Improvement of functional properties of egg white protein through phosphorylation by dry-heating in the presence of pyrophosphate

Egg white protein (EWP) was phosphorylated by dry-heating in the presence of pyrophosphate at pH 3.0-7.0 and 85 degrees C for 1 and 5 days, and the functional properties of the phosphorylated EWP (PP-EWP) were investigated. The phosphorylation was accelerated with a decrease of pH from 7.0 to 3.0 and for heating times from 1 to 5 days. The phosphorus content of EWP increased approximately 1.05% by dry-heating at pH 4.0 and 85 degrees C for 5 days in the presence of pyrophosphate, which was higher than that of casein. The electrophoretic mobility of EWP increased with an increase in the phosphorylation level. The surface hydrophobicity of EWP increased by phosphorylation. The heat stability, emulsifying properties, and digestibility of EWP were improved by phosphorylation. The calcium phosphate-solubilizing ability of EWP was enhanced by phosphorylation. A firmer and transparent heat-induced gel of PP-EWP was obtained, and the water-holding capacity of heat-induced PP-EWP gel was higher that that of the control. These results suggest that phosphorylation by dry-heating in the presence of pyrophosphate is a useful method for improving the functional properties of EWP.     

Phosphorylation of egg white proteins by dry-heating in the presence of phosphate

Food proteins were phosphorylated by heating in a dry state in the presence of phosphate. When casein, whey protein isolate (WPI), and egg white proteins (EWP), which were lyophilized from their solutions in a phosphate buffer, were dry-heated at various temperatures and pH levels for 1-5 days, EWP was more highly phosphorylated than casein and WPI. Phosphorylation of EWP was promoted with a decrease of pH from 7.0 to 3.0 when the incubation temperature was raised from 55 to 100 degrees C. The phosphorus content of EWP increased from 0.08 to 0.64% by dry-heating at pH 3.0 and 85 degrees C for 5 days in the presence of phosphate. The electrophoretic mobility of EWP increased with an increase in the phosphorylation level. The heat-induced polymerization of EWP by dry-heating was not affected by the presence of phosphate. Although the solubility of EWP decreased by dry-heating at pH 3.0-5.5, the phosphorylation depressed the insolubilization at low pH. The phosphate bonds in phosphorylated EWP (P-EWP) were stable at pH 2.0-10.0 and were more acid-labile and base-stable than phosphoesters of egg riboflavin-binding protein (RfBP). (31)P NMR spectral data suggested that besides phosphoesters, phosphodiester and polyphosphate bonds were introduced in P-EWP. Heat stability of EWP was improved, and calcium phosphate-solubilizing ability of EWP was enhanced by phosphorylation.     

Glycation and phosphorylation of beta-lactoglobulin by dry-heating: effect on protein structure and some properties

Beta-lactoglobulin (beta-Lg) was glycated with maltopentaose and subsequently phosphorylated by dry-heating in the presence of pyrophosphate to investigate the structural and functional properties of phosphorylated beta-Lg. The circular dichroism spectra showed that the change of the secondary structure in the beta-Lg molecule by glycation and subsequent phosphorylation was small. The differential scanning calorimetry thermograms of beta-Lg showed that the denaturation temperature of the most stable domain was only slightly affected, whereas the retinol-binding activity of beta-Lg was somewhat reduced by glycation and subsequent phosphorylation. These results indicated that the conformational changes of the beta-Lg molecule by glycation and subsequent phosphorylation were mild. The anti-beta-Lg antibody response was somewhat reduced by glycation, but significant changes were not observed by phosphorylation. Although the stability of beta-Lg against heat-induced insolubility was improved by glycation alone, it was further enhanced by phosphorylation. The calcium phosphate solubilizing ability of beta-Lg was enhanced by phosphorylation following glycation.     

Inhibition against heat coagulation of ovotransferrin by ovalbumin dry-heated at 120 degrees C

Ovalbumin (OVA) was aggregated stepwise by dry heating at 120 degrees C with a gradual increase in its heating times (10 min-6 h). The inhibiting effects of DHOVAs (OVAs dry-heated for various times up to 6 h) on the heat coagulation of ovotransferrin (OT) were studied. DHOVAs and OT were solubilized at 5% (w/w) concentration with 10 mM sodium phosphate buffer, pH 7.4. Their solutions were mixed at the volume ratio of 1:1 and reheated at 60 degrees C for 3. 5 min. Some remarkable differences according to dry-heating time were observed: coagulum formations were greatly inhibited in the solutions mixed with DHOVAs treated for more than around 2.0 h, with decreasing turbidity as dry-heating time increased. In addition, the effects of reheating time and temperature, as well as those of pH and ionic strength, were also examined on coagulum formation and turbidity development in connection with dry-heating time. Thus, the inhibiting effects of dry-heated egg white on the heat coagulation of fresh egg white previously described were confirmed on the molecular level of OVA and OT.     

Effect of moisture content during dry-heating on selected physicochemical and functional properties of dried egg white

This article addresses the effect of moisture content (0.8-9.9%) during dry-heating (80 degrees C) on selected physicochemical (solubility, turbidity, residual denaturation enthalpy, aggregation, surface hydrophobicity, and sulfhydryl content) and functional (foaming ability, foam density, and stability) properties of freeze-dried egg white (FDEW). Moisture content during dry-heating proved to be a parameter determining the functionality of the resulting egg white powder. The degree of conformational changes induced in the egg white proteins by dry-heating was strongly dependent on the amount of water present. Preferentially, dry-heating at 80 degrees C should be performed on egg white powder with a moisture content below 6.8%, as the loss of protein solubility above this value is extensive. In addition to insoluble aggregates, soluble, strongly stabilized aggregates were also formed, especially at higher moisture contents. The decrease in denaturation enthalpy, increase in surface hydrophobicity, and exposure of SH groups previously hidden in the protein core and their subsequent oxidation were more pronounced at prolonged dry-heating times and at higher moisture contents. These conformational changes resulted in improved foaming ability and foams with lower density. No effect of dry-heating on the foam stability was observed.     

Improvement of gel properties of dried egg white by modification with galactomannan through the Maillard reaction

The effects of Maillard reaction on gel properties of dried egg white (DEW) with galactomannan (GM) were investigated. Maillard-reacted DEW (MDEW) was prepared by dry-heating a mixture with a weight ratio of 1:4 of GM to DEW at 60 degrees C and 65% relative humidity. The modification of amino groups and polymerization of DEW proteins dry-heated with GM proceeded with increasing the dry-heating time. The covalent attachment of GM to DEW was confirmed from SDS-PAGE analysis. Gel strength and water-holding capacity of MDEW gels were higher than those of DEW dry-heated without GM (control DEW) and reached maximum after 3 days of dry-heating. The appearance of MDEW gels became transparent with increasing the dry-heating time, but control DEW gels were still turbid. MDEW dry-heated for 3 days was almost soluble even after heating of its solution at 90 degrees C, whereas control DEW proteins precipitated. The modification of DEW with GM through the Maillard reaction was an effective method to make a firm and transparent gel from DEW at broader range of pH and NaCl concentration of the medium.     

Physical Properties and Enzymatic Digestibility of Phosphorylated ae,wx, and Normal Maize Starch Prepared at Different pH Levels

Phosphorylated starches were prepared with sodium tripolyphosphate (STPP) at pH 6, 8, and 10 from waxy (wx, 3.3% amylose), normal (22.4% amylose), and two high-amylose (ae, 47 and 66% amylose) maize starches. After phosphorylation, the gelatinization peak temperature (T_p) decreased and pasting peak viscosity (PV) increased for all the starches except wx, which showed a slight increase in gelatinization temperature. There was a substantial effect of phosphorylation pH on paste viscosity. More crosslinking was found in ae starches with phosphorylation at pH 10. Sodium ions apparently decreased PV of all the phosphorylated starches while only slightly affecting PV of native starches. Phosphorylation increased swelling power of some of the starches, with maximum swelling power at phosphorylation pH 8 and minimum at pH 10. Maximum swelling power for wx starch after preparation was at pH 8 and minimum at pH 6. After phosphorylation, the clarity and freeze-thaw stability of all the starches was greatly increased compared with the native starches. Phosphorylation increased digestibility of ae starches but had little effect on wx and normal starches. After phosphorylation, the adhesiveness, springiness, and cohesiveness of all starch gels generally increased, the hardness of 47% ae and wx starches increased, and that of normal starches decreased. Enthalpy of gelatinization decreased after phosphorylation with the greatest decrease observed for ae starches. When the phosphorylation pH increased from 6 to 10, the brightness (L*) of all the phosphorylated starches decreased, while a* and b* of all the phosphorylated starch increased. Scanning electron micrographs showed some erosion on the surface of starch granules after phosphorylation.     

Phosphorylation Does Not Improve the Solubility of Rice Protein

The present study tried to phosphorylate rice protein (RP), a known insoluble food ingredient, and determine the improvement of its solubility. RP was allowed to react with sodium trimetaphosphate (STMP) at pH 11.5 and 35°C, and the results indicated that 20.6% of the RP seryl residues were phosphorylated. Interestingly, the solubility of phosphorylated RP (2.6%) was not improved compared with that of RP (2.5%) at pH 7. The involvement of hydrophobic interactions and disulfide bonds in phosphorylated RP solubility was further evaluated. The phosphorylation of RP in the presence of urea as a chaotropic agent for weakening the hydrophobic effect resulted in 22.0% phosphoseryl residues but still did not increase RP solubility. The reduction of RP disulfide bonds prior to phosphorylation resulted in 31.3% phosphoseryl residues and increased RP solubility to 8.3% at pH 7, indicating that disulfide bonds within RP could be responsible for the failure to increase its solubility after phosphorylation.     

Effect of extrusion temperature on the solubility and molecular weight of lentil bean flour proteins containing low cysteine residues

Lentil flour was extruded at die temperatures of 135, 160, and 175 degrees C. The soluble protein content in the extrudates decreased by 40.1% in the extracting buffer (1% sodium dodecyl sulfate in 50 mM sodium phosphate buffer, pH 6.9) as the extrusion die temperature was increased to 175 degrees C. The most insoluble proteins in the extrudates extruded at die temperatures of up to 175 degrees C could be resolubilized by using sonication. The total disulfide content and sulfhydryl content in the extrudates decreased. The SDS-PAGEs showed that the molecular weight distribution of proteins in the lentil flour changed little before and after extrusion as well as during reduction. The results from this study show that the extrusion temperature had less effect on the solubility and molecular weight of the lentil proteins, which contain a lower level of cysteine residues than wheat proteins.     

小麦秸秆生物炭对石油烃污染土壤的修复作用

以小麦秸秆为原材料,在300℃下缺氧裂解3、6、8 h制备生物炭,比较了3种生物炭的产率、pH值、灰分以及C、H、N元素含量,表征了300℃、6 h生物炭的表面形态,并用其作为修复材料,对大港油田的石油污染土壤进行修复。结果表明,随裂解时间的延长,生物炭产率下降,pH值升高,灰分含量增加,H/C值下降,但产率、pH值、灰分和H/C值都是从3 h到6 h差异显著,6 h到8 h差异不显著。C元素含量先升高后下降。石油污染土壤经生物炭修复14 d和28d后,总石油烃降解率分别为45.48%和46.88%,均显著高于对照组。修复14 d后土壤中的萘、苊、苯并[a]蒽、屈、苯并[b]荧蒽、苯并[k]荧蒽、苯并[a]芘、茚并[1,2,3-cd]芘也都有不同程度的下降,其中苯并[a]芘含量下降幅度达98.18%,其他几种PAH的降解率也都高于对照组,28 d后这些PAH的含量又有上升趋势。这说明小麦秸秆裂解时间对生物炭的性质有影响;300℃、6h生物炭可以用来修复石油污染的土壤。     

Thermally induced aggregates in mixtures of alpha-lactalbumin with ovalbumins from different avian species

Interactions between alpha-lactalbumin (alpha-La) and ovalbumin (OVA) in mixed systems (1:1 ratios; 2, 4, and 8% w/w total protein, respectively) heated at pH 7 and 80 degrees C for 15 min were studied using sodium dodecyl sulfate--polyacrylamide gel electrophoresis (SDS-PAGE), gel filtration chromatography (GFC), and competitive enzyme-linked immunosorbent assay (ELISA). Although alpha-La alone did not form aggregates upon heating, it formed large aggregates when heated with OVA. The aggregated molecules eluted at the void volume had a molecular mass >300 kDa. The aggregation process was quantitatively affected by different avian OVAs from five species, possessing different numbers of free sulfhydryl groups. The amount of aggregates (M(w) > 300 kDa) increased in proportion to total protein concentration, and the amount of intermediate components (M(w) < 300 kDa) and monomeric OVA and alpha-La also changed, correlating with total protein concentration during heating. The results also indicated that the aggregates and intermediates, which contained dimeric and trimeric alpha-La, were mainly formed by the intermolecular disulfide bonds. The different interactions observed in several avian OVAs may explain heat-induced gelation of various avian OVAs as well as the enhancement of heat-induced gelation of OVA by alpha-La.     

Purification and characterization of a lipoxygenase enzyme from durum wheat semolina.

Purification of a lipoxygenase enzyme from the cultivar Tresor of durum wheat semolina (Triticum turgidum var. durum Desf) was reinvestigated furnishing a new procedure. The 895-fold purified homogeneous enzyme showed a monomeric structure with a molecular mass of 95 +/- 5 kDa. Among the substrates tested, linoleic acid showed the highest k(cat)/K(m) value; a beta-carotene bleaching activity was also detected. The enzyme optimal activity was at pH 6. 8 on linoleic acid as substrate and at pH 5.2 for the bleaching activity on beta-carotene, both assayed at 25 degrees C. The dependence of lipoxygenase activity on temperature showed a maximum at 40 degrees C for linoleic acid and at 60 degrees C for bleaching activity on beta-carotene. The amino acid composition showed the presence of only one tryptophan residue per monomer. Far-UV circular dichroism studies carried out at 25 degrees C in acidic, neutral, and basic regions revealed that the protein possesses a secondary structure content with a high percentage of alpha- and beta-structures. Near-UV circular dichroism, at 25 degrees C and at the same pH values, pointed out a strong perturbation of the tertiary structure in the acidic and basic regions compared to the neutral pH condition. Moreover, far-UV CD spectra studying the effects of the temperature on alpha-helix content revealed that the melting point of the alpha-helix is at 60 degrees C at pH 5.0, whereas it was at 50 degrees C at pH 6.8 and 9.0. The NH(2)-terminal sequence allowed a homology comparison with other lipoxygenase sequences from mammalian and vegetable sources.     

Impact of preferential interactions on thermal stability and gelation of bovine serum albumin in aqueous sucrose solutions

The influence of sucrose (0--40 wt %) on the thermal denaturation and gelation of bovine serum albumin (BSA) in aqueous solution has been studied. The effect of sucrose on heat denaturation of 1 wt % BSA solutions (pH 6.9) was measured using ultrasensitive differential scanning calorimetry. The unfolding process was irreversible and could be characterized by a denaturation temperature (T(m)), activation energy (E(A)), and pre-exponential factor (A). As the sucrose concentration increased from 0 to 40 wt %, T(m) increased from 72.9 to 79.2 degrees C, E(A) decreased from 314 to 289 kJ mol(-1), and ln(A/s(-1)) decreased from 104 to 94. The rise in T(m) was attributed to the increased thermal stability of the globular state of BSA relative to its native state because of differences in their preferential interactions with sucrose. The change in preferential interaction coefficient (Delta Gamma(3,2)) associated with the native-to-denatured transition was estimated. The dynamic shear rheology of 2 wt % BSA solutions (pH 6.9, 100 mM NaCl) was monitored as they were heated from 30 to 90 degrees C, held at 90 degrees C for either 15 or 120 min, and then cooled to 30 degrees C. Sucrose increased the gelation temperature due to thermal stabilization of the native state of the protein. The complex shear modulus (G) of cooled gels decreased with sucrose concentration when they were held at 90 degrees C for 15 min because the fraction of irreversibly denatured protein decreased. On the other hand, G of cooled gels increased with sucrose concentration when they were held at 90 degrees C for 120 min because a greater fraction of irreversibly denatured protein was formed and the strength of the protein-protein interactions increased.     

氮添加对华北落叶松叶片化学计量与养分重吸收效率的影响

为了解华北落叶松林叶片化学计量特征和养分重吸收效率与N素供应的关系,以24年生华北落叶松人工林为研究对象,设置3个水平(0,8,15 g/(m~2·a))连续6年的野外氮添加控制试验,测定氮添加后华北落叶松成熟叶片、凋落叶片和林分土壤养分含量的变化。结果表明:成熟叶片C含量在年际间差异显著(P0.05),氮添加显著增加成熟叶2016—2018年的C、N含量,降低2018年的P含量,导致2018年N/P在轻度氮添加下比对照增加20.20%,重度氮添加下增加34.43%,2018年N/P在重度氮添加下出现峰值20.50,表明氮添加在一定程度上驱动该林分生长的P养分限制;凋落叶中的C、N、P含量及化学计量在年际间和氮添加处理下均呈显著差异(P0.05),氮添加显著增加凋落叶2016—2018年的C含量、C/P和N/P,显著降低2016—2018年的P含量;2016—2018年,轻度氮添加下NRE(氮重吸收效率)和NRE/PRE(氮重吸收效率/磷重吸收效率)显著降低,氮添加下PRE(磷重吸收效率)显著增加;相关分析表明,NRE与凋落叶N含量,PRE与凋落叶P含量呈显著负相关,相关系数分别为-0.860和-0.772;氮添加显著增加土壤有效氮的含量,降低土壤pH(除2016年)和速效磷含量。氮添加导致华北山地针叶林树木生长受不同程度的P养分限制,推测氮添加驱动的林分受P限制可能与该区土壤养分初始状况有关,为全球气候变化下森林的养分管理提供参考依据。     

Hydrolysis kinetics of fenthion and its metabolites in buffered aqueous media

This study investigates the hydrolysis kinetics of fenthion and its five oxidation metabolites in pH 7 and pH 9 buffered aqueous media at 25, 50, and 65 degrees C. Five metabolites and three hydrolysis products were synthesized and purified. The reactant and the corresponding hydrolysis products were determined by HPLC. Rate constant and half-life studies revealed that fenthion and its metabolites were relatively stable in neutral media, and their stability decreased as pH increased. The half-lives at 25 degrees C ranged from 59.0 days for fenthion to 16.5 days for fenoxon sulfone at pH 7, and from 55.5 days for fenthion to 9.50 days for fenoxon sulfone at pH 9; half-lives were greatly reduced at elevated temperatures. The activation energy (E(a)) was found to range from 16.7 to 22.1 kcal/mol for the compounds investigated. The phenol hydrolysis product of fenthion and fenoxon, 3-methyl-4-methylthiophenol was not stable in pH 7 and pH 9 buffered solutions at 50 degrees C, whereas 3-methyl-4-methylsulfonylphenol and 3-methyl-4-methylsulfinylphenol were relatively stable under the same conditions. At pH 9, the primary hydrolysis mechanisms of fenthion and its oxidation metabolites were combination of hydroxide ion and neutral water molecule attacking on the P atom to form corresponding phenol derivatives. Under neutral conditions, the primary hydrolysis mechanisms of fenthion and its oxidation metabolites were assumed to be the combination of water molecule attacking on the P atom to form phenol derivatives and on the C atom to yield dealkylation products.     

Inhibiting effects of egg white dry-heated at 120 degrees C on heat aggregation and coagulation of egg white and characteristics of dry-heated egg white.

Dialyzed and freeze-dried egg white (FDEW) was dry-heated at 120 degrees C for up to 6 h. The inhibiting effects of the dry-heated egg white (DHEW) on the heat aggregation and coagulation of egg white (as 10% FDEW solution) and characteristics of the DHEW were examined. From the changes in turbidities and soluble protein contents of supernatant in various mixtures of 10% FDEW and DHEW solutions induced by heating (60 degrees C, 5 min), it was found that the inhibiting capacity increased with increases in the dry-heating time (DHT). The FDEW proteins were denatured with a mild conformational change (not secondary but tertiary structure) with the increase in DHT and aggregated partially. However, the more transparent solutions of DHEW containing soluble aggregates according to DHT were also obtained after heating. The transparency according to DHT came to be scarcely affected by the NaCl concentration and the dilution with diluents containing SDS, urea, and 2-mercaptoethanol. These findings suggest that the heat aggregations and coagulations of ovotransferrin and lysozyme in the FDEW were inhibited by their bindings with the soluble aggregates in DHEW.     

Effect of pH, temperature, and moisture on the formation of volatile compounds in glycine/glucose model systems

Mixtures of glycine, glucose, and starch were extrusion cooked using sodium hydroxide at 0, 3, and 6 g/L of extruder water feed, 18% moisture, and 120, 150, and 180 degrees C target die temperatures, giving extrudates with pH values of 5.6, 6.8, and 7.4. Freeze-dried equimolar solutions of glucose and glycine were heated either dry or after equilibration to approximately 13% moisture at 180 degrees C in a reaction-tube system designed to mimic the heating profile in an extruder. Volatile compounds were isolated onto Tenax and analyzed by gas chromatography-mass spectrometry. For the extrudates, total yields of volatiles increased with decreasing pH at 180 degrees C, reached a maximum at pH 6.8 at 150 degrees C, and increased with increasing pH at 120 degrees C. Amounts increased with temperature at all pH values. Pyrazines were the most abundant class for all sets of conditions (54-79% of total volatiles). Pyrroles, ketones, furans, oxazoles, and pyridines were also identified. Yields of volatiles from the reaction-tube samples increased by >60% in the moist system. Levels of individual classes also increased in the presence of moisture, except pyrazines, which decreased approximately 3.5-fold. Twenty-one of the compounds were common to the reaction-tube samples and the extrudates.     

Partial purification of polyphenol oxidase from Chinese cabbage Brassica rapa L

Polyphenol oxidase (PPO) was purified and characterized from Chinese cabbage by ammonium sulfate precipitation and DEAE-Toyopearl 650M column chromatography. Substrate staining of the crude protein extract showed the presence of three isozymic forms of this enzyme. The molecular weight of the purified enzyme was estimated to be approximately 65 kDa by gel filtration on Toyopearl HW-55F. On SDS-PAGE analysis, this enzyme was composed of a subunit molecular weight of 65 kDa. The optimum pH was 5.0, and this enzyme was stable at pH 6.0 but was unstable below pH 4.0 or above pH 7.0. The optimum temperature was 40 degrees C. Heat inactivation studies showed temperatures >40 degrees C resulted in loss of enzyme activity. PPO showed activity to catechol, pyrogallol, and dopamine (K(m) and V(max) values were 682.5 mM and 67.6 OD/min for catechol, 15.4 mM and 14.1 OD/min for pyrogallol, and 62.0 mM and 14.9 OD/min for dopamine, respectively). The most effective inhibitor was 2-mercaptoethanol, followed in decreasing order by ascorbic acid, glutathione, and L-cysteine. The enzyme activity of the preparation was maintained for 2 days at 4 degrees C but showed a sudden decreased after 3 days.     

Effect of temperature and/or pressure on tomato pectinesterase activity

The activity of tomato pectinesterase (PE) was studied as a function of pressure (0.1-900 MPa) and temperature (20-75 degrees C). Tomato PE was rather heat labile at atmospheric pressure (inactivation in the temperature domain 57-65 degrees C), but it was very pressure resistant. Even at 900 MPa and 60 degrees C the inactivation was slower as compared to the same treatment at atmospheric pressure. At atmospheric pressure, optimal catalytic activity of PE was found at neutral pH and a temperature of 55 degrees C. Increasing pressure up to 300 MPa increased the enzyme activity as compared to atmospheric pressure. A maximal enzyme activity was found at 100-200 MPa combined with a temperature of 60-65 degrees C. The presence of Ca(2+) ions (60 mM) decreased the enzyme activity at atmospheric pressure in the temperature range 45-60 degrees C but increased enzyme activity at elevated pressure (up to 300 MPa). Maximal enzyme activity in the presence of Ca(2+) ions was noted at 200-300 MPa in combination with a temperature of 65-70 degrees C.     

Aging of whey protein films and the effect on mechanical and barrier properties

This work focuses on the aging of whey protein isolate (WPI) films plasticized with glycerol (G) and sorbitol (S). The films were cast from heated aqueous solutions at pH 7 and dried at 23 degrees C and 50% relative humidity (RH) for 16 h. They were stored in a climate room (23 degrees C, 50% RH) for 120 days, and the film properties were measured at regular intervals. The moisture content (MC) of the WPI/G films decreased from 22% (2 days) to 15% (45 days) and was thereafter constant at 15% (up to 120 days). This affected the mechanical properties and caused an increased stress at break (from 2.7 to 8.3 MPa), a decreased strain at break (from 33 to 4%), and an increased glass transition temperature (T(g)) (from -56 to -45 degrees C). The barrier properties were, however, unaffected, with constant water vapor permeability and a uniform film thickness. The MC of the WPI/S films was constant at approximately 9%, which gave no change in film properties.