Inhibition of formaldehyde production in frozen-stored minced blue whiting (Micromesistius poutassou) muscle by cryostabilizers: an approach from the glassy state theory

Adding maltodextrins to minced blue whiting muscle inhibited formaldehyde production during storage at -10 and -20 degrees C. Sucrose, however, was effective only at -20 degrees C. These results were not proportional to the difference between the storage temperature and the ice-melting onset (T(m)'), and freeze-concentration had to be considered. In the face of serious limitations to do this, resource was made to the state diagram for the sucrose-water binary system and the percentage variation of the ice-melting endotherm area of the different samples. A higher T(m)' and a lower freeze-concentration would account for the inhibiting effects of maltodextrins, whereas sucrose, despite diminishing T(m)', had an effect nearly as great as maltodextrins at -20 degrees C but had hardly any at -10 degrees C. The reason for this seems to lie in a lower freeze-concentration of solutes in the unfrozen water phase. Similarly, the differences found between sucrose and maltodextrins, as well as among maltodextrins, were also explained in terms of T(m)' and freeze-concentration.     

Elucidation of the effect of formaldehyde and lipids on frozen stored cod collagen by FT-Raman spectroscopy and differential scanning calorimetry

The effect of frozen storage (-10 and -30 degrees C), formaldehyde, and fish oil on collagen, isolated from cod muscle, was investigated. Salt- and acid-soluble collagen fractions as well as insoluble collagen indicated changes in solubility on frozen storage. Differential scanning calorimetry (DSC) showed a highly cooperative transition at 28.2 degrees C for isolated collagen. Changes in the thermodynamic properties of collagen were observed on frozen storage at -10 degrees C compared with the control at -30 degrees C because of changes in structure. In the presence of formaldehyde, there were no changes in the DSC collagen transition; however, in the presence of fish oil there was an increase in enthalpy and an extra peak was observed at 44.6 degrees C, indicating collagen-fish oil interaction. Structural changes resulted in a decrease in the solubility of collagen in salt and acid solution. FT-Raman spectra obtained for collagen at -10 degrees C and -30 degrees C confirmed the alteration of the conformation of collagen not only at -10 degrees C but also in the presence of formaldehyde and fish oil.     

Interactive responses of gala apple fruit volatile production to controlled atmosphere storage and chemical inhibition of ethylene action

Gala apples exposed to the ethylene action inhibitor 1-methylcyclopropene (1-MCP) for 12 h at 20 degrees C were stored at 1 degrees C in air or a controlled atmosphere (CA) maintained at 1 kPa O2 and 2 kPa CO2. Volatile compounds were measured after 4, 12, 20, and 28 weeks plus 1 or 7 days at 20 degrees C. Treatment with 1-MCP and then storage in air or CA or storage in CA without 1-MCP treatment reduced volatile production as compared to apples not treated with 1-MCP stored in air. The reduced production of esters, alcohols, aldehydes, acetic acid, and 1-methoxy-4-(2-propenyl)benzene was observed. Ester production by fruit stored in CA decreased throughout the storage period regardless of previous 1-MCP treatment. The production of esters, alcohols, aldehydes, acetic acid, and 1-methoxy-4-(2-propenyl)benzene by 1-MCP-treated fruit stored in air plus 7 days at 20 degrees C increased after 20 or 28 weeks of storage. Continuous exposure to 417 micromol m(-3) ethylene for 7 days at 20 degrees C after 12 or 28 weeks of storage stimulated production of many volatile compounds, primarily esters and alcohols, by fruit stored in CA or 1-MCP-treated apples stored in air. However, exposure to ethylene had no effect on the production of aldehydes or acetic acid.     

Rotational and translational mobility of small molecules in sucrose plus polysaccharide solutions

The effect of different polysaccharides on the rotational (D(rot)) and translational diffusion (D(trans)) coefficients of small molecules in concentrated systems (sucrose solutions) was investigated. Dextran (1 or 10% w/w) with different molecular masses (from 10(4) to 2 x 10(6) Da), gum arabic, or pullulan was added to solutions of sucrose (57.5% w/w). Viscosity measurements of the diffusion medium studied (sucrose and sucrose plus polysaccharide) were made using a Rheometric Scientific viscometer in a temperature range from 20 to -10 degrees C. The rotational mobility of nitroxide radicals (Tempol) dispersed in the concentrated systems was measured by electron spin resonance. The translational diffusion coefficient of fluorescein was determined by the fluorescence recovery after photobleaching method. The studied temperature range for the latter two techniques was from 20 to -16 degrees C. For these conditions of concentration and temperature, there was no ice formation in the samples. No effect of the molecular mass of dextran on D(rot) and D(trans) was observed when solutions with the same dry matter content were compared. Only pullulan and gum arabic, at 10%, had a significant effect on D(trans)( )()of fluorescein. Temperature and total dry matter content were observed to be the most important factors controlling D(rot) and D(trans) in these concentrated systems.     

Biochemical and microbial changes during the storage of minimally processed cantaloupe

The effect of storage time on pH, titratable acidity, degrees Brix, organic acids, sugars, amino acids, and color of minimally processed cantaloupe melon (Cucumis melo L. var. reticulatus Naud. cv. Mission) was determined at 4 degrees C and 20 degrees C. Changes in most of the biochemical parameters with storage time were relatively slow at the lower temperature. At 20 degrees C, a 17% loss in soluble solids and a 2-fold increase in acidity occurred after 2 days. Organic acid content also increased considerably with time at this temperature as a result of the production of lactic acid. Oxalic, citric, malic, and succinic acids were the organic acids, and glucose, fructose, and sucrose were the sugars present in the freshly cut cantaloupe. Malic acid concentration decreased concurrently with lactic acid production indicating the possible involvement of anaerobic malo-lactic fermentation along with sugar utilization by lactic acid bacteria. The effect of storage on microbial growth was determined at 4, 10, and 20 degrees C. Gram-negative stained rods grew at a slower rate at 4 degrees C and 10 degrees C than the Gram-positive mesophilic bacteria that dominated microorganism growth at 20 degrees C. Eighteen amino acids were identified in fresh cantaloupe: aspartic acid, glutamic acid, asparagine, serine, glutamine, glycine, histidine, arginine, threonine, alanine, proline, tyrosine, valine, methionine, isoleucine, leucine, phenyl alanine, and lysine. The dominant amino acids were aspartic acid, glutamic acid, arginine, and alanine. Total amino acid content decreased rapidly at 20 degrees C, but only a slight decrease occurred at 4 degrees C after prolonged storage. Changes in lightness (L), chroma, and hue at both temperatures indicate the absence of browning reactions. The results indicate the potential use of lactic acid and lactic acid bacteria as quality control markers in minimally processed fruits.     

Limited enzymatic treatment of skim milk using chymosin affects the micelle/serum distribution of the heat-induced whey protein/kappa-casein aggregates

The effects of heat treatment and limited kappa-casein hydrolysis on the micelle/serum distribution of the heat-induced whey protein/kappa-casein aggregates were investigated as a possible explanation for the gelation properties of combined rennet and acid gels. Reconstituted skim milk was submitted to combinations of 0-67% hydrolysis of the kappa-casein at 5 degrees C and heat treatment at 90 degrees C for 10 min. The protein composition of the ultracentrifugal fractions was obtained by reverse-phase high-performance liquid chromatography (RP-HPLC). The aggregates contained in each phase were isolated by size-exclusion chromatography and analyzed by RP-HPLC and sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Upon heating only, 20-30% of the total kappa-casein dissociated, while 20-30% of the total whey protein attached to the micelles. When heated milk was renneted, little changes were observed in the distribution and composition of the aggregates. Conversely, the heat treatment of partially renneted milk induced the formation of essentially micelle-bound aggregates. The results were discussed in terms of the preferred interaction between hydrophobic para-kappa-casein and denatured whey proteins.     

Activity and process stability of purified green pepper (Capsicum annuum) pectin methylesterase

Pectin methylesterase (PME) from green bell peppers (Capsicum annuum) was extracted and purified by affinity chromatography on a CNBr-Sepharose-PMEI column. A single protein peak with pectin methylesterase activity was observed. For the pepper PME, a biochemical characterization in terms of molar mass (MM), isoelectric points (pI), and kinetic parameters for activity and thermostability was performed. The optimum pH for PME activity at 22 degrees C was 7.5, and its optimum temperature at neutral pH was between 52.5 and 55.0 degrees C. The purified pepper PME required the presence of 0.13 M NaCl for optimum activity. Isothermal inactivation of purified pepper PME in 20 mM Tris buffer (pH 7.5) could be described by a fractional conversion model for lower temperatures (55-57 degrees C) and a biphasic model for higher temperatures (58-70 degrees C). The enzyme showed a stable behavior toward high-pressure/temperature treatments.     

Steady-state kinetics and thermodynamics of the hydrolysis of beta-lactoglobulin by trypsin

Hydrolysis of beta-lactoglobulin (in an equimolar mixture of the A and B variant) by trypsin in neutral aqueous solution [pH 7.7 at 25 degrees C, ionic strength 0.08 (NaCl)] was followed by capillary electrophoresis and thermodynamic parameters derived from a Michaelis-Menten analysis of rate data obtained at 10, 20, 30, and 40 degrees C for disappearance of beta-lactoglobulin. Enthalpy of substrate binding to the enzyme and the energy of activation for the catalytic process were found to have the values, DeltaH(bind) = -28 +/- 4 kJ mol(-)(1) and E(a) = 51 +/- 18 kJ mol(-)(1), respectively. Thus, beta-lactoglobulin shows an enthalpy of activation for free substrate reacting with free enzyme of about 21 kJ mol(-)(1), corresponding to a transition state stabilization of 60 kJ mol(-)(1) when compared to acid-catalyzed hydrolysis. The catalytic efficiency of trypsin in hydrolysis of beta-lactoglobulin is increased significantly by temperature; however, this effect is partly counteracted by a weaker substrate binding resulting in an increase by only 25%/10 degrees C in overall catalytic efficiency.     

蛋白水解物改性脲甲醛缓释肥的结构及氮素释放特征

针对脲甲醛养分释放与作物生长曲线不匹配的问题,该研究采用蛋白水解物来改善脲甲醛的氮素释放率。土柱淋洗结果表明,蛋白水解物降低了脲甲醛初期的氮素释放率,加快了脲甲醛在后期的氮素释放率。在当量尿素与甲醛的摩尔比为1.2时,蛋白水解物水解度越小,氮素释放率越快。到第7周,蛋白水解物改性脲甲醛的氮素释放率和未改性的脲甲醛相比,氮素释放率提高了58.9%。采用傅里叶红外光谱、X射线衍射、热重和扫描电镜分析了蛋白水解物和蛋白水解物改性脲甲醛的结构,发现:蛋白水解物的活性基团能够与甲醛反应,并与尿素聚合,以嵌段的方式引入到脲甲醛的分子结构中;蛋白水解物水解度越低,改性脲甲醛结晶度降低的越多;和未改性的脲甲醛相比,改性的脲甲醛的最大分解温度有所降低,并且改性后的脲甲醛疏松多孔。因此,可以通过蛋白水解物的水解度来调控改性脲甲醛的氮素释放率,进而适应不同作物的生长周期,提高氮肥的利用率。     

Purification and characterization of trimethylamine-N-oxide demethylase from jumbo squid (Dosidicus gigas)

Trimethylamine-N-oxide demethylase (TMAOase) was purified from Jumbo squid (Dosidicus gigas) and characterized in detail herein. The TMAOase was extracted from squid with 20 mM Tris-acetate buffer (pH 7.0) containing 1.0 M NaCl, followed by acid treatment and heat treatment. Then it was purified by deithylaminoethyl-cellulose and Sephacryl S-300 chromatography, subsequently resulting in an 839-fold purification. The molecular mass of the TMAOase was defined to be 17.5 kDa. The optimum pH of the purified TMAOase was 7.0, and its optimum temperature was confirmed to be 55 degrees C. The TMAOase was stable to heat treatment up to 50 degrees C and stable at pH 7.0-9.0. Reducing agents such as DTT, Na2SO3, and NADH were effective at activating TMAOase, and ethylenediaminetetraacetic acid, as well as Mg2+ and Ca2+, could also enhance the activity of TMAOase remarkably, whereas the TMAOase could be significantly inhibited by tea polyphenol, phytic acid and acetic acid. In addition, the TMAOase converted TMAO to dimethylamine and formaldehyde stoichiometrically with a K(m) of 26.2 mM.     

Molecular structures of gellan gum imaged with atomic force microscopy in relation to the rheological behavior in aqueous systems in the presence or absence of various cations

Aqueous solutions of gellan gum with comparable molecular masses but with different acyl contents were investigated by atomic force microscopy and rheological measurements in the presence or absence of various cations. For a high-acyl sample, no continuous network structures were identified microscopically, except in the presence of Ca (2+), where structural inhomogeneity was the highest in terms of the height distribution of molecular assemblies. Rheological thermal hysteresis between sol-gel transitions was detected in the presence of K (+) and Ca (2+), particularly Ca (2+). The storage modulus at 20 degrees C was larger in the order Na (+) < Ca (2+) < K (+). For a low-acyl sample, continuous network structures were identified in the presence of each cation, involving greater thermal hysteresis than the corresponding data for the high-acyl sample. Structural homogeneity was the highest in the presence of K (+). Thermal hysteresis and elasticity of the system were discussed in terms of continuousness and homogeneity of network structures.     

Purification and characterization of calpastatin from grass prawn muscle (Penaeus monodon)

Calpastatin, a specific calpain inhibitor was purified to electrophoretical homogeneity from grass prawn (Penaeus monodon) muscle by 100 degrees C heat-treatment, DEAE-Sephacel, and Q-Sepharose chromatographs. No significant change in the inhibitory activity of crude calpastatin was observed even after 20 min incubation at 100 degrees C, pH 7.0. The purified prawn calpastatin had a molecular weight (M(r)) of 80 and 88.7 kDa determined by SDS-PAGE and Sephacryl S-200 HR gel filtration, respectively. According to the active site titration, the purified calpastatin revealed four beef mu-calpain and two beef m-calpain binding domains, respectively. It was stable during 1 h of incubation at 30 degrees C under pH 4.5-10.0 and shown to be a highly specific inhibitor for calpain.     

1-methylcyclopropene increases storability and shelf life in climacteric and nonclimacteric plums

The effect of 1-methylcyclopropene (1-MCP) at three different doses (0.25, 0.50, and 0.75 microL L(-1)) on the ripening processes of a climacteric, cv. Santa Rosa, and a suppressed climacteric type, cv. Golden Japan, plum was studied. For both cultivars, positive effects were observed in terms of inhibition of ethylene production and delays of the physical, chemical, and biochemical changes associated with ripening. 1-MCP-treated plums were firmer with lower weight loss, reduced degrees Brix/titratable acidity ratios, and lower color changes during cold storage and subsequent shelf life at 20 degrees C than controls. For most factors, the effectiveness of 1-MCP was dose-dependent in Santa Rosa but dose-independent for Golden Japan.     

The effects of frozen storage conditions on lycopene stability in watermelon tissue

The purpose of this investigation was to evaluate the rate of deterioration of lycopene in watermelon tissue during frozen storage, because little is known about the stability of watermelon tissue lycopene under cold storage conditions. Heart tissue from each of nine individual watermelons was stored at -20 or -80 degrees C as either small chunks or puree and periodically sampled over a year's time. Initial freeze-thaw experiments indicated that a small percentage of lycopene, approximately 4-6%, degraded during an initial freeze-thaw. Analyses of the samples showed a loss of approximately 30-40% lycopene over a year's storage at -20 degrees C and a loss of approximately 5-10% over the same period at -80 degrees C. Lycopene was slightly more stable in pureed compared with diced watermelon tissue at -20 degrees C, but not at -80 degrees C. The kinetic data were best fitted by application of two simultaneous, first-order decay processes. HPLC analysis of the samples after a year's storage suggested that beta-carotene was more stable during storage at -20 degrees C than was lycopene.     

Development of a method to study the migration of six photoinitiators into powdered milk

The aim of the present work was to develop a rapid multimethod for the analysis of six photoinitiators (PIs) in powdered milk and to study the migration of these PIs from LDPE packaging into powdered milk. The optimized HPLC-DAD method showed high correlation coefficients (>0.9999) over a concentration range of 0.1-10.9 mg/L. The kinetics of migration of the photoinitiators from LDPE packaging into powdered milk were determined at different temperatures. The key parameters of migration phenomena (diffusion and partition coefficients) were determined. The diffusion coefficients at 5 degrees C ranged between 8.4 x 10(-12) (for ITX) and 5.1 x 10(-10) (for benzophenone) and those at 40 degrees C between 5.9 x 10(-10) (for ITX) and 6.1 x 10(-9) (for Irgacure 184). The diffusion coefficients of the six model migrants under study increased with temperature and showed a good Arrhenius relationship between 5 and 40 degrees C.     

Thermospectroscopic study of the adsorption mechanism of the hydroxamic siderophore ferrioxamine B by calcium montmorillonite

The behavior of iron-chelating agents in soils is highly affected by interactions with the solid phase. Still this aspect is frequently ignored. In this research the adsorption of the siderophore ferrioxamine B by Ca-montmorillonite, as a free ligand (desferrioxamine B, DFOB) and as a complex with Fe3+ (ferrioxamine B, FOB), was studied, using thermo X-ray diffraction (thermo-XRD) in the temperature range 25-360 degrees C and thermo-FTIR spectroscopy in the temperature range 25-170 degrees C. The effect of pH (4-7.5) on the adsorption was examined. Extensive use of curve-fitting analysis was required due to significant overlapping of the characteristic absorption bands of the various functional groups. Thermo-XRD analysis showed that both DFOB and FOB penetrated into the interlayer space of Ca-montmorillonite. FTIR results indicated strong interactions of DFOB within the interlayer, which involved all functional groups (NH3+, secondary amide groups, and hydroxamate groups). In contrast, the folded Fe complex of FOB retained its molecular configuration upon adsorption, and the basal spacing of the clay increased correspondingly. FOB interacted in the interlayer space of the clay, mainly through the NH of the secondary amide groups and NH3+, while the functional groups bound to the central Fe cation remained unchanged. The suspension pH had no significant effect on both DFOB and FOB adsorption at the examined range. Adsorption protected the adsorbates from thermal degradation compared to the nonadsorbed samples up to 105 degrees C. At 170 degrees C both DFOB and FOB were already partially degraded, but to a lesser extent than the nonadsorbed samples. Degradation of the molecules occurred mainly through the hydroxamic groups, which constitute the Fe-chelating center in the hydroxamic siderophore.     

Adsorption of flavonoids on resins: cyanidin 3-glucoside

Adsorption of cyanidin-3-glucoside in aqueous batch solutions was studied at pH 3.5 and 20 degrees C using 13 commercial resins with different hydrophobicity, surface areas (SA, 330-1200 m2/g), and pore radii (PR, 20-260 A). The solute affinity toward different resins was described in terms of Langmuir and Freundlich parameters; experimental data were well-fitted to the two isotherms, which were both utilized to compare resins adsorption capacity. The styrene-divinylbenzene EXA-118 resin (SA, 1200 m2/g; PR, 90 A) showed the maximum effectiveness among the tested resins; a good efficacy for removing cyanidin 3-glucoside was shown also by EXA-90 (SA, 630 m2/g; PR, 105 A). Some experiments on a styrene-divinylbenzene resin and an acrylic one demonstrated that adsorption was not influenced by pH variations of the solution within the range of 1.0-4.5. For the 10 resins having PR < or = 105 A, correlation analysis evidenced the linear increasing dependence of Freundlich constant KF on physical characteristics of surface area and pore radius. The adsorption of cyanidin 3-glucoside at 20 degrees C was compared with that of hesperidin performed in batch runs on the same resins. Moreover, the best resin (EXA-118) was tested with a sample of pigmented orange juice to assess its performance in terms of selectivity, adsorption, and desorption capabilities on a real matrix.     

Thermo-FTIR spectroscopic study of the siderophore ferrioxamine B: spectral analysis and stereochemical implications of iron chelation, pH, and temperature

FTIR spectra of the microbial siderophore, ferrioxamine B, and its nonchelated form (iron free; desferrioxamine B) were studied to facilitate in-depth investigation on the undisrupted structure of the siderophore and its interactions with the environment. Effects of iron chelation as well as those of various levels of pH and temperature on the stereochemical structure of the free ligand and the ferric complex were examined. The presence of a number of functional groups in these compounds and the mutual interaction between them resulted in significant shifts and overlapping of their characteristic absorption bands. Thermal and pH treatments combined with a comprehensive use of curve-fitting analysis facilitated bands resolution. Absorption bands of all functional groups were identified. The results imply that the compact and rigid structure of the ferric complex (ferrioxamine B) is sustained by intense and specific intramolecular hydrogen bonds. Dehydration was the main process observed at low temperature (25-60 degrees C). At 105 degrees C the free ligand form (desferrioxamine B) had already begun to decompose, whereas ferrioxamine B exhibited stability. The thermal destruction became acute at the 170 degrees C treatment for both molecules. The secondary amide groups and the hydroxamate groups, which comprise the binding site for the Fe atom in the complex, were found to be the most sensitive to the thermal degradation. Significant pH effects were observed only for desferrioxamine B samples at pH 9, accompanied by partial decomposition, similar to that observed at 105 degrees C. Deprotonation of desferrioxamine B was found to begin with the deprotonation of the NH(3+) group. Characteristics of the rigid conformational structure of the ferric complex and the state of the NH(3+) group, both assumed to play an important role in the recognition and uptake of the siderophore by membranal receptors, were elaborated by means of FTIR and are discussed in detail.     

Effect of thermal treatment on the quality of cloudy apple juice

Apple juice from eight different varieties of apples was heated at high-temperature (60-90 degrees C) and short-time (20-100 s) (HTST) combinations. To determine the effect of heating conditions on enzymatic browning and cloud stability in apple juices, the activity of polyphenol oxidase and pectinesterase was analyzed and correlated with the thermal treatment conditions and the quality of the juice. Additional investigations included the measurement of pH value, soluble solid content, titratable acidity, color, and turbidity after 3 and 6 months. The results showed that HTST treatment at 80 degrees C already inactivated polyphenol oxidase, whereas pectinesterase activity was reduced to half and could even at 90 degrees C not be inactivated completely. In fact, highest residual pectinesterase activity was found at 60 degrees C. Heating at 70 degrees C caused stable pectinesterase activity and even a slight increase for 50 and 100 s heating times. Turbidity and lightness increased after HTST treatment. In particular, differences in cloud stability between the varieties were measured. HTST parameters did not correlate with the residual cloud stability after 6 months. The sensory evaluation revealed that only a few combinations were distinguishable. The best stability of cloud and color in relation to heat impact was achieved by HTST treatment between 70 degrees C/100 s and 80 degrees C/20 s.     

Effects of cryostabilizers, low temperature, and freezing on the kinetics of the pectin methylesterase-catalyzed de-esterification of pectin

The kinetics of the pectin methylesterase (PME)-catalyzed de-esterification of pectin was studied at 25 degrees C in the presence of sucrose, fructose, maltodextrin (DE = 16.5-19.5), and carboxymethylcellulose at different concentrations and in the presence of maltodextrin and sucrose at different concentrations in a temperature range between +25 and -4 degrees C in subcooled and frozen states. The objective was to determine whether the reaction is diffusion-controlled, to gain insight about the factors determining the diffusion of the reactants, and to determine the effect of the carbohydrates, low temperature, and freezing on the structural conformation of the enzyme. The results indicate that the PME-catalyzed de-esterification of pectin is diffusion-controlled. Nevertheless, the diffusion is not controlled by the macroviscosity of the reaction medium, but rather by the microviscosity experienced by the diffusants. Low temperature in the temperature range studied does not affect the structural conformation of the enzyme, while freezing seems to have some effect.