, and process steps. However, their separation is required before they can be applied for further applications. Electrodialysis (ED) is a promising separation method, but its efficiency needs to be improved when separating AAs with similar isoelectric points. Thus, specific conversions are required to form product with different charges. Here we studied the enzymatic conversions which can be used as a means to aid the ED separation of neutral AAs. A model mixture containing L-serine, L-phenylalanine and L-methionine was used. The reactions of L-serine decarboxylase and L-phenylalanine ammonia-lyase were employed to specifically convert serine and phenylalanine into ethanolamine and trans-cinnamic acid. At the isoelectric point of methionine (pH 5.74), the charge of ethanolamine and trans-cinnamic acid are +1 and -1, therefore facilitating potential separation into three different streams by electrodialysis. Here the enzyme kinetics, specificity, inhibition and the operational stabilities were studied, showing that both enzymes can be applied simultaneously to aid the ED separation of neutral AAs.

The selective conversion of glutamic acid in amino acid mixtures using glutamate decarboxylase--a means of separating amino acids for synthesizing biobased chemicals.

Amino acids (AAs) derived from hydrolysis of protein rest streams are interesting feedstocks for the chemical industry due to their functionality. However, separation of AAs is required before they can be used for further applications. Electrodialysis may be applied to separate AAs, but its efficiency is limited when separating AAs with similar isoelectric points. To aid the separation, specific conversion of an AA to a useful product with different charge behavior to the remaining compounds is desired. Here the separation of L-aspartic acid (Asp) and L-glutamic acid (Glu) was studied. L-Glutamate α-decarboxylase (GAD, Type I, EC 4.1.1.15) was applied to specifically convert Glu into γ-aminobutyric acid (GABA). GABA has a different charge behavior from Asp therefore allowing a potential separation by electrodialysis. Competitive inhibition and reduced operational stability caused by Asp could be eliminated by maintaining a sufficiently high concentration of Glu. Immobilization of GAD does not reduce the enzyme's initial activity. However, the operational stability was slightly reduced. An initial study on the reaction operating in a continuous mode was performed using a column reactor packed with immobilized GAD. As the reaction mixture was only passed once through the reactor, the conversion of Glu was lower than expected. To complete the conversion of Glu, the stream containing Asp and unreacted Glu might be recirculated back to the reactor after GABA has been removed. Overall, the reaction by GAD is specific to Glu and can be applied to aid the electrodialysis separation of Asp and Glu.