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1.
The inactivation of apple pectin methylesterase (PME) with dense phase carbon dioxide (DPCD) combined with temperatures (35-55 degrees C) is investigated. DPCD increases the susceptibility of apple PME to the temperatures and the pressures have a noticeable effect on apple PME activity. A labile and stable fraction of apple PME is present and the inactivation kinetics of apple PME by DPCD is adequately described by a two-fraction model. The kinetic rate constants k L and k S of labile and stable fractions are 0.890 and 0.039 min (-1), and the decimal reduction times D L and D S are 2.59 and 58.70 min at 30 MPa and 55 degrees C. Z T representing temperature increase needed for a 90% reduction of the D value and the activation energy E a of the labile fraction at 30 MPa is 22.32 degrees C and 86.88 kJ /mol, its Z P representing pressure increase needed for a 90% reduction of the D value and the activation volume V a at 55 degrees C is 21.75 MPa and -288.38 cm (3)/mol. The residual activity of apple PME after DPCD exhibits no reduction or reactivation for 4 weeks at 4 degrees C.  相似文献   

2.
The Brassicaceae plant family contains high concentrations of glucosinolates, which can be hydrolyzed by myrosinase yielding products having an anticarcinogenic activity. The pressure and temperature stabilities of endogenous broccoli myrosinase, as well as of the synthetic isothiocyanates sulforaphane and phenylethyl isothiocyanate, were studied in broccoli juice on a kinetic basis. At atmospheric pressure, kinetics of thermal (45-60 degrees C) myrosinase inactivation could be described by a consecutive step model. In contrast, only one phase of myrosinase inactivation was observed at elevated pressure (100-600 MPa) combined with temperatures from 10 up to 60 degrees C, indicating inactivation according to first-order kinetics. An antagonistic effect of pressure (up to 200 MPa) on thermal inactivation (50 degrees C and above) of myrosinase was observed indicating that pressure retarded the thermal inactivation. The kinetic parameters of myrosinase inactivation were described as inactivation rate constants (k values), activation energy (Ea values), and activation volume (Va values). On the basis of the kinetic data, a mathematical model describing the pressure and temperature dependence of myrosinase inactivation rate constants was constructed. The stability of isothiocyanates was studied at atmospheric pressure in the temperature range from 60 to 90 degrees C and at elevated pressures in the combined pressure-temperature range from 600 to 800 MPa and from 30 to 60 degrees C. It was found that isothiocyanates were relatively thermolabile and pressure stable. The kinetics of HP/T isothiocyanate degradation could be adequately described by a first-order kinetic model. The obtained kinetic information can be used for process evaluation and optimization to increase the health effect of Brassicaceae.  相似文献   

3.
A combined high-pressure carbon dioxide (HP-CO 2) and thermal degradation reaction of betanin and isobetanin in aqueous solution was investigated and can be described by a first-order decay. At 45 degrees C, the degradation rate constant ( k) for each pigment component significantly increased (the half-life ( t 1/2) decreased, p < 0.05) with elevated pressure. Furthermore, HP-CO 2 treatment led to lower k values (higher t 1/2 values) than thermal treatment. However, k and t 1/2 values approached those of thermal treatment when the pressure was >30 MPa combined with temperatures exceeding 55 degrees C. Moreover, betanin was more stable than isobetanin under HP-CO 2. E a values ranged from 94.01 kJ/mol for betanin and 97.16 kJ/mol for isobetanin at atmospheric pressure to 170.83 and 142.69 kJ/mol at 50 MPa, respectively. A higher pressure and temperature as well as longer exposure time resulted in higher values of L*, b*, C*, and h degrees . HP-CO 2 induced more degradation products from betanin and isobetanin than thermal treatment with an identical temperature and exposure time.  相似文献   

4.
The rate of isomerization of alpha acids to iso-alpha acids (the compounds contributing bitter taste to beer) was determined across a range of temperatures (90-130 degrees C) to characterize the rate at which iso-alpha acids are formed during kettle boiling. Multiple 12 mL stainless steel vessels were utilized to heat samples (alpha acids in a pH 5.2 buffered aqueous solution) at given temperatures, for varying lengths of time. Concentrations of alpha acids and iso-alpha acids were quantified by high-pressure liquid chromatography (HPLC). The isomerization reaction was found to be first order, with reaction rate varying as a function of temperature. Rate constants were experimentally determined to be k1 = (7.9 x 10(11)) e(-11858/T) for the isomerization reaction of alpha acids to iso-alpha acids, and k2 = (4.1 x 10(12)) e(-12994/T) for the subsequent loss of iso-alpha acids to uncharacterized degradation products. Activation energy was experimentally determined to be 98.6 kJ per mole for isomerization, and 108.0 kJ per mole for degradation. Losses of iso-alpha acids to degradation products were pronounced for cases in which boiling was continued beyond two half-lives of alpha-acid concentration.  相似文献   

5.
Degradation parameters of purified anthocyanins from purple-fleshed potato (cv. Purple Majesty) heated at high temperatures (100-150 °C) were determined. Purified anthocyanins, prepared by removing salts, sugars, and colorless nonanthocyanin phenolics from the crude extract, were monitored and quantified using HPLC and spectrophotometry for heat-induced degradation products. Separation of colorless phenolics from the anthocyanins was confirmed using HPLC at two wavelengths, 280 and 520 nm. The degradation kinetics of purified anthocyanins followed a first-order reaction with reaction rate constants (k values) of 0.0262-0.2855 min(-1), an activation energy of 72.89 kJ/mol, thermal death times (D values) of 8.06-8789 min, and a z value of 47.84 °C over the temperature range of 100-150 °C. The enthalpy and entropy of activation were 59.97 kJ/mol and -116.46 J/mol·K, respectively. The antioxidant capacity in the purified anthocyanins, measured by DPPH and ABTS assays, was increased after the thermal treatment, indicating antioxidant activities of degradation products in the samples.  相似文献   

6.
The thermal stability of phosphatidylcholine (PC) liposomes (colloidal dispersions of bilayer-forming polar lipids in aqueous solvents) in the presence and absence of the antimicrobial polypeptide nisin was evaluated using differential scanning calorimetry (DSC) and low-intensity ultrasonic spectroscopy (US). PC liposome mixtures with varying acyl chain lengths (C16:0 and C18:0) were formed in buffer with or without entrapped nisin. Gel-to-liquid crystalline phase transition temperatures (T(M)) of liposomes determined from DSC thermograms were in excellent agreement with those determined by ultrasonic velocity and attenuation coefficient measurements recorded at 5 MHz. The dipalmitoylphosphatidylcholine (DPPC) T(M) measured by DSC was approximately 41.3 and approximately 40.7 degrees C when measured by ultrasonic spectroscopy. The T(M) of distearoylphosphatidylcholine (DSPC) and DPPC/DSPC 1:1 liposomes was 54.3 and 54.9 degrees C and approximately 44.8 and approximately 47.3 degrees C when measured by DSC and US, respectively. The thermotropic stability generally increased upon addition of nisin. Analysis of the stepwise decrease in ultrasonic velocity with temperature indicated an increased compressibility corresponding to a loss of structure upon heating.  相似文献   

7.
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.  相似文献   

8.
Degradation of the major alkamides in E. purpurea extracts was monitored under four different accelerated storage conditions, phenolic-depleted and phenolic-rich dry E. purpurea extracts and phenolic-depleted and phenolic-rich DMSO E. purpurea extracts at 70, 80, and 90 degrees C. Degradation of alkamides followed apparent first-order reaction rate kinetics. Alkamides degraded faster in dry films than in DMSO solution. The phenolic acids acted as antioxidants by limiting the loss of the alkamides in dry E. purpurea extracts. In contrast, E. purpurea alkamides in DMSO degraded faster when the phenolic fraction was absent. The overall order of degradation rate constants was alkamides 1 approximately 2 approximately 6 > 9 approximately 8 > 3 approximately 5 approximately 7. The energy of activation (Ea) predicted for alkamide degradation averaged 101 +/- 12 kJ/mol in dry films +/- phenolic acids, suggesting the oxidation mechanism was the same under both conditions. In DMSO solutions, Ea values were about one-half of those in dry films (61 +/- 14 kJ/mol), suggesting a different mechanism for alkamide oxidation in solution compared to dry. Predicted half-lives for alkamides in extracts suggested very good stability.  相似文献   

9.
This study examined the temperature and pH dependence of the in vitro autoxidation rate of bovine, ovine, porcine, and cervine oxymyoglobin that had been isolated and purified from three muscles of different oxidative stability--Longissimus dorsi, Gluteus medius, and Biceps femoris. To avoid obtaining unreliable estimates of autoxidation rate as has occurred in many previous studies, in this study, precautions were taken to eliminate the effects of freezing, chemical reduction with hydrosulfite, and contaminating metal ions on the reaction rate. When these precautions were taken, the rate constants for the different myoglobins studied were similar to each other but were 2-7-fold lower, and the Ea (activation energy) was 20-100% higher than that reported in most previous studies. The type of muscle the myoglobin was isolated from had no effect on the reaction rate or the Ea; however, the species did have a significant effect (p < 0.05) with porcine myoglobin having a 10% lower reaction rate and a 20% lower Ea than myoglobin from the other species. Increasing the reaction pH from 5.50 to 6.50 produced an exponential increase in reaction rate but only a small curvilinear change in Ea that had a maximum at pH 6.00.  相似文献   

10.
The influence of succinylation on lysozyme is studied using circular dichroism, fluorescence spectroscopy, and differential scanning calorimetry. The spectroscopic data reveal that at room temperature the structures of succinylated lysozyme and native lysozyme are similar. However, the calorimetric results show that the thermal stability of succinylated lysozyme is lower than that of native lysozyme. For succinylated lysozyme, the denaturation temperature (Td) varies in the range of 325-333 K (52-60 degrees C) and the associated denaturation enthalpy (DeltadenH) varies between 225 and 410 kJ/mol. For lysozyme, Td is 342-349 K (69-76 degrees C) and DeltadenH is 440-500 kJ/mol. From these data, the change in the heat capacity (DeltadenCp) upon thermal denaturation is derived. For lysozyme, DeltadenCp is 7.5 kJ/mol/K, and for succinylated lysozyme, it is 16.7 kJ/mol/K. The value of DeltadenCp for lysozyme is comparable to previously reported values. The high value of DeltadenCp for succinylated lysozyme is explained in terms of an extended degree of unfolding of the secondary structure and exposure of the apolar parts of the succinyl groups. Furthermore, the Gibbs energy of denaturation, as a function of temperature, derived from the thermodynamic analysis of the calorimetric data, indicates a cold-denaturated state of succinylated lysozyme below 20 degrees C. However, because a denatured state at low temperatures could not be detected by CD or fluorescence measurements, the native state may be considered to be metastable at those conditions.  相似文献   

11.
Low-temperature blanching of vegetables activates the enzyme pectin methylesterase (PME), which demethylates cell wall pectins and improves tissue firmness. This temperature activation of PME has been investigated by measuring the formation of methanol in intact tissue of green beans and tomatoes. Rates of methanol formation at temperatures of 35-65 degrees C were obtained by measuring the release of methanol from thin slices of tomato pericarp or green bean pod material. Activation energies of 112 and 97 kJ mol(-1) were calculated for PME activity in green beans and tomatoes, respectively. These activation energies indicate that the rate of pectin demethylation at 65 degrees C will be nearly 100 times that at 25 degrees C. PME activity was also determined titrimetrically using a solubilized form of the enzyme and purified pectin at temperatures from 30 to 60 degrees C. Under these conditions, much lower activation energies of 37 and 35 kJ mol(-1) were obtained for green beans and tomatoes, respectively. Methanol accumulation during heating of whole intact green beans was also determined and yielded an activation energy similar to that obtained with sliced beans. Whole green beans held at room temperature did not accumulate any methanol, but sliced or homogenized beans did. If whole beans were first heated to 45 degrees C and then cooled, methanol accumulation was observed at room temperature. These results indicate that two factors contribute to the observed high rate of pectin de-esterification during low-temperature blanching: (1) An irreversible change, causing PME to become active, occurs by heating to > or = 45 degrees C. (2) The high activation energy for pectin de-esterification means that the rate of de-esterification increases substantially with increasing temperature.  相似文献   

12.
Virgin olive oil samples with similar oxidative stabilities and fatty acid compositions were stored for 24 months. Changes in the lipid substrate were followed by peroxide value and K(232) measurements. HPLC was used to evaluate changes in the alpha-tocopherol, pigment, and squalene contents. Total polar phenol content was measured colorimetrically. The loss of alpha-tocopherol and carotenoids was comparable with that of polar phenol content, suggesting an active participation in autoxidation. The limited role of squalene in autoxidation was further confirmed using an olive oil model and in the presence of alpha-tocopherol. Pheophytin a degradation was high, although spectrometric estimation of chlorophyll content did not indicate so. Evaluation of pheophytin a activity at three different levels of addition on the oil model indicated a concentration-dependent antioxidant role more pronounced at elevated temperatures, which could be partially due to the activity of certain degradation products.  相似文献   

13.
The reactivity of purine derivatives (uric acid, xanthine, hypoxanthine, and purine) toward triplet-excited riboflavin in aqueous solution at pH 6.4 is described on the basis of kinetic (laser flash photolysis), electrochemical (square-wave voltammetry), and theoretical data (density functional theory, DFT). Direct deactivation of triplet-excited riboflavin in aqueous solution, pH 6.4 at 24 degrees C, in the presence of uric acid, xanthine, and hypoxanthine strongly suggests a direct electron transfer from the purine to the triplet-excited riboflavin with k = 2.9 x 10(9) M(-1) s(-1) (DeltaH(++) = 14.7 kJ mol(-1), DeltaS(++) = -15.6 J mol(-1) K(-1)), 1.2 x 10(9) M(-1) s(-1) (DeltaH(++) = 34.3 kJ mol(-1), DeltaS(++) = +45.3 J mol(-1) K(-1)), and 1.7 x10(8) M(-1) s(-1) (DeltaH(++) = 122 kJ mol(-1), DeltaS(++) = +319 J mol(-1) K(-1)), respectively. From the respective one-electron oxidation potentials collected in aqueous solution at pH 6.4 for uric acid (E = +0.686 vs normal hydrogen electrode, NHE), xanthine (E = +1.106 vs NHE), and hypoxanthine (E = +1.654 vs NHE), the overall free energy changes for electron transfer from the quencher to the triplet-excited riboflavin are as follows: uric acid (DeltaG(o) = -114 kJ mol(-1)), xanthine (DeltaG(o) = -73.5 kJ mol(-1)), hypoxanthine (DeltaG(o) = -20.6 kJ mol(-1)), and purine (DeltaG(o) > 0). The inertness observed for purine toward triplet-excited riboflavin corroborates with its electrochemical inactivity in the potential range from 0 up to 2 V vs NHE. These data are in agreement with the DFT results, which show that the energy of the purine highest occupied molecular orbital (HOMO) (-0.2685 arbitrary unit) is lower than the energy of the semioccupied molecular orbital (SOMO) (-0.2557 a.u.) of triplet-excited riboflavin, indicating an endergonic process for the electron-transfer process. The rate-determining step for deactivation by purine derivatives can be assigned to an electron transfer from the purine derivative to the SOMO orbital of the triplet-excited riboflavin. The results show that uric acid may compete with oxygen and other antioxidants to deactivate triplet-excited riboflavin in milk serum and other biological fluids leading to a free radical process.  相似文献   

14.
Oil-in-water emulsions containing cationic droplets stabilized by lecithin-chitosan membranes were produced using a two-stage process. A primary emulsion containing anionic lecithin-coated droplets was prepared by homogenizing oil and emulsifier solution using a high-pressure valve homogenizer (5 wt % corn oil, 1 wt % lecithin, 100 mM acetic acid, pH 3.0). A secondary emulsion containing cationic lecithin-chitosan-coated droplets was formed by diluting the primary emulsion with an aqueous chitosan solution (1 wt % corn oil, 0.2 wt % lecithin, 100 mM acetic acid, and 0.036 wt % chitosan). The stabilities of the primary and secondary emulsions with the same oil concentration to thermal processing, freeze-thaw cycling, high calcium chloride concentrations, and lipid oxidation were determined. The results showed that the secondary emulsions had better stability to droplet aggregation during thermal processing (30-90 degrees C for 30 min), freeze-thaw cycling (-10 degrees C for 22 h/30 degrees C for 2 h), and high calcium chloride contents (相似文献   

15.
Using 2,2-azino-bis(3-ethylbenzthiazoline-6-sulfonate) (ABTS) as substrate, it has been shown that the increased peroxidase activity for decreasing pH of myoglobin activated by hydrogen peroxide is due to a protonization of ferrylmyoglobin, MbFe(IV)=O, facilitating electron transfer from the substrate and corresponding to pK(a) approximately 5.2 at 25.0 degrees C and ionic strength 0.16, rather than due to specific acid catalysis. On the basis of stopped flow absorption spectroscopy with detection of the radical cation ABTS(.+), the second-order rate constant and activation parameters for the reaction between MbFe(IV)=O and ABTS were found to have the values k = 698 +/- 32 M(-1) s(-1), DeltaH# = 66 +/- 4 kJ mol(-1), and DeltaS# = 30 +/- 15 J mol(-1) K(-1) at 25.0 degrees C and physiological pH (7.4) and ionic strength (= 0.16 M NaCl). At a lower pH (5.8) corresponding to the conditions in meat, values were found as follows: k = 3.5 +/- 0.3 x 10(4) M(-1) s(-1), DeltaH# = 31 +/- 6 kJ mol(-1), and DeltaS# = -53 +/- 19 J mol(-1) K(-1), indicative of a shift from outersphere electron transfer to an innersphere mechanism. For steady state assay conditions, this shift is paralleled by a shift from saturation kinetics at pH 7.4 to first-order kinetics for H2O2 as substrate at pH 5.8. In contrast, the activation reaction between myoglobin and hydrogen peroxide was found at 25.0 degrees C to be slow and independent of pH with values of 171 +/- 7 and 196 +/- 19 M(-1) s(-1) found at physiological and meat pH, respectively, as determined by sequential stopped flow spectroscopy, from which a lower limit of k = 6 x 10(5) M(-1) s(-1) for the reaction between perferrylmyoglobin, .MbFe(IV)=O, and ABTS could be estimated. As compared to the traditional peroxidase assay, a better characterization of pseudoperoxidase activity of heme pigments and their denatured or proteolyzed forms is thus becoming possible, and specific kinetic effects on activation, substrate oxidation, or shift in rate determining steps may be detected.  相似文献   

16.
Tocopherols (alpha, beta, gamma, and delta) and Trolox were found to deactivate triplet-excited riboflavin in homogeneous aqueous solution (7:3 v/v tert-butanol/water) with second-order reaction rates close to diffusion control [k2 between 4.8 x 10(8) (delta-tocopherol) and 6.2 x 10(8) L mol(-1) s(-1) (Trolox) at 24.0 +/- 0.2 degrees C] as determined by laser flash photolysis transient absorption spectroscopy. In aqueous buffer (pH 6.4) the rate constant for Trolox was 2.6 x 10(9) L mol(-1) s1 and comparable to the rate constant found for ascorbate (2.0 x 10(9) L mol(-1) s(-1)). The deactivation rate constant was found to be inferior in heterogeneous systems as shown for alpha-tocopherol and Trolox in aqueous Tween-20 emulsion (approximately by a factor of 4 compared to 7:3 v/v tert-butanol/water). Neither beta-carotene (7:3 v/v tert-butanol/water and Tween-20 emulsion), lycopene (7:3 v/v tert-butanol/water), nor crocin (aqueous buffer at pH 6.4, 7:3 v/v tert-butanol/water, and Tween-20 emulsion) showed any quenching on the triplet excited state of riboflavin. Therefore, all carotenoids seem to reduce the formation of triplet-excited riboflavin through an inner-filter effect. Activation parameters were based on the temperature dependence of the triplet-excited deactivation between 15 and 35 degrees C, and the isokinetic behavior, which was found to include purine derivatives previously studied, confirms a common deactivation mechanism with a bimolecular diffusion-controlled encounter with electron (or hydrogen atom) transfer as rate-determining step. DeltaH for deactivation by ascorbic acid, Trolox, and homologue tocopherols (ranging from 18 kJ mol(-1) for Trolox in Tween-20 emulsion to 184 kJ mol(-1) for ascorbic acid in aqueous buffer at pH 6.4) showed a linear dependence on DeltaS (ranging from -19 J mol(-1) K(-1) for Trolox in aqueous buffer at pH 6.4 to +550 J mol(-1) K(-1) for ascorbic acid in aqueous buffer pH 6.4). Among photooxidation products from the chemical quenching, lumicrome, alpha-tocopherol quinones and epoxyquinones, and alpha-tocopherol dimers were identified by ESI-QqTOF-MS.  相似文献   

17.
Vanillin was found to be efficient as a deactivator of ferrylmyoglobin with a second-order rate constant of k(2) = 57 ± 1 L mol(-1) s(-1) for reduction to metmyoglobin with ΔH(?) = 58.3 ± 0.3 kJ mol(-1) and ΔS(?) = -14 ± 1 J mol(-1) K(-1) in aqueous pH 7.4 solution at 25 °C. Binding to β-lactoglobulin (βLG) was found to affect the reactivity of vanillin at 25 °C only slightly to k(2) = 48 ± 2 L mol(-1) s(-1) (ΔH(?) = 68.4 ± 0.4 kJ mol(-1) and ΔS(?) = 17 ± 1 J mol(-1) K(-1)) for deactivation of ferrylmyoglobin. Binding of vanillin to βLG was found to have a binding stoichiometry vanillin/βLG > 10 with K(A) = 6 × 10(2) L mol(-1) and an apparent total ΔH° of approximately -38 kJ mol(-1) and ΔS° = -55.4 ± 4 J mol(-1) K(-1) at 25 °C and ΔC(p, obs) = -1.02 kJ mol(-1) K(-1) indicative of increasing ordering in the complex, as determined by isothermal titration microcalorimetry. From tryptophan fluorescence quenching for βLG by vanillin, approximately one vanillin was found to bind to each βLG far stronger with K(A) = 5 × 10(4) L mol(-1) and a ΔH° = -10.2 kJ mol(-1) and ΔS° = 55 J mol(-1) K(-1) at 25 °C. The kinetic entropy/enthalpy compensation effect seen for vanillin reactivity by binding to βLG is concluded to relate to the weakly bound vanillin oriented through hydrogen bonds on the βLG surface with the phenolic group pointing toward the solvent, in effect making both ΔH(?) and ΔS(?) more positive. The more strongly bound vanillin capable of tryptophan quenching in the βLG calyx seems less or nonreactive.  相似文献   

18.
Kinetics of chlorophyll degradation and color loss in heated broccoli juice   总被引：2，自引：0，他引：2  
Degradation of chlorophyll in broccoli juice occurred at temperatures exceeding 60 degrees C. Chemical analysis revealed that degradation of chlorophyll a and b to pheophytin a and b, respectively, followed first-order kinetics and that chlorophyll a was more heat sensitive than chlorophyll b. Temperature dependencies of chlorophyll a and b degradation rate constants could be described by Arrhenius equations with activation energies (E(a)) of 71.04 +/- 4.89 and 67.11 +/- 6.82 kJ/mol, respectively. Objective greenness measurements, using the -a value as the physical property, together with a fractional conversion kinetic analysis, indicated that green color degradation followed a two-step process. Kinetic parameters for the first degradation step were in accordance with the kinetic parameters for pheophytinization of the total chlorophyll content, as determined by chemical analysis (E(a) approximately 69 kJ/mol). The second degradation step, that is, the subsequent decomposition of pheophytins, was characterized by an activation energy of 105.49 +/- 4.74 kJ/mol.  相似文献   

19.
The degradation rate and sorption characteristics of the triazolopyrimidine sulfonanilide herbicide florasulam and its principal degradation product 5-hydroxyflorasulam (5-OH-florasulam) were determined as a function of temperature and moisture in three different soils. The half-life for degradation of florasulam ranged from 1.0 to 8.5 days at 20-25 degrees C and from 6.4 to 85 days at 5 degrees C. The half-life for degradation of 5-OH-florasulam ranged from 8 to 36 days at 20-25 degrees C and from 43 to 78 days at 5 degrees C. The degradation rate of both compounds was strongly influenced by temperature, with activation energies ranging from 57 to 95 kJ/mol for florasulam and from 27 to 74 kJ/mol for 5-OH florasulam. Soil moisture content had negligible impact on the degradation rate. Apparent (nonequilibrium) sorption coefficients for florasulam and 5-OH-florasulam at 0 days after treatment (DAT) were 0.1-0.6 L/kg and increased linearly with time for both florasulam and 5-OH-florasulam (r(2) > 0.90) to levels as high as 12-23 L/kg. Heats of adsorption were calculated on one soil as a function of time. Heat of adsorption values for both florasulam and 5-OH-florasulam increased as incubation time increased and the amount of each compound decreased; values were near 0 kJ/mol initially and increased to a maximum of 91 and 66 kJ/mol for florasulam and 5-OH-florasulam, respectively.  相似文献   

20.
Pectinmethylesterase of navel oranges shows two fractions greatly differing in thermostability. The most thermostable fraction accounts for approximately 10% of total activity. The thermal inactivation of this fraction follows first-order kinetics both in 5 mM, pH 3.5, citrate buffer and in orange juice at the same pH, showing a z value of 5.1 degrees C and an activation energy (E(a)) of 435 kJ mol(-)(1) K(-)(1). The heat resistance of the enzyme is approximately 25-fold higher in the juice than in citrate buffer. When ascorbic acid, sucrose, glucose, and fructose are added to the citrate buffer at the concentrations found in orange juice, the heat resistance of the enzyme increases 3-fold. The addition of pectin at 0.01% concentration multiplies it by a factor of 50. Manothermosonication (MTS), the simultaneous application of heat and ultrasound under moderate pressure (200 kPa), at 72 degrees C, increases the inactivation rate 25 times in buffer and >400 times in orange juice. MTS inactivation shows a higher z value (35.7 degrees C) and lower E(a) (56.9 kJ mol(-)(1) K(-)(1)) than simple heating.  相似文献   

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