Lipid stability and antioxidant profile of microsomal fraction of broiler meat enriched with α-lipoic acid and α-tocopherol acetate

The importance of the linkage between nutrition and health is a hot issue. Like other food-related sectors, the meat industry is undergoing foremost transformations, driven among other things by changes in consumer requirements. The present study was designed to evaluate the lipid stability and antioxidative potential of leg and breast microsomal fraction of broiler meat fed on ALA and ATA. For the first 3 weeks of growth, broilers were fed on feed supplemented with ATA (200 mg/kg of feed) and during the last 3 weeks broilers were fed on feed supplemented with ALA (25, 75, 150 mg/kg of feed) and a constant level of ATA (200 mg/kg of feed). The body weight of the carcass was measured after every week of growth until 6 weeks. Positive correlation between the antioxidant activity and the TPC was observed. Higher values of TBARS were detected in leg muscles than in breast muscles. HPLC data revealed ALA and ATA contents were higher in T(4) (leg, 5.55 ± 0.19 and 3.87 ± 0.15 μg/mg of protein; breast, 5.63 ± 0.20 and 2.03 ± 0.10 μg/mg of protein, respectively) and lowest in T(5) (ALA, leg, 1.40 ± 0.06 μg/mg of protein; breast, 1.54 ± 0.05 μg/mg of protein; ATA, leg, 1.25 ± 0.06 μg/mg of protein; breast, 0.63 ± 0.008 μg/mg of protein), in which the only oxidized oil was used. Oxidized oil in feed reduced weight gain and increased TBARS, whereas TPC, DPPH, ALA, and ATA values decreased in both leg and breast meat.     

Grape Seed and Tea Extracts and Catechin 3-Gallates Are Potent Inhibitors of α-Amylase and α-Glucosidase Activity

This study evaluated the inhibitory effects of plant-based extracts (grape seed, green tea, and white tea) and their constituent flavan-3-ol monomers (catechins) on α-amylase and α-glucosidase activity, two key glucosidases required for starch digestion in humans. To evaluate the relative potency of extracts and catechins, their concentrations required for 50 and 90% inhibition of enzyme activity were determined and compared to the widely used pharmacological glucosidase inhibitor, acarbose. Maximum enzyme inhibition was used to assess relative inhibitory efficacy. Results showed that grape seed extract strongly inhibited both α-amylase and α-glucosidase activity, with equal and much higher potency, respectively, than acarbose. Whereas tea extracts and catechin 3-gallates were less effective inhibitors of α-amylase, they were potent inhibitors of α-glucosidase. Nongallated catechins were ineffective. The data show that plant extracts containing catechin 3-gallates, in particular epigallocatechin gallate, are potent inhibitors of α-glucosidase activity and suggest that procyanidins in grape seed extract strongly inhibit α-amylase activity.     

Recovery and characterization of α-zein from corn fermentation coproducts

Zeins were isolated from corn ethanol coproduct distiller's dried grains (DDG) and fractionated into α- and β γ-rich fractions. The effects of the ethanol production process, such as fermentation type, protease addition, and DDG drying temperature on zein recovery, were evaluated. Yield, purity, and molecular properties of recovered zein fractions were determined and compared with zein isolated from corn gluten meal (CGM). Around 29-34% of the total zein was recovered from DDG, whereas 83% of total zein was recovered from CGM. Process variations of cooked and raw starch hydrolysis and fermentation did not affect the recovery, purity, and molecular profile of the isolated zeins; however, zein isolated from DDG of raw starch fermentation showed superior solubility and film forming characteristics to those from conventional 2-stage cooked fermentation DDG. Protease addition during fermentation also did not affect the zein yield or molecular profile. The high drying temperature of DDG decreased the purity of isolated zein. SDS-PAGE indicated that all the isolated α-zein fractions contained α-zein of high purity (92%) and trace amounts of β and γ-zeins cross-contamination. Circular dichroism (CD) spectra confirmed notable changes in the secondary structure of α-zeins of DDG produced from cooked and raw starch fermentation; however, all the α-zeins isolated from DDG and CGM showed a remarkably high order of α-helix structure. Compared to the α-zein of CGM, the α-zein of DDG showed lower recovery and purity but retained its solubility, structure, and film forming characteristics, indicating the potential of producing functional zein from a low-value coproduct for uses as industrial biobased product.     

Variability of hydrolysis of β-, αs1-, and αs2-caseins by 10 strains of Streptococcus thermophilus and resulting bioactive peptides

Milk proteins contain numerous potential bioactive peptides, which may be released by digestive proteases or by the proteolytic system of lactic acid bacteria during food processing. The capacity of Streptococcus thermophilus to generate peptides, especially bioactive peptides, from bovine caseins was investigated. Strains expressing various levels of the cell envelope proteinase, PrtS, were incubated with α(s1)-, α(s2)-, or β-casein. Analysis of the supernatants by LC-ESI-MS/MS showed that the β-casein was preferentially hydrolyzed, followed by α(s2)-casein and then α(s1)-casein. Numbers and types of peptides released were strain-dependent. Hydrolysis appeared to be linked with the accessibility of different casein regions by protease. Analysis of bonds hydrolyzed in the region 1-23 of α(s1)-casein suggests that PrtS is at least in part responsible for the peptide production. Finally, among the generated peptides, 13 peptides from β-casein, 5 from α(s2)-casein, and 2 from α(s1)-casein have been reported as bioactive, 15 of them being angiotensin-converting enzyme inhibitors.     

Inhibitory effects of muscadine anthocyanins on α-glucosidase and pancreatic lipase activities

Inhibitory effects of the Noble muscadine grape extracts and the representative phytochemicals for anthocyanins (i.e., cyanidin and cyanidin-3,5-diglucoside) on two enzymes, that is, α-glucosidase and pancreatic lipase, were investigated regarding their antidiabetic activities. The study demonstrated that the anthocyanin extracts and the selected chemicals obeyed the competitive mode against the enzymes. The methanolic extracts of whole fruit and skin of the muscadine showed inhibitory activities against the α-glucosidase with their IC(50) values at 1.50 and 2.73 mg/mL, and those against the lipase at 16.90 and 11.15 mg/mL, respectively, which indicated that the muscadine extracts possessed strong antidiabetic activities. Particularly, the ethyl acetate (EtoAc) extract and the butanol (BuOH) extract exhibited much higher inhibitory activities against both enzymes than the CHCl(3) and water extracts, while the majority of anthocyanins existed in the BuOH fractions. Moreover, cyanidin exhibited a much stronger antidiabetic activity than cyanidin-3,5-diglucoside, suggesting that anthocyanins may have higher inhibitory activities after being digested. Further chromatographic analysis by high-performance liquid chromatography-mass spectrometry identified five individual anthocyanins, including cyanidin, delphinidin, petunidin, peonidin, and malvidin glycosides.     

Effect of saccharide structure and size on the degree of substitution and product dispersity of α-lactalbumin glycated via the Maillard reaction

The course of the Maillard reaction between α-lactalbumin and various mono- and oligosaccharides in the solid state was studied using UPLC-ESI-TOF-MS. Individual reaction products were monitored for their degree of substitution per protein molecule (DSP). The Maillard reaction rate depended on the saccharide type and decreased when the saccharide size increased. Conjugation with charged saccharides was hindered when a specific average DSP was reached, probably resulting from electrostatic repulsion. The DSP varied between 0 and 15, and the standard deviation of the average DSP, which is a measure for product dispersity, increased to 1.9. Similar experiments were performed with a dipeptide. Relative reaction rates in these experiments were 1 for glucose, 0.28 for maltose, and 0.16 for maltotriose. Comparison of the results obtained using α-lactalbumin and the dipeptide made clear that the Maillard reaction rate is determined by a number of factors, including saccharide reactivity and lysine accessibility.     

Transport across Caco-2 cell monolayer and sensitivity to hydrolysis of two anxiolytic peptides from αs1-casein, α-casozepine, and αs1-casein-f91-97: effect of bile salts

α-Casozepine and f91-97, peptides from α(s1)-casein, display anxiolytic activity in rats and may have to cross the intestinal epithelium to exert this central effect. We evaluated their resistance to hydrolysis by the peptidases of Caco-2 cells and their ability to cross the cell monolayer. To mimic physiological conditions, two preparations of bile salts were used in noncytotoxic concentrations: porcine bile extract and an equimolar mixture of taurocholate, cholate, and deoxycholate. The presence and composition of bile salts appeared to modulate the peptidase activities of the Caco-2 cells involved (i) in the hydrolysis of α-casozepine, leading to much higher formation of fragments f91-99, f91-98, and f91-97, and (ii) in the hydrolysis of f91-97, leading to lower degradation of this peptide. Transport of α-casozepine across Caco-2 monolayer increased significantly, in the presence of bile extract, and of fragment f91-97, in the presence of bile salts.     

Effect of α-casein on DNA adsorption by Andosols and by soil components

Andosols and the soil components (allophanes, humic acids, and goethite) had been autoclaved to destroy the nuclease activity of soil microflora. DNA adsorption by allophanes and Andosols was decreased by increasing the amount of α-casein added to the allophanes and to soils up to casein concentration of 5 mg ml^?1. DNA adsorption by humic acids was significantly increased by increasing the amount of α-casein up to 1.0 mg ml^?1, whereas the addition of 20 mg α-casein ml^?1 completely blocked DNA adsorption. These results can explain why the addition of excess skim milk is operationally needed for effective DNA extraction from Andosols. The amount of DNA adsorbed by Andosols treated with dephosphorylated α-casein was significantly higher than that of not treated Andosols (p?相似文献   

Design, synthesis, and insecticidal activity of novel pyrazole derivatives containing α-hydroxymethyl-N-benzyl carboxamide, α-chloromethyl-N-benzyl carboxamide, and 4,5-dihydrooxazole moieties

On the basis of commercial insecticides tebufenpyrad and tolfenpyrad, two series of novel pyrazole-5-carboxamides containing α-hydroxymethyl-N-benzyl or α-chloromethyl-N-benzyl and pyrazoles containing 4,5-dihydrooxazole moieties were designed and synthesized via the key intermediate 2-amino-1-(4-substituted) phenyl ethanol. The structures of target compounds were confirmed by (1)H NMR and elemental analysis or high-resolution mass spectrum (HRMS), and their activities against cotton bollworm (Helicoverpa armigera), diamondback moth (Plutella xylostella), bean aphid (Aphis craccivora), mosquito (Culex pipiens pallens), and spider mite (Tetranychus cinnabarinus) were tested. The results of bioassays indicated that compounds containing α-chloromethyl-N-benzyl and compounds containing 4,5-dihydrooxazole showed high insecticidal activity against cotton bollworm. Especially, stomach activities of compounds Ij, Il, and IIe were 60% at 5 mg kg(-1). Moreover, the target compounds exhibited high selectivity between cotton bollworm and diamondback moth, although both of them belong to the order Lepidoptera. Although the activities against diamondback moth were at a low level, some of the target compounds exhibited antifeedant activity. The compounds also had good activities against bean aphid, mosquito, and spider mite. The foliar contact activity of compounds Ic, Id, Ie, and IIf against bean aphid were 95, 95, 100, and 95%, respectively, at 200 mg kg(-1). The miticidal and ovicidal activities of compound IIi against spider mite were both 95% at 200 mg kg(-1). Furthermore, a trivial change at 4-position of pyrazole ring would lead to great changes in properties and activities, which can easily be deduced by comparing the activities of compounds in series I (4-chloro-pyrazole compounds) with corresponding compounds in series II (4-hydro-pyrazole compounds), especially from the miticidal and ovicidal activities of Ii and IIi against spider mite.     

Purification and characterization of α-galactosidase from white chickpea (Cicer arietinum)

Glycosylated α-galactosidase (melibiase) has been purified from white chickpea ( Cicer arietinum ) to 340-fold with a specific activity of 61 units/mg. Cicer α-galactosidase showed a M(r) of 45 kDa on SDS-PAGE and by MALDI-TOF. The optimum pH and temperature with pNPGal were 4.5 and 50 °C, respectively. The K(m) for hydrolysis of pNPGal was 0.70 mM. Besides hydrolyzing the pNPGal, Cicer α-galactosidase also hydrolyzed natural substrates such as melibiose, raffinose, and stachyose very effectively; hence, it can be exploited commercially for improving the nutritional value of soy milk. Galactose was found to be a competitive inhibitor. The property of this enzyme to cleave the terminal galactose residues can be utilized for converting the group B erythrocytes to group O erythrocytes.     

Cross-linking behavior and foaming properties of bovine α-lactalbumin after glycation with various saccharides

α-Lactalbumin was glycated via the Maillard reaction in the dry state using various mono- and oligosaccharides. The reaction resulted not only in coupling of the saccharides to α-lactalbumin but also in cross-linked proteins. The glycation rate and the extent of cross-link formation were highly dependent on the saccharide used. Glycation by arabinose and xylose led to a very fast protein cross-link formation, whereas glucose showed a relatively low protein cross-linking ability. The stability of foams, created using the various glycated protein samples, depended on the type of saccharide used, the extent of glycation, and possibly the amount of cross-linked protein. Compared to nonmodified α-lactalbumin, glycation with rhamnose and fucose improved foam stability, whereas application of glucose, galacturonic acid, and their oligosaccharides did not exert a clear effect. Mass spectrometric analysis revealed that dehydration of the Amadori products is an indicator of the formation of protein cross-links.     

Physicochemical properties of β and α'α subunits isolated from soybean β-conglycinin

Soy protein has shown great potential for use in biobased adhesives. β-Conglycinin is a major component of soy protein; it accounts for 30% of the total storage protein in soybean seeds. β-Conglycinin was isolated and purified, and its subunits' (β, α'α) physicochemical and adhesive properties were characterized. Crude β-conglycinin was isolated from soy flour and then purified by the ammonium sulfate precipitation method. The α'α and β subunits were isolated from the purified β-conglycinin by anion exchange chromatography. Yields of α'α subunits and β subunits from 140 g of soy flour were 1.86 g (1.3%) and 0.95 g (0.67%), respectively. The minimum solubility for α'α subunits, β subunits, and β-conglycinin occurred in pH ranges of 4.1-5.4, 3.5-7.0, and 4.8-5.3, respectively. Transmission electron microscopy showed that the β subunits existed as spherical hydrophobic clusters, whereas α'α subunits existed as uniformly discrete particles at pH 5.0. Differential scanning calorimetry showed that β subunits had higher thermal stability than α'α subunits. The pH had a lesser effect on adhesion strength of the β subunits than on that of the α'α subunits. The adhesives made from β subunits also showed greater water resistance than those from α'α subunits and β-conglycinin. Soy protein rich in β subunits is likely a good candidate for developing water-resistant adhesives.     

Effect of Protease Treatment Before Hydrolysis with α-Amylase on the Rate of Starch and Protein Hydrolysis of Maize,Whole Sorghum,and Decorticated Sorghum

We studied the effect of sorghum decortication and protease treatment on starch hydrolysis before liquefaction with thermoresistant α-amylase and the generation of free amino nitrogen (FAN) in preparation for subsequent steps of ethanol production. A bifactorial experiment with a level of confidence of P < 0.05 was designed to study differences among maize, whole sorghum, and decorticated sorghum and the effectiveness of the protease treatment before starch liquefaction. Sorghum was decorticated 9.7% to remove most of the pericarp and part of the germ and increase starch concentration. Starch concentration increased in decorticated kernels, whereas total phenols, fiber, and fat decreased. The decorticated sorghum had significantly higher starch and protein hydrolysis compared with the whole kernel. Protease treatment before liquefaction improved the rate of starch hydrolysis, especially in mashes from whole and decorticated sorghums. Whole and decorticated sorghum hydrolyzates treated with protease contained ≈50% more reducing sugars than the untreated counterparts. Maize yielded hydrolyzates with the the highest amount of FAN, followed by decorticated and whole sorghums. The maize and both sorghum hydrolyzates treated with protease contained ≈60 and 30% more FAN compared with the untreated counterparts. Both sorghum decortication and protease treatments before hydrolysis with α-amylase are recommended to increase ethanol yields, save processing time (and therefore energy), and to produce mashes with higher FAN content, which is considered as an important yeast substrate.     

Integrated effect of potassium humate and α-tocopherol applications on soil characteristics and performance of Phaseolus vulgaris plants grown on a saline soil

Soil salinity is one of the major problems of agriculture that limits plant performance, particularly in arid and semiarid regions. Therefore, the effect of potassium humate (KH) and α-tocopherol (TOC), used singly or in integration, on soil characteristics, and on plant performance, physio-biochemical attributes and antioxidative defense system of Phaseolus vulgaris L. plants grown under salt stress (EC = 6.35–6.42 dS m^?1) was investigated. Half g KH kg^?1 soil was used as soil amendment before sowing and 1.0 mM TOC was used as foliar spray twice; at 25 and 40 days after sowing. Results showed that, KH significantly improved soil physical and chemical properties, which positively reflected on plant growth and productivity, physio-biochemical attributes, mineral nutrients (N, P, K and Ca), osmoprotectants (soluble sugars and proline), non-enzymatic (ascorbic acid, glutathione and TOC) and enzymatic (superoxide dismutase, catalase and guaiacol peroxidase (GPOX)) antioxidants compared to untreated controls. The single TOC foliar application recorded the same positive results of KH. Integrated KH + TOC treatment was most effective compared to the single treatments. The above results recommended benefits of this integrated KH + TOC for the possibility of sustainable agronomic performance of common beans grown on saline soils.     

Isolation and identification of sea buckthorn (Hippophae rhamnoides) phenolics with antioxidant activity and α-glucosidase inhibitory effect

This study was performed to evaluate the antioxidant and α-glucosidase inhibitory effects from the extract, fractions, and isolated compounds of sea buckthorn leaves. Six compounds, kaempferol-3-O-β-D-(6'-O-coumaryl) glycoside, 1-feruloyl-β-D-glucopyranoside, isorhamnetin-3-O-glucoside, quercetin 3-O-β-D-glucopyranoside, quercetin 3-O-β-D-glucopyranosyl-7-O-α-L-rhamnopyranoside, and isorhamnetin-3-O-rutinoside, were isolated from sea buckthorn leaf extracts. The butanol fraction (EC(50) = 1.81 μg/mL) along with quercetin 3-O-β-D-glucopyranoside (EC(50) = 1.86 μg/mL) had a higher DPPH radical-scavenging activity and showed stronger reducing power (OD(700) = 1.83 and 1.78, respectively). The butanol fraction (477 mg GAE/g) contained the highest amount of phenolic compounds and also the most powerful α-glucosidase inhibitory effect (86%) at 5 μg/mL. The results indicate that sea buckthorn leaf extracts could potentially be used for food additives and the development of useful natural compounds.     

Profiles and α-amylase inhibition activity of proanthocyanidins in unripe Manilkara zapota (chiku)

Proanthocyanidins in unripe Manilkara zapota (chiku) were isolated using solvent extraction followed by Sephadex LH-20 fractionation with a yield of 0.9%. HPLC analysis using a diol column revealed well-resolved oligomers ranging from dimer to hexamer. The majority of the proanthocyanidins are composed of higher-degree oligomers appearing as one large peak in the chromatogram. Analysis of the proanthocyanidins using LC/MS showed that (epi)gallocatechins were the dominant extension unit in the proanthocyanidins. In agreement with this result, thiolysis treatment of the proanthocyanidins using mercaptoacetic acid produced thioether derivatives of (epi)gallocatechins as the major product and (epi)gallocatechin gallate derivatives as the minor product. The mean of the degree of polymerization was estimated to be 9.0. From MALDI-TOF MS, B-type gallocatechin oligomers up to decamer could be detected. The unripe chiku proanthocyanidins are thus good starting material for preparation of (epi)gallocatechin derivatives. The proanthocyanidins was shown to inhibit α-amylase with an IC(50) value of 4.2 ± 0.2 μg/mL and inhibit α-glucosidase with an IC(50) of 16.6 ± 0.3 μg/mL.     

Incorporation of 15N-labeled ammonia into glutamine amide groups by protein-glutaminase and analysis of the reactivity for α-lactalbumin

Protein-glutaminase (PG) is an enzyme that catalyzes the deamidation of protein-bound glutamine residues. We found that an enzyme labeling technique (ELT), which is a stable isotope labeling method based on transglutaminase (TGase) reaction, is applicable for PG. PG catalyzed incorporation of (15)N-labeled ammonium ions into reactive glutamine amide groups in α-lactalbumin similarly to TGase and deamidated the most reactive glutamine amide group once labeled with (15)N. Furthermore, we investigated the effect of ammonium ions on the PG activity by peptide mapping, and more reactive glutamine residues were detected than were detected by the ELT in the presence of ammonium ions. This is probably because ammonium ions are competitive inhibitors, causing decreased reactivity for glutamine residues. We propose the reaction scheme of PG in the presence of the (15)N-labeled ammonium ions and show that the ELT method with PG is useful for evaluating the activity of PG.     

Similarity of fine specificity of IgA anti-gliadin antibodies between patients with celiac disease and humanized α1KI mice

Gliadins, and primarily α-gliadins containing several sequences such as aa 31-49, aa 56-88 (33-mer), aa 57-68, and aa 69-82, are critical in the induction of immune response or toxic reaction leading to the development of celiac disease (CLD). The role of IgA anti-gliadin antibodies (IgA AGA) is unknown. To this end, we prepared several humanized monoclonal IgA AGA using transgenic α1KI mice. Employing Pepscan with overlapping decapeptides of α-gliadin we observed a robust similarity between the specificity of humanized mouse monoclonal IgA AGA and IgA AGA from patients with florid CLD. The common immunodominant region included several sequential epitopes localized in the N-terminal part of α-gliadin (QFQGQQQPFPPQQPYPQPQPFP, aa 29-50, and QPFPSQQPYLQL, aa 47-58). Notably, IgA AGA produced by clones 8D12, 15B9, 9D12, and 18E2 had significant reactivity against sequences localized in the 33-mer, LQLQPFPQPQ (aa 56-65) and PQLPYPQPQPFL (aa 69-80). Humanized mouse monoclonal IgA AGA that have a known specificity are suitable as standard in ELISAs to detect serum IgA AGA of CLD patients and for studying the AGA pathogenic role in CLD, especially for analyzing the translocation of complex of specific IgA antibodies and individual gliadin peptides through enterocyte barrier.     

Extracts of Maqui ( Aristotelia chilensis ) and Murta ( Ugni molinae Turcz.): sources of antioxidant compounds and α-Glucosidase/α-Amylase inhibitors

The objective of this work was to evaluate the antioxidant and antihemolytic activities of crude, aqueous, and organic-aqueous extracts of maqui ( Aristotelia chilensis ) and murta ( Ugni molinae Turcz.), together with their inhibiting effect on enzymes involved in the metabolism of carbohydrates. Radical scavenging activity, inhibition of linoleic acid oxidation in a micellar system, antihemolytic activity, and inhibition of α-amylases and α-glucosidases were analyzed. Crude extracts of maqui leaves and fruits were found to be important sources of polyphenolic compounds, showing 69.0 ± 0.9 and 45.7 ± 1.1 mg GAE/g dm, respectively. Polyphenols from maqui leaves were active as antioxidants and antihemolytic compounds (p < 0.05), showing a noncompetitive inhibiting effect on α-glucosidase. Flavan-3-ol polymers and glycosylated flavonols, such as quercetin glucoside and kaempferol glucoside, were tentatively identified in extracts. This preliminary observation provides the basis for further examination of the suitability of polyphenol-enriched extracts from maqui and murta as nutritional or medicinal supplements with potential human health benefits.     

In vitro digestibility of α-casozepine, a benzodiazepine-like peptide from bovine casein, and biological activity of its main proteolytic fragment

α-Casozepine is a peptide, corresponding to the sequence 91-100 of the bovine α(s1)-casein, displaying anxiolytic activity in the rat. The α(s1)-casein tryptic hydrolysate containing this peptide decreases stress effects after oral administration in various species including man. Therefore, the stability of this peptide toward gastric and pancreatic proteases has been assessed by using pepsin, chymotrypsin/trypsin, Corolase PP, pepsin followed by chymotrypsin/trypsin or pepsin followed by Corolase PP. α-Casozepine was slowly degraded by chymotrypsin, much more sensitive to pepsin and Corolase PP but not completely destroyed after 4 h kinetics. The bonds in the region 91 to 95 of the α-casozepine were totally resistant to hydrolysis by all studied proteases. Surprisingly, a fragment, corresponding to the sequence 91-97 and found in all the hydrolysis media in significant amount, possessed an anxiolytic activity in three behavioral tests measuring this parameter. This peptide could participate in the in vivo activity of α-casozepine.