Effect of hydrocolloids on the thermal denaturation of proteins

The thermal denaturation of bovine serum albumin (BSA), lysozyme and whey protein isolate (WPI) in the presence of hydrocolloids (pectin, guar gum, ι-carrageenan) was investigated. A decrease in the thermal stability of lysozyme was observed in the mixture of protein with ι-carrageenan. The increase in the enthalpy of denaturation (ΔH) of BSA and lysozyme in the presence of hydrocolloids was attributed to the protection of globular proteins against aggregation through blockage of their hydrophobic binding sites by the bulky polysaccharide moeity. Biopolymers had a stabilizing effect on WPI. The thermal stability was the highest in the presence of pectin, whereas the lowest transition temperature was observed in the presence of guar gum. A single transition peak was observed for pure WPI. However, WPI exhibited two transition temperatures when together with pectin and i-carrageenan. WPI was stable against heat denaturation at acidic pH values (pH 4.0), while it was denatured at a low temperature at an alkaline pH (pH 9.0) in the presence of pectin. This was attributed to the formation of extra hydrogen bonding. The increase in the concentration of pectin has little affect on the heat stability of WPI; however, it reduces the cooperativity of transition.     

Effect of pulsed light treatment on structural and functional properties of whey protein isolate

This work aimed at investigating the effects of Pulsed Light (PL) processing at different fluences (from 4 to 16 J/cm²) on the structure and functional properties of Whey Protein Isolate (WPI) solution. The determination of the free and total sulfhydryl (SH) groups was used to detect the variation of WPI tertiary and quaternary structure. Additionally, PL-induced changes in secondary structure were determined by FT-IR spectroscopy and the differential scanning calorimetry (DSC), and primary structure by carbonyl content.The experimental data demonstrated that PL treatments increased the concentration of total and free sulfhydryl groups and protein carbonyls. A decrease of the denaturation temperature and enthalpy ratio with increasing the intensity of PL treatments was observed in DSC measurements. Small but significant changes in the secondary structure of PL treated WPI solution were also taking place and detected. The extent of whey protein structure modifications was fluence dependent. The results of this investigation demonstrated the potential of PL treatments to induce dissociation and partial unfolding of WPI, thus improving some of their functional properties, such as solubility and foaming ability.     

Effect of microbial transglutaminase treatment on thermal stability and pH-solubility of heat-shocked whey protein isolate

Whey protein isolate (WPI) dispersions (5% protein, pH 7.0) were subjected to heat-shock at 70 °C for 1, 5 and 10 min. The heat-shocked WPI dispersions were treated with microbial transglutaminase (MTGase) enzyme, and thermal properties and pH-solubility of the treated proteins were investigated. Heat-shocking of WPI for 10 min at 70 °C increased the thermal denaturation temperature (T_d) of β-lactoglobulin in WPI by about 1.5 °C. MTGase treatment (30 h, 37 °C) of the heat-shocked WPI significantly increased the T_d of β-lactoglobulin by about 6.3–7.3 °C when compared with heat-shocked only WPI at pH 7.0. The T_d increased by about 13–15 °C following pH adjustment to 2.5; however, the T_d of heat-shocked WPI was not substantially different from heat-shocked and MTGase-treated WPI at pH 2.5. Both the heat-shocked and the heat-shocked-MTGase-treated WPI exhibited U-shaped pH-solubility profiles with minimum solubility at pH 4.0–5.0. However, the extent of precipitation of MTGase-treated WPI samples at pH 4.0–5.0 was much greater than all heat-shocked and native WPI samples. The study revealed that while MTGase cross-linking significantly enhanced the thermal stability of β-lactoglobulin in heat-shocked WPI, it caused pronounced precipitation at pH 4.0–5.0 via decreasing the hydrophilic/hydrophobic ratio of the water-accessible protein surface.     

Ionic strength and buffering capacity of emulsifying salts determine denaturation and gelation temperatures of whey proteins

Ionic conditions affect the denaturation and gelling of whey proteins, affecting the physical properties of foods in which proteins are used as ingredients. We comprehensively investigated the effect of the presence of commonly used emulsifying salts on the denaturation and gelling properties of concentrated solutions of β-lactoglobulin (β-LG) and whey protein isolate (WPI). The denaturation temperature in water was 73.5°C [coefficient of variation (CV) 0.49%], 71.8°C (CV 0.38%), and 69.9°C (CV 0.41%) for β-LG (14% wt/wt), β-LG (30% wt/wt), and WPI (30% wt/wt), respectively. Increasing the concentration of salts, except for sodium hexametaphosphate, resulted in a linear increase in the denaturation temperature of WPI (kosmotropic behavior) and an acceleration in its gelling rate. Sodium chloride and tartrate salts exhibited the strongest effect in protecting WPI against thermal denaturation. Despite the constant initial pH of all solutions, salts having buffering capacity (e.g., phosphate and citrate salts) prevented a decrease in pH as the temperature increased above 70°C, resulting in a decline in denaturation temperature at low salt concentrations (≤0.2 mol/g). When pH was kept constant at denaturation temperature, all salts except sodium hexametaphosphate, which exhibited chaotropic behavior, exhibited similar effects on denaturation temperature. At low salt concentration, gelation was the controlling step, occurring up to 10°C above denaturation temperature. At high salt concentration (>3% wt/wt), thermal denaturation was the controlling step, with gelation occurring immediately after. These results indicate that the ionic and buffering properties of salts added to milk will determine the native versus denatured state and gelation of whey proteins in systems subjected to high temperature, short time processing (72°C for 15 s).     

Pilot-scale formation of whey protein aggregates determine the stability of heat-treated whey protein solutions—Effect of pH and protein concentration

Denaturation and consequent aggregation in whey protein solutions is critical to product functionality during processing. Solutions of whey protein isolate (WPI) prepared at 1, 4, 8, and 12% (wt/wt) and pH 6.2, 6.7, or 7.2 were subjected to heat treatment (85°C × 30 s) using a pilot-scale heat exchanger. The effects of heat treatment on whey protein denaturation and aggregation were determined by chromatography, particle size, turbidity, and rheological analyses. The influence of pH and WPI concentration during heat treatment on the thermal stability of the resulting dispersions was also investigated. Whey protein isolate solutions heated at pH 6.2 were more extensively denatured, had a greater proportion of insoluble aggregates, higher particle size and turbidity, and were significantly less heat-stable than equivalent samples prepared at pH 6.7 and 7.2. The effects of WPI concentration on denaturation/aggregation behavior were more apparent at higher pH where the stabilizing effects of charge repulsion became increasingly influential. Solutions containing 12% (wt/wt) WPI had significantly higher apparent viscosities, at each pH, compared with lower protein concentrations, with solutions prepared at pH 6.2 forming a gel. Smaller average particle size and a higher proportion of soluble aggregates in WPI solutions, pre-heated at pH 6.7 and 7.2, resulted in improved thermal stability on subsequent heating. Higher pH during secondary heating also increased thermal stability. This study offers insight into the interactive effects of pH and whey protein concentration during pilot-scale processing and demonstrates how protein functionality can be controlled through manipulation of these factors.     

Functionality of spray-dried strawberry powder: effects of whey protein isolate and maltodextrin

The effectiveness of two drying agents, namely whey protein isolate (WPI) and maltodextrin (MD), was evaluated during spray-drying of strawberry puree. With the increase of WPI substitution in the feed material, the surface tension of strawberry puree decreased, and powder recovery increased. Powder recovery (R_p) increased from 39.2 ± 2.3% (S:MD:WPI = 60:40:0) to 56.5 ± 2.8% when MD was replaced by WPI (S:MD:WPI = 60:39:1). Surface morphology of powders showed that the addition of WPI resulted in shrunken particle surface, which gave rise to smaller D_B and particle size. The particles were not spherical, and even with the addition of 0.5% WPI, the particle morphology was altered. The surface shrinkage of strawberry powder increased with increase in WPI from 0.5% to 10%. The production efficiency of strawberry powder could be greatly improved when MD was replaced by 1% WPI.     

Heat-Induced Aggregation Properties of Whey Proteins as Affected by Storage Conditions of Whey Protein Isolate Powders

The control of storage as any other manufacturing steps of dairy powders is essential to preserve protein functional properties. This study aimed to determine the effects of different storage conditions on both protein denaturation and protein lactosylation in whey protein isolate (WPI) powder, and also on heat-induced aggregation. Two different storage temperature conditions (20 and 40 °C) were studied over 15 months. Our results showed that protein lactosylation progressively increased in WPI powders over 15 months at 20 °C, but heat-induced aggregation properties did not significantly differ from non-aged WPI. On the other hand, powders presented a high level of denaturation and aggregation at 40 °C from the first 2 weeks of storage, involving first protein lactosylation and then aggregation in the dry state. This was correlated with an increasing Browning Index from 15 days of storage. These changes occurred with a decrease in aggregate size after heat treatment at 5.8?≤?pH?≤?6.6 and modification of heat-induced aggregate shapes.     

Comparative study of denaturation of whey protein isolate (WPI) in convective air drying and isothermal heat treatment processes

The extent and nature of denaturation of whey protein isolate (WPI) in convective air drying environments was measured and analysed using single droplet drying. A custom-built, single droplet drying instrument was used for this purpose. Single droplets having 5 ± 0.1 μl volume (initial droplet diameter 1.5 ± 0.1 mm) containing 10% (w/v) WPI were dried at air temperatures of 45, 65 and 80 °C for 600 s at constant air velocity of 0.5 m/s. The extent and nature of denaturation of WPI in isothermal heat treatment processes was measured at 65 and 80 °C for 600 s and compared with those obtained from convective air drying. The extent of denaturation of WPI in a high hydrostatic pressure environment (600 MPa for 600 s) was also determined. The results showed that at the end of 600 s of convective drying at 65 °C the denaturation of WPI was 68.3%, while it was only 10.8% during isothermal heat treatment at the same medium temperature. When the medium temperature was maintained at 80 °C, the denaturation loss of WPI was 90.0% and 68.7% during isothermal heat treatment and convective drying, respectively. The bovine serum albumin (BSA) fraction of WPI was found to be more stable in the convective drying conditions than β-lactoglobulin and α-lactalbumin, especially at longer drying times. The extent of denaturation of WPI in convective air drying (65 and 80 °C) and isotheral heat treatment (80 °C) for 600 s was found to be higher than its denaturation in a high hydrostatic pressure environment at ambient temperature (600 MPa for 600 s).     

草莓切片微波真空干燥特性及干燥品质研究

提高水果干燥效率、干制品质量和降低干燥能耗,对草莓切片进行微波真空干燥,研究草莓切片微波真空干燥特性及其干后品质。通过二次回归正交试验,建立各指标与干燥功率、样品厚度及干燥室压力等因素间的回归数学模型,分析草莓切片微波干燥特性,讨论干燥功率、样品厚度及干燥室压力等因素对干制品的复水率、VC 保存率和干燥能耗的影响。结果表明：随着样品厚度与压力的降低和干燥功率的增加,干燥速率增加;随着样品厚度的增加和干燥功率与压力的降低,复水率和VC 保存率增加;随着样品厚度与干燥功率的增加和压力的降低,干燥能耗减少。最后,利用多目标非线性优化方法,确定了草莓切片微波真空干燥最优工艺参数,即微波功率6.18W/g、切片厚度5.05mm、干燥室压力55.19Pa。     

Influence of pH on the dry heat-induced denaturation/aggregation of whey proteins

The effect of pH on the heat-induced denaturation/aggregation of whey protein isolate (WPI) in the dry state was investigated. WPI powders at different pH values (6.5, 4.5, and 2.5) and controlled water activity (0.23) were dry heated at 100 °C for up to 24 h. Dry heating was accompanied by a loss of soluble proteins (native-like β-lactoglobulin and α-lactalbumin) and the concomitant formation of aggregated structures that increased in size as the pH increased. The loss of soluble proteins was less when the pH of the WPI was 2.5; in this case only soluble aggregates were observed. At higher pH values (4.5 and 6.5), both soluble and insoluble aggregates were formed. The fraction of insoluble aggregates increased with increasing pH. Intermolecular disulphide bonds between aggregated proteins predominated at a lower pH (2.5), while covalent cross-links other than disulphide bonds were also formed at pH 4.5 and 6.5. Hence, pH constitutes an attractive tool for controlling the dry heat-induced denaturation/aggregation of whey proteins and the types of interactions between them. This may be of great importance for whey ingredients having various pH values after processing.     

Rheological,thermal and microstructural properties of whey protein isolate‐modified cassava starch mixed gels at different pH values

The objective of this study was to investigate the rheological, thermal and microstructural properties of whey protein isolate (WPI)‐hydroxypropylated cassava starch (HPCS) gels and WPI‐cross‐linked cassava starch (CLCS) gels at different pH values (5.75, 7.00 and 9.00). The rheological results showed that the WPI‐modified starch gels had greater storage modulus (G?) values than the WPI‐native cassava starch gels at pH 5.75 and 7.00. Differential scanning calorimetry curves suggested that the phase transition order of the WPI and modified starch changed as the pH increased. Scanning electron microscopy images showed that the addition of HPCS and CLCS contributed to the formation of a compact microstructure at pH 5.75 and 7.00. A comprehensive analysis showed that the gelling properties of the WPI‐modified starch were affected by the difference between the WPI denaturation temperature and modified starch gelatinisation temperature and by the granular properties of the modified starch during gelatinisation. These results may contribute to the application of WPI‐modified starch mixtures in food preparation.     

Controlling denaturation and aggregation of whey proteins during thermal processing by modifying temperature and calcium concentration

Whey protein isolate solutions (8.00 g protein/100 g; pH 6.8) were treated for 2 min at 72, 85 or 85 °C with 2.2 mM added calcium Ca to produce four whey protein systems: unheated control (WPI‐UH), heated at 72 °C (WPI‐H72), heated at 85 °C (WPI‐H85) or heated at 85 °C with added Ca (WPI‐H85Ca). Total levels of whey protein denaturation increased with increasing temperature, while the extent of aggregation increased with the addition of Ca, contributing to differences in viscosity. Significant changes in Ca ion concentration, turbidity and colour on heating of WPI‐H85Ca, compared to WPI‐UH, demonstrated the role of Ca in whey protein aggregation.     

Edible Coatings on Frozen King Salmon: Effect of Whey Protein Isolate and Acetylated Monoglycerides on Moisture Loss and Lipid Oxidation

Whey protein isolate (WPI) and acetylated monoglyceride (AMG) coatings were evaluated for effectiveness against moisture loss and lipid oxidation of frozen King salmon. A model gel material was also used to screen coatings for effectiveness against moisture loss. Coatings of low-melting-point AMG used alone or after applying WPI solution or WPI powder were effective in reducing the rate of moisture loss by 42–65% during the first 3 wk of storage. Onset of lipid oxidation was delayed and peak peroxide values were reduced in samples coated with WPI solution/antioxidant overspray or those containing low-melting-point AMGs. No differences in effectiveness were found among the coating treatments.     

Effects of thermally induced denaturation on technological-functional properties of whey protein isolate-based films

This study examined how and to what extent the degree of denaturation affected the technological-functional properties of whey protein isolate (WPI)-based coatings. It was observed that denaturation affected the material properties of WPI-coated films significantly. Surface energy decreased by approximately 20% compared with native coatings. Because the surface energy of a coating should be lower than that of the substrate, this might result in enhanced wettability characteristics between WPI-based solution and substrate surface. Water vapor barrier properties increased by about 35% and oxygen barrier properties increased by approximately 33%. However, significant differences were mainly observed between coatings made of fully native WPI and ones with a degree of denaturation of 25%. Higher degrees of denaturation did not lead to further improvement of material properties. This observation offers cost-saving potential: a major share of denatured whey proteins may be replaced by fully native ones that are not exposed to energy-intensive heat treatment. Furthermore, native WPI solutions can be produced with higher dry matter content without gelatinizing. Hence, less moisture has to be removed through drying, resulting in reduced energy consumption.     

OPTIMIZING STABILITY OF ORANGE JUICE FORTIFIED WITH WHEY PROTEIN AT LOW pH VALUES

Abstract The influence of temperature, heating time and pH on the stability of whey protein-fortified Valencia orange juice was determined by uronic acid content, degree of esterification (DE), % transmission measurements (%T) and capillary electrophoretic analysis of the juice-protein supernatants. Uronic acid content and charge of pectins showed no significant change in heat-treated samples with added proteins. The %T decreased with decreasing pH and increasing temperature and heating time for α-lactalbumin (α-lac), β-lactoglobulin (β-lg) and whey protein isolate (WPI). The lowest transmission values were shown at pH 3.0 and 85C. Capillary electropherograms confirmed more extensive juice-protein interactions in WPI and β-lg added juices than in those containing α-lac, especially at low pH, resulting in more stable juice-protein mixtures.     

Coating of Peanuts with Edible Whey Protein Film Containing α‐Tocopherol and Ascorbyl Palmitate

ABSTRACT: Physical properties of whey protein isolate (WPI) coating solution incorporating ascorbic palmitate (AP) and α‐tocopherol (tocopherol) were characterized, and the antioxidant activity of dried WPI coatings against lipid oxidation in roasted peanuts were investigated. The AP and tocopherol were mixed into a 10% (w/w) WPI solution containing 6.7% glycerol. Process 1 (P1) blended an AP and tocopherol mixture directly into the WPI solution using a high‐speed homogenizer. Process 2 (P2) used ethanol as a solvent for dissolving AP and tocopherol into the WPI solution. The viscosity and turbidity of the WPI coating solution showed the Newtonian fluid behavior, and 0.25% of critical concentration of AP in WPI solution rheology. After peanuts were coated with WPI solutions, color changes of peanuts were measured during 16 wk of storage at 25 °C, and the oxidation of peanuts was determined by hexanal analysis using solid‐phase micro‐extraction samplers and GC‐MS. Regardless of the presence of antioxidants in the coating layer, the formation of hexanal from the oxidation of peanut lipids was reduced by WPI coatings, which indicates WPI coatings protected the peanuts from oxygen permeation and oxidation. However, the incorporation of antioxidants in the WPI coating layer did not show a significant difference in hexanal production from that of WPI coating treatment without incorporation of antioxidants.     

干燥方式及碱液处理对鲜枸杞干燥特性和品质的影响

为了缩短鲜枸杞干燥时间,降低能耗,提高枸杞干制品品质,采用清水和不同质量分数（2%、4%和6%） 的Na2CO3溶液对枸杞进行前处理后,分别进行热风和热泵干燥,测定并分析了所获得枸杞干果的干燥速率、色 泽、复水率以及主要营养成分（多糖、总类胡萝卜素、黄酮）含量。结果表明：Na2CO3前处理能使枸杞表皮蜡质 层变薄、断裂,形成水分通道,进而缩短枸杞干燥时间,较为适宜的Na2CO3质量分数为2%。在干燥效率方面,热 泵和热风干燥没有显著性差异,但是在干燥产品品质上,热泵干燥要明显优于热风干燥。相对于恒温恒湿干燥, 分阶段变温干燥在保证干燥产品品质的同时,加快干燥速率,缩短干燥时间。因此枸杞干燥的最适工艺参数为 2% Na2CO3前处理,干燥温度40 ℃（2 h）-45 ℃（4 h）-50 ℃（6 h）-55 ℃（10 h）,干燥相对湿度40%的热泵干 燥。此工艺条件下枸杞干燥时间为22 h,干燥枸杞色差值为15.09,复水率为2.35 g/g,多糖含量为10.29 g/100 g,黄 酮含量为0.43 g/100 g,总类胡萝卜素含量为1 503.13 μg/g。     

Effect of pH and addition of corn oil on the properties of whey protein isolate-based films using response surface methodology

Response surface methodology (RSM) was used to investigate pH and corn oil (CO) effects on the properties of films formed from whey protein isolate (WPI). Test films were evaluated for tensile strength (TS), puncture strength (PT), percentage elongation at break point (E), water vapour permeability (WVP) and oxygen permeability (OP). TS of WPI films increased with increasing pH, while addition of CO produced no trend. However, when WPI solution pH increased >10.0, film TS generally decreased with CO addition (>11%). E values increased dramatically with increasing levels of CO when pH for WPI solutions were >8.5. However, pH had no effect on E values. WPI solutions possessing high pH values (maximum pH value of 10.62) produced WPI films with the highest PT values. WVP had a quadratic relationship with pH and CO addition. OP had an inversely linear relationship with increasing pH (6.5–10.5) and a quadratic relationship with CO addition. Optimal pH (9.88) and CO level (2.93%), determined from physical test film data, were predicted by RSM.     

微波干燥条件对杏脯干燥特性与品质的影响

目的:提高杏脯的干燥效率及产品品质。方法:分别用转盘式微波炉(RMD)和微波对流耦合干燥机(MCD)干燥杏脯,考察微波功率、微波发射方式、切分程度及物料是否转动对杏脯干燥特性、焦化率、色值、感官品质及复水特性的影响,并与传统热风干燥(HD)进行比较。结果:与HD的1 040 min(16块)和840 min(48块)相比,微波干燥显著缩短干燥时间,不同微波干燥条件下所需的干燥时间为40～400 min;脉冲比越大或功率越高或物料尺寸越大,干燥所用时间越短,在MCD中控温微波干燥耗时最长。无论是在RMD还是不控温MCD中静态干燥,杏脯均出现严重的烧焦现象,焦化率为17%～100%,物料转动时焦化率高于静态干燥的,而在MCD中控温静态干燥避免了物料的烧焦现象,且MCD中控温静态干燥的杏脯色值和感官评价最接近HD的,复水比与HD仅相差3.45%～5.17%,获得最高的感官评价分(87.2分)。结论:MCD中控温静态干燥可以作为杏脯的高效干燥方法。     

Functionality of extrusion--texturized whey proteins

Whey, a byproduct of the cheesemaking process, is concentrated by processors to make whey protein concentrates (WPC) and isolates (WPI). Only 50% of whey proteins are used in foods. In order to increase their usage, texturizing WPC, WPI, and whey albumin is proposed to create ingredients with new functionality. Extrusion processing texturizes globular proteins by shearing and stretching them into aligned or entangled fibrous bundles. In this study, WPC, WPI, and whey albumin were extruded in a twin screw extruder at approximately 38% moisture content (15.2 ml/min, feed rate 25 g/min) and, at different extrusion cook temperatures, at the same temperature for the last four zones before the die (35, 50, 75, and 100 degrees C, respectively). Protein solubility, gelation, foaming, and digestibility were determined in extrudates. Degree of extrusion-induced insolubility (denaturation) or texturization, determined by lack of solubility at pH 7 for WPI, increased from 30 to 60, 85, and 95% for the four temperature conditions 35, 50, 75, and 100 degrees C, respectively. Gel strength of extruded isolates increased initially 115% (35 degrees C) and 145% (50 degrees C), but gel strength was lost at 75 and 100 degrees C. Denaturation at these melt temperatures had minimal effect on foaming and digestibility. Varying extrusion cook temperature allowed a new controlled rate of denaturation, indicating that a texturized ingredient with a predetermined functionality based on degree of denaturation can be created.