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Five new triterpenoids named as euphatexols C - G (1-5) were isolated from the latex of Euphorbia resinifera. Their chemical structures were determined by extensive spectroscopic analysis, including IR, HRMS, 1 D and 2 D NMR data. Compounds 1-5 showed moderate anti-inflammatory activity with IC50 values of 22.30, 48.04, 21.89, 38.15 and 41.15 μM, respectively.

1,1,1,3,3,3-Hexafluoroisopropylmethyl ether (HFE-356 mmz), with its ODP = 0 and low global warming potential, is a promising alternative foam blowing agent, cleaning fluid, and refrigerant. The vap...

As one of the most promising alternative refrigerants, 1,1,1,3,3,3-hexafluoro-2-methoxypropane (HFE-356 mmz) is considered to have the potential to be applied in a high temperature heat pump and th...

Bismuth-contained therapies are effective in treating gastric ulcer and eliminating Helicobacter pylori (Hp). Anion polysaccharides ligand could reduce the intake of bismuth, and enhance drug efficacy of bismuth compounds. In this study, pectin-bismuth (PB) was prepared and the changes of PB structure in acidic environment were reported for the first time. The structure of PB was characterized by FT-IR, XRD, and TGA, which suggested that combined with bismuth could alter the crystal structure of pectin. XPS confirmed the ionic binding of Bi3+ with carboxyl groups of pectin. The aggregating of PB with different pH level were also investigated, and the influence of pH on PB structure were observed by SEM. Results showed that PB has much larger volume of flocculation in acidic environment compared with bismuth nitrate. Additionally, apparent shear stress (τa) of PB suspension was evaluated. These results revealed the structural characteristics and acid-induced aggregation of pectin-bismuth, and bismuth could aggregate in acidic solution with the gelation of pectin.

Three new highly oxygenated lanostane triterpenoids, applanaic acids A–C (1–3), were isolated from the fruiting bodies of the basidiomycete Ganoderma applanatum. Among them, applanaic acid B (2) po...

Essential oil-loaded edible films usually suffer from short-term antimicrobial effects due to the uncontrolled evaporation of essential oils during film preparation and storage. A novel approach was developed to fabricate soluble soybean polysaccharide (SSPS)-based films that incorporated oregano essential oil (OEO) as antimicrobial agent. OEO was first encapsulated in a Pickering emulsion stabilized by complex coacervates of acid soluble soy protein (ASSP) and SSPS. Films were then prepared by incorporating the Pickering emulsions into SSPS solutions, where octenyl succinic anhydride (OSA) was used as the esterifying agent for interfacial and bulk SSPS. Incorporation of Pickering emulsion led to the decrease in transparency and tensile strength of films as the loading percentage increased. The surface and cross-sectional morphological observation revealed that OEO droplets distributed well in film matrix with evident internal cavities in films. The ASSP/SSPS complexes interface avoided flocculation and coalescence among OEO droplets, and the esterification reaction between SSPS and OSA reinforced the interfacial layer and the continuous phase. The immobilization effect held more essential oils within the film matrix during film preparation and showed prolonged antimicrobial property against three selected pathogenic bacteria.

The objective of this research was to study the octenyl succinic anhydride (OSA) modified SSPS (OSA-SSPS) formed via SSPS esterified with OSA. Cross-flow ultrafiltration was used to separate polysaccharides after esterification process and then OSA-SSPS with high molecular weight (HMW) as well as OSA-SSPS with low molecular weight (LMW) were obtained. The formation of OSA-SSPS was confirmed by fourier transform infrared spectroscopy which showed a new characteristic peak at around 1730.05 cm−1 (C=O). The viscosity of OSA-SSPS (HMW) was up to 80 mPa s while the value of SSPS was close to 30 mPa s in the 10 wt% concentration. The size distribution of OSA-SSPS indicated that OSA-SSPS (HMW) had a concentrated size in 1 μm while SSPS expressed three characteristic peaks. Particle size distribution showed that SSPS cross-linked successfully with OSA via the esterification, meanwhile, the side reactions were produced small molecules. The zeta potential of OSA-SSPS (−38.23 ± 0.24 mV) were 1.5 times as much as SSPS (−26.67 ± 0.31 mV). Compared the stability of SSPS with OSA-SSPS (HMW) in the acidic milk drink (AMD), the measurement of dispersion state (e.g. precipitation percent and turbidity) after centrifugation confirmed that OSA-SSPS (HMW) stabilized protein better than SSPS (p

The objective of this work was characterize and evaluate the protein-stabilizing property of pea soluble polysaccharide (PSPS) extracted from pea by-products using spray-drying and ethanol precipitation oven drying, obtaining PSPS-A and PSPS-B, respectively. The weight average molecular weight (Mw) of PSPS-A and PSPS-B were 625 kDa and 809 kDa, respectively. The results of Fourier transform infrared spectroscopy (FT-IR) analysis indicated that PSPS-A, PSPS-B and soybean soluble polysaccharide (SSPS) contained the same functional groups. The absolute negative charges of PSPS-A or PSPS-B in aqueous solution were slightly higher than that of SSPS at pH 2.0 to 7.0. The apparent diameter of PSPS-B (479.1 nm) was larger than that of PSPS-A (127.7 nm) and SSPS (209.5 nm) were measured by dynamic light scattering. The AFM images revealed that both PSPS-A and PSPS-B possessed star-like structures with more side chains as compared to SSPS. It was found that the addition of 0.15% PSPS-A or 0.1% PSPS-B was adequate to prevent the aggregation of protein and obtain stable dispersion. Furthermore, PSPS has a wider pH range (pH 3.6–4.6) to stabilize milk protein than SSPS (pH 3.6–4.2).

Anion- and solvent-induced single-crystal-to-single-crystal transformation within an iron(II) triazole system has been generated from {[Fe(TPPT)2Cl2]·CHCl3}n (1a) to [Fe(TPPT)(C2O4)0.5Cl(H2O)]n (1b). Luminescence studies indicated that the resultant 1b can be considered as a promising luminescent probe for CrO42– and cyano molecules.

In this work, three methods were utilized to modify citrus fiber (CF), xylanase hydrolysis, combination of xylanase treatment and water media ball milling (WMBM) or dry micronization by ball mill (DMBM). The chemical composition results showed xylanase treatment could increase the content of soluble dietary fiber (SDF) from 10.31 to 19.12 g/100 g CF and decrease the cellulose content from 38.97 to 35.85 g/100 g as well as the hemicellulose content from 22.16 to 18.83 g/100 g. WMBM could further change the chemical components, while DMBM showed tiny effects. The physicochemical properties of all modified CF are higher than the raw material, especially the enzyme-WMBM treatment could significantly increase the water holding capacity (WHC) by 2.08-folds, the oil retention capacity (ORC) by 1.53-folds and the water swelling capacity (WSC) by 4.56-folds higher than the unmodified CF. Besides, the modifications improved the cholesterol adsorption capacity (CAC), the glucose adsorption (GAC) and total antioxidant capacity (TAC) of the CFs progressively. The FT-IR spectra showed no spectra transform but peak intensity changes in the three modified CFs, the crystalline decreased from 28.16% to 18.60% after xylanase treatment, while increased from 18.60% to 24.00% (19.05%) after WMBM (DMBM) treatment, the SEM results showed the structure of CFs became looser and more porous, the thermogravimetric analysis showed the thermal ability of CF was improved after the modifications. The modifications altered the distribution of monosaccharides of CF as well. Overall results suggest that the modifications could change the structure of CF, the xylanase and xylanase-WMBM treatment could effectively improve the hydration capacities of CF.

Licorice is the dried root of Glycyrrhiza plants, which have long been used as flavourings, sweeteners, demulcents and expectorants in Western countries; as anti-allergic and anti-inflammatory drugs in China and Japan; and as therapeutics for diseases, such as cancers, heart disease and diabetes, in Russia and Eastern Europe. Licorice extract powder is the aqueous extract of licorice. Lycyrrhizic acid and flavonoids are the main bioactive constituents of Licorice extract powder that have health functions. Two drying methods, vacuum drying and microwave-vacuum drying, were comparatively studied to determine their impact on the physicochemical and antioxidant capacity of licorice extract powder, including its water-solubility, hygroscopicity, flowability, compression moldability, disintegration time, GA and total flavonoids compound contents and antioxidant capacity. The results showed that the physicochemical and antioxidant capacity of licorice extract powder were affected by the drying method. Microwave-vacuum drying maintained the GA and flavonoids components contents as well as the antioxidant capacity and reduced hygroscopicity. However, microwave-vacuum dried powders had a lower water-dissolution and a longer disintegration time than powders tablets.

Scutellariae Radix (Labiatae family) is the dried root of Scutellaria baicalensis Georgi, which is sometimes referred to as Huang Qin in Chinese. This root is an important traditional medicine in Asia to treat inflammatory and allergic diseases. Scutellaria extract is prepared from Scutellariae Radix, and it is an important intermediate for the preparation of many traditional Chinese medicine agents. For the preparation of Scutellaria extract, drying is an indispensable process, and two different drying methods, microwave-vacuum and vacuum drying, have been adopted in practical production. However, the effect of the two different drying methods on the physicochemical properties and biological activity of Scutellaria extract are largely unknown. Thus, in this paper, the drying kinetics and curve, the dissolution, the physicochemical properties and the antioxidant activity were assessed to evaluate the effect of the two different drying methods on Scutellaria extract powder. The results indicated that the microwave-vacuum drying has a significantly shorter drying time (9 to 13 min), a higher dissolution (34 ± 1.5%), a lower hygroscopicity (16.04 to 17.22%), a better flowability (the repose angle was 45.7 ± 1.2° to 46.6 ± 2.5°, compression degree was 38.7 ± 1.1 to 40.2 ± 0.6%) and formability (the tensile strength was 1.66 ± 0.07 to 1.83 ± 0.41 MPa), as well as higher antioxidant capacity (IC50 was 11.3 ± 0.5 to 11.8 ± 0.8 μg), than those of vacuum drying (130 to 150 min, 32 ± 1.3%, 19.74% to 20.02%, 48.2 ± 2.3° to 49.7 ± 2.2°, 51.6 ± 1.4% to 53.7 ± 1.9%, 1.57 ± 0.20 to 1.60 ± 0.36 MPa, 13.5 ± 0.9 to 13.9 ± 0.8 μg) (P 0.05). Thus, microwave-vacuum drying might be a good method for drying Scutellaria extract.

In this research, citrus dietary fiber (CF) was modified by two methods, homogenization or alkalinehydrogenperoxide (chemical) treatment, to improve its physicochemical properties. The homogenization and chemical treatment highly increased the CF's water swelling capacity by 433% and 276%, respectively. The water holding capacity of CF significantly increased by 253% after homogenization and 197% after chemical treatment. Both treatments increased CF's total dietary fiber content and thermal stability. Moreover, the chemically treated CF thermal stability was higherthan the homogenized one. Scanning electron microscopy (SEM) results showed the modified CFs exhibited porous structure. XRD and NMR results showed that the CF's crystalline region could be disrupted by both treatments. Overall results suggest that the two treatments could effectivelyimprove CF physicochemical properties. The modified fibers might be potentially used as functional food ingredients.

Pectin is widely distributed in plant cell wall, most of which have limited emulsifying properties. Ethanol could alter the solubility of pectin, and affect its emulsifying properties. No creaming and breaking of emulsion appeared in 21% (v/v) ethanol contained emulsion. This project investigated the influence of ethanol (0%-35%, v/v) on conformation and emulsifying properties of pectin. Results shown that ethanol could reduce the helix conformation and zeta potential of pectin chain, which leading to compact conformation and enhanced interaction among pectin molecules. Although emulsion droplet diameter increased with ethanol content, the most stable emulsion was found in 21% (v/v) ethanol. CLSM also indicated over-aggregated pectin have a poor adsorption capacity on the interface of O/W. All results manifested the emulsifying properties of pectin can be improved by 21% (v/v) ethanol. This study provides a new strategy to improve the emulsifying property of pectin by changing its conformation.

In 25% (v/v) ethanol system, an acid induced pectin gelling mechanism was proposed in this study, which could be used to construct emulsion gel system. FT-IR, GPC, and monosaccharides analysis were used to investigated the structure of pectins. HMP and LMP are different in molecular wight and chain structure, and HMP shows excellent gelling property. Intermolecular interaction of acid/ethanol induced HMP gel was investigated with SDS, Urea, and shifted pH. Those results indicated HMP has larger molecular wight, more neutral sugar side chain, and lower zeta potential than LMP, which facilitates the construction of compact gel network. LMP and HMP emulsions with 25% (v/v) ethanol were prepared and HMP emulsions with different oil volume fractions (Φ 0.2–0.75) exhibit gelling properties. Furthermore, the compact structure of HMP gel is stable during the freeze-thaw cycle which improved the freeze-thaw stability of pectin emulsions.

Soybean soluble polysaccharide (SSPS) is anionic polysaccharide extracted from the by-product of isolated soy protein production. In this study, a simple and eco-friendly procedure had been developed to prepare high-molecular-weight octenyl succinic esters of SSPS (OSA-SSPS) via the esterification between SSPS and octenyl succinic anhydride (OSA). The absolute molecular weights of OSA-SSPS and SSPS were 620 kDa and 53 kDa, respectively. OSA-SSPS had some similar properties to SSPS, such as microstructure and viscosity of 1 wt% concentration. However, compared to SSPS, OSA-SSPS showed different milk protein stabilization properties. The stabilizing behavior of OSA-SSPS was better than that of SSPS at pH range of 3.8–4.6, and poorer at pH 3.6. The model mixture of OSA-SSPS had smaller particle sizes at pH range of 3.8–4.6 and larger absolute negative charges at pH 2.0–10.0. In addition, from the molecular diameter measured by DLS and AFM image, the surface concentration of OSA-SSPS was larger than that of SSPS, which indicated that the thicker OSA-SSPS layer produces larger steric repulsion to milk protein particles. The mechanism for the greater ability of OSA-SSPS to stabilize milk proteins was proposed on the basis of the results discussed in this research.

This research presents a green procedure to prepare oil in water (O/W) emulsion from acid soluble soy protein (ASSP) and soy soluble polysaccharide (SSPS), a long-term stable nanoscale system for delivering the lipophilic components. The emulsion technique involved the preparation complexion using ASSP and SSPS by electrostatic and hydrophobic interactions as well as high pressure homogenization. The average diameter of the droplet of emulsions (fresh and heated) is 263±2nm. Such emulsions resulted in heating stable dispersions containing corn oil at the concentration of 20.0%, even at the pH around the isoelectric points of ASSP. After 90days storage at 4°C, the mean diameter of emulsions after heating at 80°C for 60min is 314±1nm compared with 341±3nm of emulsions unheated. The heat-stability of dispersions were affected by emulsion conditions, so the present research demonstrates the emulsion stability against heat treatment, ionic strength and pH change.

The structural responses of soy protein isolate under various processing conditions are of practically important for broadening its functionalities. In this work, multilevel structural responses of β-conglycinin and glycinin under acidic or alkaline heat treatment were investigated. Our results suggested that heat treatment under acidic (i.e., pH2.5) or alkaline (i.e., pH8.5) conditions induced multilevel structural responses of β-conglycinin and glycinin: under acidic heat treatment, both β-conglycinin and glycinin underwent hydrolysis and experienced disruption and reorganization in ordered secondary structure. This process was accompanied with changes in tertiary structure where previously buried regions were exposed to the aqueous phase to different extent. Small-angle x-ray scattering (SAXS) results indicated that the protein conformations evolved from globular ones to elongated ellipsoids, with a more remarkable elongation effect in glycinin than β-conglycinin. Upon solvent evaporation, β-conglycinin favored aggregation with a low "lateral to vertical ratio", glycinin tended to aggregate in a high "lateral to vertical ratio" style. In contrast, alkaline heat treatment did not induce hydrolysis but disturbed the secondary structure instead. The protein monomers maintained the globular conformation and assembled into irregular large aggregates during solvent evaporation. Under either treatment, glycinin responded more sensitively than β-conglycinin at all structure levels. The observed multi-level structural responses can be used to guide the rational modification of soy protein isolate with controlled conformation.

Rutin is a common dietary flavonoid with important antioxidant and pharmacological activities. However, its application in the food industry is limited mainly because of its poor water solubility. The subcritical water (SW) treatment provides an efficient technique to solubilize and achieve the enrichment of rutin in soy protein isolate (SPI) by inducing their complexation. The physicochemical, interfacial, and emulsifying properties of the complex were investigated and compared to the mixtures. SW treatment had much enhanced rutin-combined capacity of SPI than that of conventional method, ascribing to the well-contacted for higher water solubility of rutin with stronger collision-induced hydrophobic interactions. Compared to the mixtures of rutin with proteins, the complex exhibited an excellent surface activity and improved the physical and oxidative stability of its stabilized emulsions. This improving effect could be attributed to the targeted accumulation of rutin at the oil-water interface accompanied by the adsorption of SPI resulting in the thicker interfacial layer, as evidenced by higher interfacial protein and rutin concentrations. This study provides a novel strategy for the design and enrichment of nanovehicle providing water-insoluble hydrophobic polyphenols for interfacial delivery in food emulsified systems.

Pectin-rich dietary fibers were prepared from citrus peel through alkaline hydrogen peroxide treatment (AHP-CF) or homogenization treatment (H-CF). Structural and physicochemical properties of the citrus fibers were evaluated and compared with a commercial one (Fiberstar). Results showed that pectin content of citrus fibers (CF) increased from 15.23% to 21.52% and 26.79% after AHP and homogenization treatment. AHP-CF had the highest water-holding capacity (WHC) (21.32 g/g), water-swelling capacity (WSC) (32.70 mL/g) and cation exchange capacity (CEC) (1.02 Meq/g) among the fibers. SEM results showed porous or wrinkled surface of the treated CFs. XRD and TG analysis indicated that AHP treatment increased the crystallinity and thermal stability of CF while homogenization treatment was the opposite. Besides, H-CF had similar chemical component, oil-holding capacity and CEC with Fiberstar but higher WHC, WSC and thermal stability. These results suggested that AHP-CF and H-CF might be suitable to be an additive used in functional food.

In this research, the citrus fiber was modified by the alkali combined with high-speed homogenization (chemo-mechanical treatment) to improve its functional properties. The singly alkaline treated fiber was also evaluated to help us better understand the chemo-mechanical treatment's effect on citrus fiber. We compared the properties of modified citrus fibers with the untreated one and a commercial one (AQ Plus) which had excellent water holding capacity. The chemo-mechanical treated fiber's water swelling capacity was significantly improved to 35.56 mL/g (from 4.86 mL/g), higher than that of AQ Plus (28.25 mL/g). Its water holding capacity was increased to 25.52 g/g from 8.24 g/g, similar to that of AQ Plus (25.28 g/g). The chemo-mechanical treatment destroyed the citrus fiber's crystalline region, helped it form a rougher surface and porous inner structure, increased its soluble dietary fiber content and exposed more hydrogen bonds to water. Citrus fiber obtained from this chemo-mechanical method could be potentially used as food ingredients.

Protease prehydrolysis followed by subcritical water (SW) treatment was carried out to extract protein from heat-denatured soy meal. The composition, physicochemical, interfacial and emulsifying properties of soy protein isolate (SPI) were evaluated. A significant increase in extraction yield was observed although protein purity was decreased with prolonged hydrolysis. Due to contaminated β-glucosidase in protease from Aspergillus oryzae, Maillard reaction and the conversion of isoflavone glycosides into aglycones occurred, leading to the enrichment of aglycones in SPI. Compared to native SPI, enzyme-assisted SW-prepared SPI exhibited higher hydrophobic amino acids, surface hydrophobicity, and interfacial adsorption due to protein unfolding, accompanied by the formation of small soluble aggregates. Additionly, remarkable improvements of emulsifying ability and physical stability of emulsion were probably associated with higher surface protein loads. These results could develop a feasible protocol for producing nutrient-enhanced soy proteins with excellent emulsifying properties as novel functional ingredients applied in food industry.

The preparation of soy β-conglycinin-dextran nanogels (∼90 nm) went through two stages, which are safe, facile, and green. First, amphiphilic graft copolymers were formed by dextran covalently attaching to β-conglycinin via Maillard dry-heating reaction. Second, the synthesized conjugates were heated above the denaturation temperature at the isoelectric point (pH4.8) so as to assemble nanogels. The effects of pH, concentration, heating temperature, and time on the fabrication of nanogels were examined. The morphology study displayed that the nanogels exhibited spherical shape with core-shell structures, which was reconfirmed by zeta-potential investigation. Both circular dichroism spectra and surface hydrophobicity analyses indicated that the conformations of β-conglycinin in the core of nanogels were changed, and the latter experiment further revealed that the hydrophobic groups of β-conglycinin were exposed to the surface of protein. The nanogels were stable against various conditions and might be useful to deliver hydrophobic bioactive compounds.

Aims Atherosclerosis is the most common cause of cardiovascular disease, such as myocardial infarction and stroke. Previous study revealed that microRNA (miR)-134 promotes lipid accumulation and proinflammatory cytokine secretion through angiopoietin-like 4 (ANGPTL4)/lipid lipoprotein (LPL) signaling in THP-1 macrophages. Methods ApoE KO male mice on a C57BL/6 background were fed a high-fat/high-cholesterol Western diet, from 8 to 16 weeks of age. Mice were divided into four groups, and received a tail vein injection of miR-134 agomir, miR-134 antagomir, or one of the corresponding controls, respectively, once every 2 weeks after starting the Western diet. After 8 weeks we measured aortic atherosclerosis, LPL Activity, mRNA and protein levels of ANGPTL4 and LPL, LPL/ low-density lipoprotein receptor related protein 1 Complex Formation, proinflammatory cytokine secretion and lipid levels. Results Despite this finding, the influence of miR-134 on atherosclerosis in vivo remains to be determined. Using the well-characterized mouse atherosclerosis model of apolipoprotein E knockout, we found that systemic delivery of miR-134 agomir markedly enhanced the atherosclerotic lesion size, together with a significant increase in proinflammatory cytokine secretion and peritoneal macrophages lipid contents. Moreover, overexpression of miR-134 decreased ANGPTL4 expression but increased LPL expression and activity in both aortic tissues and peritoneal macrophages, which was accompanied by increased formation of LPL/low-density lipoprotein receptor-related protein 1 complexes in peritoneal macrophages. However, an opposite effect was observed in response to miR-134 antagomir. Conclusions These findings suggest that miR-134 accelerates atherogenesis by promoting lipid accumulation and proinflammatory cytokine secretion via the ANGPTL4/LPL pathway. Therefore, targeting miR-134 may offer a promising strategy for the prevention and treatment of atherosclerotic cardiovascular disease.

Two unusual euphane triterpenoids, named euphatexols A (1) and B (2), were isolated from the latex of Euphorbia resinifera. Their structures were elucidated based on the extensive analysis of spectroscopic data (HRMS, 1D and 2D NMR). Compound 1 possesses a rare tetrahydrofuran ring formed via C-1 and C-11, which is firstly reported in euphane triterpenoids. Compound 2 represents an unusual 27-nor-euphane triterpenoid. Moreover, compounds 1 and 2 showed significant cytotoxic activities against HepG2 cells with 87.0% and 87.4% inhibition rate at 1 μM, respectively.

The formation and interfacial adsorption of glycinin/chitosan (CS) soluble complex were investigated at acidic pH. The stability of the mixed emulsion stabilized by the complex was also evaluated at pH 4.5. Turbidimetric analysis, isothermal titration calorimetry (ITC) and dynamic light scattering were used to characterize the dynamic formation of the complex. The results showed that soluble complexes were formed mainly at pHs between 4.0 and 6.0, depending on CS/Glycinin mixing ratio. At pH 4.5, soluble complex was formed and saturated at mixing ratio = 0.1, showing a maximum size distribution at 164.2 nm. We found that the glycinin/CS soluble complex showed improved interfacial adsorption than glycinin at pH 4.5. In detail, dynamic interfacial adsorption data showed the coefficient of diffusion ( K diff ), unfolding ( K 1 ) and rearrangement ( K 2 ) for soluble complex ( K diff , K 1 and K 2 : 0.58 mNm −1 s −0.5 , 2.23 E−4 s −1 and 5.78 E−4 s −1 ) were higher than those of the glycinin ( K diff , K 1 and K 2 : 0.32 mNm −1 s −0.5 , 1.72 E−4 s −1 and 4.63 E−4 s −1 ). The droplet size and confocal observation of the mixed emulsion fabricated with glycinin/CS soluble complex displayed improved stability at mixing ratios of 0.1 to/and 0.2, suggesting the synergistic effect of the two molecules. We concluded that interfacial and emulsifying properties of glycinin could be improved by formation of glycinin/CS soluble complex at acidic pH.

The objective of this research was to fabricate novel gelatin films crosslinked by a naturally biochemical crosslinker (genipin) to achieve a controlled release of antimicrobial lysozyme. Lysozyme release kinetic studies were performed at acidic and/or neutral pH. Antimicrobial properties of the films were evaluated and an attempt was made to relate the antimicrobial activity of the films to release kinetics of lysozyme. The release kinetic profiles of lysozyme from gelatin films could be described as a two-step biphasic process, an initial burst effect followed by subsequent slower release, and close linear relationships between released lysozyme activities and incubating time were observed during burst release course. Genipin crosslinking retarded the release of lysozyme at pH 7.0, in a dose dependent manner, while lysozyme was rapidly released from the films at pH 3.8. Concomitantly, antimicrobial activity of the films decreased gradually as genipin concentration increased. The present data showed that gelatin films modified by genipin crosslinking efficiently retarded the release of lysozyme, being a promising way to extend antimicrobial effects during food storage and to enhance food safety.

The objective of this research is to investigate the complex of soy protein isolate (SPI) and chitosan (CS) heated (121 °C, 15 min) at low pH. The formation and functional properties of heated SPI–CS complex were investigated by electrophoresis, Fourier transform infrared spectroscopy (FTIR), solubility, ζ -potential and emulsifying property. The results indicated that the heated SPI–CS complex is probably more like a soluble SPI–CS aggregate which is driven by electrostatic interaction. Heated SPI–CS complex exhibited improved solubility than SPI (less than 10%) and unheated SPI–CS mixture (about 50%) at pH 4.0 because of the increased electrostatic repulsion ( ζ -potential) after heat treatment. The effects of mixing ratios, molecular weights (MW) and charge densities (CD) of chitosan on the stability of heated SPI–CS complex showed the influence was mainly dependent on mixing ratios and CD of chitosan. Concomitantly, the emulsifying activity index of SPI at pH 4.0 was significantly improved by heated complexation and the emulsion stability index was not affected. Additionally, the heated SPI and/or SPI–CS complex exhibited slightly decreased pepsin and trypsin digestibility. The results suggested that the physicochemical and functional properties of SPI could be modulated by heated complexing with chitosan, using appropriate mixing ratio, MW and CD of chitosan.

The conjugation reaction between soy β-conglycinin and dextran via Maillard reaction in crowded liquid system was studied. Apparent viscosity indicated that environment became more and more crowded with the increase of dextran concentration. The covalently linked conjugate was produced by incubating aqueous solution containing soy β-conglycinin and dextran at pH 7.0 and 95 °C for 6 h. Free amino group content and sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) profile showed that soy β-conglycinin–dextran conjugate was successfully formed and macromolecular crowding enhanced the extent of glycation. The results of atomic force microscopy indicated that glycation inhibited the thermal aggregate of protein. Meanwhile, the tertiary structure of protein in conjugate changed with increasing number of aromatic side-chains exposed in heating environment. All data showed that the introduction of macromolecular crowding in soy β-conglycinin–dextran conjugate was an effective and promising method for linking polysaccharides to proteins.

Microfluidization followed by density-based separation was employed to extract protein from broken rice by disrupting protein-starch agglomerates. Follow-up enzyme treatments (amylase and glucoamylase) were performed to further improve the purity of the protein-rich fraction. High protein recovery (81.87%) and purity (87.89%) were obtained. The protein composition, solubility, structural properties, and in vitro digestibility of rice proteins prepared by enzyme-assisted microfluidization (EM-RP) and alkaline extraction (AE-RP) were compared. EM-RP was mainly composed of glutelin, which had low solubility and native structure. By contrast, large quantities of prolamin and globulin appeared in the AE-RP except glutelin, leading to the richness of glutamic acid/glutamine, leucine, aromatic and charged amino acids in the AE-RP. Compared to AE-RP, EM-RP showed higher digestibility due to the richness of glutelin (an easy-to-digest protein), as evidenced by higher nitrogen release during pepsin-trypsin digestion. The presence of prolamin (an indigestible protein) in AE-RP decreased protein digestibility although alkaline extraction improved its hydrolysis. These results suggest that enzyme-assisted microfluidization could be an effective technique to non-destructively and selectively extract rice glutelin.

ABT-348 [1-(4-(4-amino-7-(1-(2-hydroxyethyl)-1H-pyrazol-4-yl)thieno[3,2-c]pyridin-3-yl)phenyl)-3-(3-fluorophenyl)urea] is a novel ATP-competitive multitargeted kinase inhibitor with nanomolar potency (IC(50)) for inhibiting binding and cellular autophosphorylation of Aurora B (7 and 13 nM), C (1 and 13 nM), and A (120 and 189 nM). Cellular activity against Aurora B is reflected by inhibition of phosphorylation of histone H3, induction of polyploidy, and inhibition of proliferation of a variety of leukemia, lymphoma, and solid tumor cell lines (IC(50) = 0.3-21 nM). In vivo inhibition of Aurora B was confirmed in an engrafted leukemia model by observing a decrease in phosphorylation of histone H3 that persisted in a dose-dependent manner for 8 h and correlated with plasma concentration of ABT-348. Evaluation of ABT-348 across a panel of 128 kinases revealed additional potent binding activity (K(i) < 30 nM) against vascular endothelial growth factor receptor (VEGFR)/platelet-derived growth factor receptor (PDGFR) families and the Src family of cytoplasmic tyrosine kinases. VEGFR/PDGFR binding activity correlated with inhibition of autophosphorylation in cells and inhibition of vascular endothelial growth factor (VEGF)-stimulated endothelial cell proliferation (IC(50) ≤ 0.3 nM). Evidence of on-target activity in vivo was provided by the potency for blocking VEGF-mediated vascular permeability and inducing plasma placental growth factor. Activity against the Src kinase family was evident in antiproliferative activity against BCR-ABL chronic myeloid leukemia cells and cells expressing the gleevec-resistant BCR-ABL T315I mutation. On the basis of its unique spectrum of activity, ABT-348 was evaluated and found effective in representative solid tumor [HT1080 and pancreatic carcinoma (MiaPaCa), tumor stasis] and hematological malignancy (RS4;11, regression) xenografts. These results provide the rationale for clinical assessment of ABT-348 as a therapeutic agent in the treatment of cancer.

BACKGROUND: Several methods have been reported for the conjugation of proteins with polysaccharides. Protein–polysaccharide conjugates can be formed by traditional dry heating, but this process is not attractive from an industrial viewpoint, and no commercial conjugates have been manufactured in this way. In the present study, in order to develop a more practical reaction method, macromolecular crowding was used to attach polysaccharides to proteins. RESULTS: Soy protein isolate–dextran conjugates (SDCs) were prepared via the initial stage of the Maillard reaction in macromolecular crowding conditions. The impact of various processing conditions on the formation of SDCs was investigated. The optimal conditions chosen from the experiments were a soy protein isolate/dextran ratio of 1:1 (w/w), a pH of 6.5, a reaction temperature of 60 °C and a reaction time of 30 h. Circular dichroism spectroscopy showed that the secondary and tertiary structures of the conjugates were changed significantly. Structural flexibility increased, allowing better display of their functional characteristics. The conjugates had a composition with various sizes, especially macromolecules, according to gel permeation chromatography. Thermal analysis showed that the thermal stability of the conjugates was improved. CONCLUSION: The production of SDCs under macromolecular crowding conditions appears to be an effective and promising technique, representing an advance over classic protein glycosylation methods. Copyright © 2012 Society of Chemical Industry

Soybean oil bodies and oleosins are known to be useful in foods and other emulsion systems. The influence of NaCl addition (0–500 mM), thermal processing (30, 60, 90 and 120 °C, 30 min), and freeze-thaw cycling (−20 °C, 24 h/30 °C, 2 h) on the stability of uncoated and ι-carrageenan coated soybean oil body emulsions at pH 3 and 7 was analyzed using particle electrical charge, particle size distribution, creaming stability and confocal laser scanning microscopy measurements. The stability of the uncoated emulsions to NaCl addition depended on pH, which was attributed to electrostatic screening effects. For NaCl, the uncoated emulsions were relatively stable from 0 to 150 mM at pH 3, but aggregated at ≥ 50 mM at pH 7; however, the ι-carrageenan coated emulsions at pH 3 and 7 were stable at all NaCl concentrations. The thermal stability of uncoated and ι-carrageenan coated emulsions may be relative to pH and holding temperature. Both uncoated and ι-carrageenan coated emulsions were stable at pH 7, whereas the uncoated emulsions at pH 3 became unstable when heated above 90 °C, but the ι-carrageenan coated emulsion droplets at pH 3 only extensively coalesced at 120 °C. The ι-carrageenan coated emulsions at pH 3 and 7 exhibited little droplet aggregation after three freeze-thaw cycles in the presence of sucrose. These results suggest that ι-carrageenan coated soybean oil body emulsions have similar or improved stability compared to uncoated emulsions and may be utilized as functional soy products in the food and other industries.

This work is directed towards the preparation of chemoselective ruthenium catalyst. The catalyst is a new type of ruthenium(II) complexes supported on γ-Al2O3, which have ruthenium(II) centers coordinated to the ligands triphenylphosphine and (1S,2S)-1,2-Diphenyl-1,2-ethanediamine. The catalyst for the selective hydrogenation of ketones in the mild conditions is investigated. The results show that the performance of the catalystis greatly influenced by the ratio of Ru and PPh3 and reduction time, respectively.

The effect of ι-carrageenan (ι-C) and soybean soluble polysaccharide (SSPS), on quality characteristics of tofu was evaluated. The addition of 0.05-0.2% (w/v) polysaccharide increased the yield of tofu. However, higher polysaccharide concentration could not sustain the observed increase. At temperature rise ramp, dG'/dt of tofu with SSPS was increased slightly than the samples with ι-C, due to difference in charge density and thermodynamic incompatibility between polysaccharide and soybean globulin. The addition of SSPS exhibited more increase in hardness and springiness of tofu as compared to ι-C. Microstructure of tofu with SSPS was more homogeneous. The addition of properly selected polysaccharide could improve the properties of tofu, which may be beneficial for food process

The amino acid (AA) composition and physicochemical and conformational properties of protein isolate (SNPI), globulin (SNG) and albumin (SNA) fractions from soapnut seeds were evaluated. The essential AA of SNG, SNA and SNPI (except sulfur-containing AA) are sufficient for the FAO/WHO suggested requirements for 2–5 year old infants. SNG and SNPI showed similar electrophoresis patterns and AA compositions, the subunit of those proteins consisted of two polypeptides linked by disulfide bonds. In contrast, SNA showed a different AA compositions and SDS–PAGE pattern. Both SNG and SNPI presented a typical U-shape protein solubility (PS)–pH profile, SNA showed a completely different PS–pH profile, especially at pH 2.0–4.0. The near-UV circular dichroism (CD), differential scanning calorimetry (DSC) and tryptophan fluorescence spectra analyses indicated that the flexibility in tertiary conformations decreased in the order: SNA > SNPI > SNG, while soapnut proteins had a similar secondary conformation, with a highly ordered structure (the β-types), as evidenced by far-UV CD spectra.

Summary The aim of this investigation was to explore the pH-induced conformational changes of phaseolin using differential scanning calorimetry (DSC), fluorescence and circular dichroism (CD) spectra. The surface charges at the varying pH and ionic strength were also determined to probe the possible relationship between the surface charges of phaseolin and its conformation. The ζ-potential of phaseolin decreased from 27.9 mV at pH 3.0 to –44 mV at pH 9.4, and the isoelectric point (iep) occurred at pH 4.21, which were comparable with the theoretical estimations derived from amino acid composition and pK values. The iep of phaseolin was independent of ionic strength, while the magnitude of ζ-potential decreased as the ionic strength increased. The near-UV CD, DSC and fluorescence spectra analyses indicated highly acidic and alkaline pH conditions induced the loss of tertiary conformation of phaseolin. The far-UV CD spectra analysis confirmed pH-shift led to the decreases in ordered secondary structure compositions. The present results suggested the loss of secondary and/or tertiary conformation of phaseolin as a result of the varying pattern in electrostatic interactions as pH shifted from 7.0 to acidic or alkalic pH.

Oil bodies, with their unique structural proteins, oleosins, are known to be useful in foods and other emulsion systems. The influence of κ, ι, and λ-carrageenans on the stability of soybean oil body emulsions at different pH values (pH 3, 4, 5 and 7) was investigated by particle electrical charge, particle size distribution, creaming stability and confocal laser scanning microscopy measurements. In acidic environment (pH 3, 4 and 5), the droplet charge of soybean oil body emulsions stabilized with carrageenan decreased with increasing carrageenan concentration for all types of carrageenan investigated, suggesting their adsorption to the oil body droplet surfaces. Extensive droplet aggregation and creaming were observed in the emulsions stabilized with λ-carrageenan at pH 3 and 5, indicating that soybean oil body droplets were bridged by carrageenan. At pH 7, there was no significant change in the droplet charge of soybean oil body emulsions stabilized with three types of carrageenan, but the emulsions stabilized with ι-carrageenan were more stable to creaming due to depletion flocculation than the emulsions stabilized with κ or λ-carrageenan after seven days storage. The probable reason was that ι-carrageenan, which had the most densely charged helical structure, was most effective at creating highly charged interfacial membranes, thus reducing the depletion flocculation to occur.