Effects of heating on the interaction of lipid and zein in a dry powder system

The effects of heat treatment on the interaction of lipid and zein in a dry powder system were investigated. Linolenic acid ethyl ester (LAE) was mixed with the zein powder. The glass transition temperature (T(g)) for the dry powder zein was shown to be approximately 107 degrees C by differential scanning calorimetry. The thermogram of the zein-LAE mixed powder showed an exothermic transition near the T(g) of zein. Fourier transform infrared (FT-IR) spectroscopy was used for detecting the structural changes in zein by heat treatment, that is, elevating the temperature from 25 to 160 degrees C. The heat treatment of the powdery zein with and without LAE caused increases in the alpha-helix, beta-turn, and beta-sheet, concomitant with decreases in the intermolecular hydrogen-bonded beta-sheet and random coil. Such changes in the secondary structure were more drastic for the powder with LAE. The heating of the zein-LAE mixed powder also caused decreases in the peaks originating from LAE in the FT-IR spectra. These results suggest that the heat treatment induced the interaction of the zein and LAE in the powdery system. The influence of heating on the antioxidative activity of dry powder zein was studied by measurements of the peroxide value. When zein-LAE mixed powder was heated before storage, the oxidation of LAE was inhibited for 7 days, whereas LAE was oxidized within 1 day in the absence of heat treatment.     

Effects of protein and peptide addition on lipid oxidation in powder model system

The effect of protein and peptide addition on the oxidation of eicosapentaenoic acid ethyl ester (EPE) encapsulated by maltodextrin (MD) was investigated. The encapsulated lipid (powder lipid) was prepared in two steps, i.e., mixing of EPE with MD solutions (+/- protein and peptides) to produce emulsions and freeze-drying of the resultant emulsions. EPE oxidation in MD powder progressed more rapidly in the humid state [relative humidity (RH) = 70%] than in the dry state (RH = 10%). The addition of soy protein, soy peptide, and gelatin peptides improved the oxidation stability of EPE encapsulated by MD, and the inhibition of lipid oxidation by the protein and the peptides was more dramatic in the humid state. Especially, the oxidation of EPE was almost perfectly suppressed when the lipid was encapsulated with MD + soy peptide during storage in the humid state for 7 days. Several physical properties such as the lipid particle size of the emulsions, the fraction of nonencapsulated lipids, scanning electron microscopy images of powder lipids, and the mobility of the MD matrix were investigated to find the modification of encapsulation behavior by the addition of the protein and peptides, but no significant change was observed. On the other hand, the protein and peptides exhibited a strong radical scavenging activity in the powder systems as well as in the solution systems. These results suggest that a chemical mechanism such as radical scavenging ability plays an important role in the suppression of EPE oxidation in MD powder by soy proteins, soy peptides, and gelatin peptides.     

Identification of food-derived collagen peptides in human blood after oral ingestion of gelatin hydrolysates

In the present study, we identified several food-derived collagen peptides in human blood after oral ingestion of some gelatin hydrolysates. Healthy human volunteers ingested the gelatin hydrolysates (9.4-23 g) from porcine skin, chicken feet, and cartilage after 12 h of fasting. Negligible amounts of the peptide form of hydroxyproline (Hyp) were observed in human blood before the ingestion. After the oral ingestion, the peptide form of Hyp significantly increased and reached a maximum level (20-60 nmol/mL of plasma) after 1-2 h and then decreased to half of the maximum level at 4 h after the ingestion. Major constituents of food-derived collagen peptides in human serum and plasma were identified as Pro-Hyp. In addition, small but significant amounts of Ala-Hyp, Ala-Hyp-Gly, Pro-Hyp-Gly, Leu-Hyp, Ile-Hyp, and Phe-Hyp were contained.     

Neural cadherin: role in selective cell-cell adhesion

Cadherins are a family of Ca2+-dependent intercellular adhesion molecules. Complementary DNAs encoding mouse neural cadherin (N-cadherin) were cloned, and the cell binding specificity of this molecule was examined. Mouse N-cadherin shows 92 percent similarity in amino acid sequence to the chicken homolog, while it shows 49 percent and 43 percent similarity to epithelial cadherin and to placental cadherin of the same species, respectively. In cell binding assays, mouse N-cadherin did not cross-react with other mouse cadherins, but it did cross-react with chicken N-cadherin. The results indicate that each cadherin type confers distinct adhesive specificities on different cells, and also that the specificity of N-cadherin is conserved between mammalian and avian cells.     

Effects of Ca2+ and sulfhydryl reductant on the polymerization of soybean glycinin catalyzed by mammalian and microbial transglutaminases

Two types of transglutaminases (TGases), Ca(2+)-dependent TGase derived from guinea pig liver (GTGase) and Ca(2+)-independent TGase derived from a variant of Streptoverticillium mobaraense (MTGase), were used to study the cross-linking of soybean 11S globulin (glycinin). The effects of sulfhydryl reductant (dithiothreitol, DTT) and Ca(2+) on the conformation and TGase-catalyzed polymerization of glycinin were investigated. The conformational change of glycinin was probed by spectral methods. The degree of cross-linking and the polymer (aggregate) formation were analyzed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and dynamic light scattering, respectively. Addition of DTT stimulated the TGase-catalyzed cross-linking reactions without destroying the secondary and tertiary structure of glycinin but did not influence the polymer or aggregate formation. It was found that Ca(2+) caused the formation of larger size polymers at lower concentrations, while it suppressed the polymerization at higher concentrations. In addition, the cross-linking behaviors of glycinin were shown to be different between MTGase- and GTGase-catalyzed systems.     

Effects of enzymatic deamidation by protein-glutaminase on structure and functional properties of wheat gluten

Protein-glutaminase (PG) purified from Chryseobacterium proteolyticum was used to investigate its deamidation effects on wheat gluten. Water-insoluble gluten was able to be deamidated to the extent of deamidation degree (DD) 72% in 200 mM sodium phosphate buffer (pH 7) at 40 degrees C for 30 h. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis exhibited an upper shift of gluten bands with only deamidation for 1.5-2.0 h (DD 35-45%) compared to the bands of nondeamidated gluten. Results of Fourier transform infrared analysis revealed alterations in secondary structure of gluten by PG deamidation. The assignment within amide I region showed decreases in both inter- (around 1695 cm(-1)) and intramolecular beta-sheets (around 1680 cm(-1)) by deamidation suggesting the deterioration of the aggregation ability of gluten molecules. Solubility and emulsification properties of gluten at pH 7 were improved by deamidation, while both properties at pH 3 were deteriorated by deamidation. Enzyme-linked immunosorbent assay identified that allergenicity of deamidated gluten as compared to the nondeamidated cohorts was decreased remarkably as the deamidation time was prolonged.     

Discrete sandwich compounds of monolayer palladium sheets

Despite the abundance of "sandwich" complexes, in which two cyclic aromatic hydrocarbon ligands flank a metal center, this motif has not been extended to sheets of multiple metal atoms. We prepared and isolated two such compounds. In the first, three palladium centers form a planar triangular array, capped by chlorides, between two cycloheptatrienyl ligands. In the second, a pentapalladium sheet adopts an edge-sharing triangle-trapezoid skeleton between two naphthacene rings. The compounds were characterized by x-ray crystallography and nuclear magnetic resonance spectroscopy. The nature of bonding in the clusters was analyzed by quantum calculations.     

Seed abortion of ‘Tosa-Buntan’ pummelo pollinated with soft-X-irradiated pollens

Cross-pollination was performed with soft-X-irradiated hyuga-natsu pollens (1000 Gy) for ‘Tosa-Buntan’ pummelo (Citrus grandis (L.) Osbeck). This resulted in the transformation of large and complete seeds into small and empty ones (practically seedless). Although fruit set, fruit retention, total soluble solids content (TSS) and titratable acidity of the juice were not affected, decrement in the fruit size was observed. Two weeks after the pollination, endosperm cell division with free nuclei began in both the non-irradiated and irradiated pollen treatment conditions. Seven weeks after pollination, endosperm division with the cell wall occurred in the non-irradiated pollen treatment conditions; however, the endosperm development ceased in most ovules that underwent the irradiated pollen treatment, and the ovules remained in their free nuclear stage. The delayed degeneration of the ovules, following successful fertilization and commencement of endosperm cell division, allow these seedless fruits to be categorized as pseudo-parthenocarpic.     

Inhibition of growth hormone secretagogue receptor antagonist, [D-Lys-3]-GHRP-6, in adipogenesis of ovine and rat adipocytes

Ghrelin and growth hormone secretagogues receptor (GHS‐R or ghrelin receptor) have been reported as being one of the factors of adipogenesis in adipocytes. To investigate the involvement of ghrelin and GHS‐R in adipocytes, the effect of the GHS‐R antagonist, [D‐Lys‐3]‐GHRP‐6 (His‐D‐Trp‐D‐Lys‐Trp‐D‐Phe‐Lys‐NH₂), on the process of adipogenesis in ovine and rat adipocytes was evaluated. [D‐Lys‐3]‐GHRP‐6 (10^?7 mol/L) significantly inhibited adipogenic differentiation of ovine and rat preadipocytes prepared from adipose tissues. The level of peroxisome proliferator activated receptor (PPAR)‐γ2 mRNA, an adipogenic marker, was decreased during the differentiation of adipocytes treated with [D‐Lys‐3]‐GHRP‐6 for 10 days. Ghrelin stimulated adipogenesis, also causing an increment of glycerol‐3‐phosphate dehydrogenase and upregulation of PPAR‐γ2. Furthermore, the antilipolytic effect of ghrelin was attenuated by treatment with [D‐Lys‐3]‐GHRP‐6 in both types of isolated adipocytes. Overall, the results of the present study highlight that GHS‐R in adipogenesis can be blocked by treatment with [D‐Lys‐3]‐GHRP‐6.