Stabilization of biopolymer microgels formed by electrostatic complexation: Influence of enzyme (laccase) cross-linking on pH,thermal, and mechanical stability

Biopolymer microgels formed by electrostatic complexation are often susceptible to disintegration when environmental conditions are changed, and so methods are required to improve their stability. In this study, microgels were formed by electrostatic complexation of a protein (type-B gelatin) and a polysaccharide (beet pectin). The impact of enzyme (laccase) crosslinking of the ferulic acid groups on the beet pectin was then studied as a method to improve microgel stability to environmental stresses. Gelatin–beet pectin (1:0.25 w/w) microgels were formed at 35 °C and pH 4.4, and then the pH dependence of the ζ-potential, size, turbidity, and microstructure of the microgels was measured in the absence and presence of laccase cross-linking. Our results suggested that crosslinking occurred within the microgels (rather than between them) since no particle aggregation was observed after enzyme treatment. Enzyme crosslinking did not affect the ζ-potential of the microgels, but it did decrease their size. Both cross-linked and non-cross-linked microgels were stable to aggregation at low (2–3) and high (4.4–7) pH values, but not at intermediate values (3–4.4), which was attributed to their low surface charge. Cross-linking improved the resistance of the microgels to shearing-induced disruption (300 rpm for 24 h) and to thermal-induced disruption (50 °C for 2 min). These cross-linked biopolymer microgels may have applications for texture modification, encapsulation, or controlled release.     

Impact of whey protein – Beet pectin conjugation on the physicochemical stability of β-carotene emulsions

The aim of the present study was to investigate the impact of whey protein isolate (WPI)-beet pectin conjugation on the physical and chemical properties of oil-in-water emulsions incorporating β-carotene within the oil droplets. Covalent coupling of WPI to beet pectin was achieved by dry heating of WPI-beet pectin mixtures of different weight ratios at 80, 90, 100 °C and 79% relative humidity for incubation times ranging from 1 to 9 h. It was confirmed by SDS-polyacrylamide gel electrophoresis that WPI covalently linked to beet pectin. The physical and chemical stability of β-carotene emulsions was characterized by droplet size and distribution, transmission profiles using novel centrifugal sedimentation technique, microstructure and β-carotene degradation during the storage. Compared with those stabilized by WPI alone and unheated WPI-beet pectin mixtures, β-carotene emulsions stabilized by WPI-beet pectin conjugates had much smaller droplet sizes, more homogenous droplet size distribution, less change in centrifugal transmission profiles and obviously improved freeze–thaw stability, indicating a very substantial improvement in the physical stability. Rheological analysis exhibited that emulsions stabilized by WPI-beet pectin conjugates changed from a shear thinning to more like Newtonian liquid compared those with WPI alone and unheated WPI-beet pectin mixtures. Degradation of β-carotene in emulsion during storage was more obviously retarded by WPI-beet pectin conjugate than WPI and unheated WPI-beet pectin mixture, probably due to a thicker and denser interfacial layer in emulsion droplets. These results implied that protein–polysaccharide conjugates were able to improve the physical stability of β-carotene emulsion and inhibit the deterioration of β-carotene in oil-in-water emulsions.     

Enzyme catalyzed oxidative gelation of sugar beet pectin: Kinetics and rheology

Sugar beet pectin (SBP) is a marginally utilized co-processing product from sugar production from sugar beets. In this study, the kinetics of oxidative gelation of SBP, taking place via enzyme catalyzed cross-linking of ferulic acid moieties (FA), was studied using small angle oscillatory measurements. The rates of gelation, catalyzed by horseradish peroxidase (HRP) (EC 1.11.1.7) and laccase (EC 1.10.3.2), respectively, were determined by measuring the slope of the increase of the elastic modulus (G′) with time at various enzyme dosages (0.125–2.0 U mL⁻¹). When evaluated at equal enzyme activity dosage levels, the two enzymes produced different gelation kinetics and the resulting gels had different rheological properties: HRP (with addition of H₂O₂) catalyzed a fast rate of gelation compared to laccase (no H₂O₂ addition), but laccase catalysis produced stronger gels (higher G′). The main effects and interactions between different factors on the gelation rates and gel properties were examined in response surface designs in which enzyme dosage (0.125–2.0 U mL⁻¹ for HRP; 0.125–10 U mL⁻¹ for laccase), substrate concentration (1.0–4.0%), temperature (25–55 °C), pH (3.5–5.5), and H₂O₂ (0.1–1.0 mM) (for HRP only) were varied. Gelation rates increased with temperature, substrate concentration, and enzyme dosage; for laccase catalyzed SBP gelation the gel strengths correlated positively with increased gelation rate, whereas no such correlation could be established for HRP catalyzed gelation and at the elevated gelation rates (>100 Pa min⁻¹) gels produced using laccase were stronger (higher G′) than HRP catalyzed gels at similar rates of gelation. Chemical analysis confirmed the formation of ferulic acid dehydrodimers (diFAs) by both enzymes supporting that the gelation was a result of oxidative cross-linking of FAs.     

β-Lactoglobulin conformation and mixed sugar beet pectin gel matrix is changed by laccase

Sugar beet pectin (SBP) and β-lactoglobulin (BLG) contain ferulic acid and tyrosine, respectively, potential substrates for laccase. Dispersions of BLG were treated with laccase and/or heat and SBP to assess potential for ferulic acid in SBP to influence laccase conjugation of BLG. Changes were investigated by size exclusion chromatography combined with multi angle laser light scattering (HPSEC-MALLS), refractive index (RI) and UV detector, particle size and ζ-potential analysis. Molecular weight (MW) of BLG decreased from 3.7 × 10⁴ to 2.9 × 10⁴ and root mean square (RMS) decreased from 41 to 36 after laccase treatment. The slope of a conformation plot increased from 0.35 to 0.72, indicating a change in shape in laccase treated BLG to more random coil. While laccase did not affect MW of BLG, MW of BLG increased after sequential heat and laccase treatment to 2.9 × 10⁶ and 4.4 × 10⁶, respectively. Free thiol (SH) increased by heat and laccase treatment of BLG; tyrosine in BLG increased only by heat. An increased MW and decreased ferulic acid in SBP was observed in the presence of BLG and laccase. The increase in MW was attributed to entrapment of BLG in SBP cross-linked matrix catalyzed by laccase.     

TG酶和漆酶对双歧杆菌益生菌酸奶品质的影响

为了比较谷氨酰胺转氨酶(TG酶)和漆酶的添加对双歧杆菌益生菌酸奶感官、蛋白质交联及组织质构变化的影响,测定和分析了两种酶交联益生菌酸奶的游离氨基变化率、感官、质构、表观黏度、蛋白条带及微观结构,并添加阿魏酸改善漆酶酸奶的品质。结果表明:当TG酶用量增加时,TG酶交联酸奶的游离氨基变化率、感官得分和硬度显著增大(p<0.05),胶黏性、粘聚性及表观黏度先增大后减小(p<0.05),内聚性变化不显著(p>0.05),TG酶最佳用量为1.8 U/g;随着漆酶用量的增加,漆酶酸奶游离氨基变化率、感官得分、硬度、内聚性、胶黏性、粘聚性及表观黏度均先增大后减小(p<0.05),漆酶最佳用量为0.3 U/g;添加4.5 mmol/L的阿魏酸明显改善了漆酶交联酸奶的感官、质构及表观黏度;所有待测酸奶中均缺少β-lg条带,TG酶交联酸奶的κ-CN和β-CN条带消失,聚集成了新的蛋白质,而漆酶交联酸奶和阿魏酸+漆酶酸奶与对照及TG酶酸奶相比,分子量在14 kDa的蛋白条带明显变宽;经两种酶交联的酸奶,三维网络结构变得致密,TG酶交联酸奶的胶粒分布更均匀,网络结构更致密,且在漆酶交联酸奶中添加了阿魏酸后,相较于漆酶交联酸奶,蛋白胶束聚集的更紧密,从而得出,不同类型酶对牛奶乳蛋白质交联的催化作用不同,但均可改善酸奶的感官及食用品质。     

漆酶诱导大豆分离蛋白-甜菜果胶双网络凝胶的构建

大豆分离蛋白是食品工业中常用的凝胶材料,但其对环境较为敏感,所成凝胶具有机械性能单一,成形性较差等缺点,而多糖对蛋白质的修饰可以改善蛋白质的凝胶性质。本研究通过向大豆分离蛋白中添加适量甜菜果胶,调节大豆分离蛋白和甜菜果胶浓度来构建双网络凝胶,以达到改善蛋白质单一网络凝胶的机械和质构特性的目的。实验中通过酶促和加热两步处理,得到大豆分离蛋白-甜菜果胶双网络凝胶。随着大豆分离蛋白浓度的提高,双网络凝胶的弹性也随之提高。而甜菜果胶浓度越高,双网络凝胶的硬度和咀嚼性越大。当大豆分离蛋白浓度为11%,甜菜果胶浓度为1.5%,加酶量为100 nkat/g底物时,所获的凝胶具有最高的持水率(95.28%)。当大豆分离蛋白浓度为8%,甜菜果胶浓度为2.5%,加酶量为100 nkat/g底物时,双网络凝胶的硬度和咀嚼性分别为4.25/g和4.06/J。大豆分离蛋白-甜菜果胶双网络凝胶的构建,改善了凝胶的机械性能及持水能力,形成了更加有序的三维网状结构。     

Cross-linking proteins by laccase: Effects on the droplet size and rheology of emulsions stabilized by sodium caseinate

The aim of this work was to evaluate the influence of laccase and ferulic acid on the characteristics of oil-in-water emulsions stabilized by sodium caseinate at different pH (3, 5 and 7). Emulsions were prepared by high pressure homogenization of soybean oil with sodium caseinate solution containing varied concentrations of laccase (0, 1 and 5 mg/mL) and ferulic acid (5 and 10 mM). Laccase treatment and pH exerted a strong influence on the properties with a consequent effect on stability, structure and rheology of emulsions stabilized by Na-caseinate. At pH 7, O/W emulsions were kinetically stable due to the negative protein charge which enabled electrostatic repulsion between oil droplets resulting in an emulsion with small droplet size, low viscosity, pseudoplasticity and viscoelastic properties. The laccase treatment led to emulsions showing shear-thinning behavior as a result of a more structured system. O/W emulsions at pH 5 and 3 showed phase separation due to the proximity to protein pI, but the laccase treatment improved their stability of emulsions especially at pH 3. At pH 3, the addition of ferulic acid and laccase produced emulsions with larger droplet size but with narrower droplet size distribution, increased viscosity, pseudoplasticity and viscoelastic properties (gel-like behavior). Comparing laccase treatments, the combined addition of laccase and ferulic acid generally produced emulsions with lower stability (pH 5), larger droplet size (pH 3, 5 and 7) and higher pseudoplasticity (pH 5 and 7) than emulsion with only ferulic acid. The results suggested that the cross-linking of proteins by laccase and ferulic acid improved protein emulsifying properties by changing functional mechanisms of the protein on emulsion structure and rheology, showing that sodium caseinate can be successfully used in acid products when treated with laccase.     

A novel improvement in whey protein isolate emulsion stability: Generation of an enzymatically cross-linked beet pectin layer using horseradish peroxidase

Extensive research has indicated that the electrostatic attraction between polysaccharides and proteins on the oil-water interface can improve the stability of emulsions. However, this electrostatic effect will be weakened or even eliminated as the solution pH or ionic strength of emulsions change, resulting in the shedding of the polysaccharide layer. We prepared primary oil-in-water emulsions at pH 7.0 using whey protein isolate (WPI) as an emulsifier and then beet pectin was added to form secondary emulsions. After the pH of emulsions was adjusted to 4.0 to promote electrostatic attraction between the beet pectin molecules and the protein-coated droplets, horseradish peroxidase was added to generate a cross-linked beet pectin coating. Results show that stable emulsions coated with WPI and cross-linked beet pectin interfaces could be formed. The sensitivity of the emulsions to the environmental stresses of pH changes, ions addition, thermal processing and freezing was also characterized in this work. Our results support the view that cross-linked beet pectin improves the stability of emulsions and is superior to simple deposition on the surface of lipid droplets. The interfacial engineering technology used in this study could be used to create food emulsions with improved stability to environmental stresses.     

Properties of konjac glucomannan–whey protein isolate blend films

Edible composite packaging has been developed by blending biocomponents for specific applications, aiming to take advantage of complementary functional properties or to overcome their respective flaws. The aim of this work was to study the effect of incorporation of whey protein isolate (WPI) on the properties of konjac glucomannan (KGM) based films. Five aqueous solutions of KGM and/or WPI were prepared by casting and solvent evaporation of 1:0, 0.8:3.4, 0.6:3.6, 0.4:3.8 and 0:4.2 g KGM:g WPI/100 g solution. Glycerol (Gly) was used as a plasticizer at 1.5 and 1.8 g/100 g solution. The result showed that incorporated WPI proportionally increased transparency of KGM-based films. An increase in proportion of WPI resulted in decreased tensile strength and elastic modulus as well as improved flexibility. The incorporation of WPI into the KGM matrix led to an increase in water insolubility which enhanced product integrity and water resistance. Nevertheless, WPI did not improve water vapor barrier of KGM–WPI films. WPI and blend film with the highest concentration of WPI could be heat sealed at 175 °C. Overall, the range of Gly in this study did not apparently affect properties of the films.     

Oxidative cross-linking of potato proteins by fungal laccases: Reaction kinetics and effects on the structural and functional properties

Aiming at developing biocatalytic approach to modulate potato proteins functionalities, laccase-catalyzed oxidative cross-linking of potato proteins was investigated in terms of enzyme kinetics, reaction time course and product structural-functional properties. The catalytic efficiency (kcat/Km, mM⁻¹S⁻¹) of fungal laccases in oxidizing patatin-enriched potato protein (PAT, 0.010–0.748) was higher than that of potato protease inhibitors (PIs, 0.008–0.184). While PIs formed more efficiently oxidative cross-linked products. Cross-linking of potato proteins were achieved by laccase alone or by laccase-ferulic acid system; ferulic acid contributed to higher cross-linking extent and to the antioxidant activity of modified proteins. Potato proteins exhibited similar or slightly enhanced solubility upon cross-linking, except that highly cross-linked PIs (cross-linking extent >30%) obtained from Coriolus hirsutus laccase (LacCh)-treatments showed reduced solubility. General improvement in the emulsification property of potato proteins was observed upon cross-linking. Cross-linked potato proteins from LacCh-6 h treatment showed good foaming property; these proteins exhibited enhanced molecular flexibility and the characteristics of mild cross-linking extent (9.6–17.1%) with the accumulation of moderate molecular weight fraction (PAT:60–80 kDa, PIs:30–40 kDa). This study will lay foundations for the exploitation of potato proteins as functional ingredients.Industrial relevanceThe exploitation of novel proteins as functional ingredients is needed in order to meet the high demands for natural, healthy-oriented and sustainable food products. Laccase-catalyzed protein cross-linking is a promising green technology for tailoring the functionality of protein ingredients and achieving the desired textural/rheological quality of final products. The current study demonstrated the effectiveness of this enzymatic approach to enhance foaming and emulsifying properties of potato proteins. This approach can be adopted to modulate the functionality of other plant proteins and to develop plant proteins-based functional ingredients for various applications including stable delivery system, fat-replacing biopolymer matrix, meat analog/vegan products and gluten-replacement formulations.     

Laccase mediated conjugation of sugar beet pectin and the effect on emulsion stability

Laccase catalyzes intermolecular cross-links between ferulic acid of sugar beet pectin (SBP). Conjugation of SBP by laccase was confirmed by increased molecular weight, monitored by size exclusion chromatography, combined with multi-angle laser light scattering (SEC–MALLS), by reduced ferulic acid concentration detected at UV 325 nm, as well as by increased particle size. In addition, cross-linked SBP developed a more compact, branched structure as verified by a smaller root mean square (RMS) when molecular weight increased. Emulsions prepared with conjugated SBP had significantly smaller d_4,3 diameter and uniform droplet size, with more negative ζ-potential than non-treated SBP, during 30 days storage at 37 °C. The d_4,3 diameter was 5.3 μm and 3.8 μm for SBP and conjugated SBP, respectively. Covalently conjugated SBP has increased functionality and improved emulsion stability, most likely attributable to development of thick layer at the oil interface.     

Effects of the proteinaceous moiety on the emulsifying properties of sugar beet pectin

The role of the proteinaceous moiety in emulsifying was investigated using pectin from sugar beet as a model polysaccharide. Physicochemical and macromolecular characteristics of sugar beet pectin were examined with or without an enzymatic modification using multiple acid-proteinases. The enzymatic modification decreased the total protein content from 1.56±0.15% to 0.13±0.02% by the Bradford method without significant change in ferulic acid or most constitutional sugars. It also decreased the weight-average molecular weight (M_w) from 517±28 to 254±20 kg/mol and the z-average root-mean-square radius of gyration from 43.6±0.8 to 35.0±0.6 nm. Emulsifying properties of the polysaccharide with or without the enzymatic modification were evaluated by emulsion droplet size and creaming stability of O/W emulsions (pH 3.0) containing 15 w/w% middle-chain triglyceride and 1.5 w/w% sugar beet pectin as main constituents. The modification increased the average diameter (d_3,2) of emulsion droplets from 0.56±0.04 to 3.00±0.25 μm immediately after the preparation, suggesting a decrease in the emulsifying activity. It caused the creaming of the emulsions during incubation at 60 °C, which was in line with the finding that macroscopic phase separation occurred only in the presence of the modified pectin after storage at 20 °C for a day, suggesting a decrease in the emulsion stabilizing ability. The modification also decreased significantly the amount of the pectin fraction that adsorbed onto the surface of emulsion droplets from 14.58±2.21% to 1.22±0.03% and the interfacial concentration of the polysaccharide from 1.42±0.23 to 0.45±0.05 mg/m², where the proteinaceous materials in the pectin molecules activated the oil-water interface. Results from the present study suggest an important role of the proteinaceous moiety to explain the emulsifying properties of sugar beet pectin as in the case of gum arabic and soy soluble polysaccharide.     

Pectin quantity,composition and physicochemical behaviour as influenced by the purification process

To examine the purification procedure effect on the pectin amount, purity, macromolecular characteristics, and gelling ability, three pectin isolates, namely, alcohol (APP)-, dialysis (DPP)-, and metal ion (MPP)-purified pectins are obtained from acid extracts of yellow passion fruit rind using alcohol-precipitation, dialysis, or ion-binding precipitation. The results show that the amount of MPP (4.1 g/100 g) is significantly (p < 0.05) lower than the amount of the two other pectins (6.8–7.5 g/100 g). In contrast, MPP has a higher galacturonic acid (78.9 g/100 g) and lower neutral sugar (9.7 g/100 g), ash (0.9 g/100 g), and protein (1.4 g/100 g) contents than the remainder (62.4–70.1, 16.0–17.8, 2.7–5.8, 3.1–3.2 g/100 g, respectively). Molecular-weight distribution patterns suggest that MPP is free of neutral sugar oligosaccharide contaminants unlike the others, especially APP. Therefore, the term of ‘the galacturonic acid yield’ is introduced to complement the conventional term of ‘the pectin yield’. Furthermore, MPP gel preparation is likely to set more rapidly, with the gel formed achieving a much higher strength. It is concluded that the pectin amount, composition, and physicochemical properties can be considerably affected by the purification mode.     

Physicochemical properties of sugar beet pulp pectin by pulsed electric field treatment

This research focused on pulsed electric field (PEF) modification of pectin from sugar beet pulp. Experimental parameters including electric field intensity (18–30 kV cm^?1) and pulse time (806–2418 μs) were used, and the physicochemical properties of PEF‐treated pectin were evaluated by various instrumental techniques such as scanning electron microscopy, X‐ray diffraction, dynamic light scattering and Fourier transform infrared spectroscopy. The results showed that the degree of esterification, viscosity average molecular weight and particle size of pectin decreased with the increase in electric field intensity and pulse time. Meanwhile, some sharp interstices were shown on the surface of pectin, and its crystalline regions were destroyed after being treated with PEF. Results revealed that PEF technology is an effective method to obtain low‐molecular‐weight pectin with different degrees of esterification and obtain a desired production in food application.     

Functional properties of milk proteins as affected by enzymatic oligomerisation

Milk proteins were enzymatically modified by transglutaminase, lactoperoxidase, laccase as well as glucose oxidase and analysed for changes in molar mass distribution, techno- and tropho-functional properties.The study revealed that high degrees of protein cross-linking were not only detected upon enzymatic modification of milk proteins by transglutaminase, but also upon incubation with oxidoreductases like lactoperoxidase, laccase as well as glucose oxidase. Due to different reaction mechanisms, oligomeric (20,000–200,000 g/mol) and polymeric (>200,000 g/mol) reaction products with different functional property profiles were synthesised. In contrast to transglutaminase-treated milk proteins, e.g., lactoperoxidase-treated milk proteins performed outstanding interfacial properties and glucose oxidase-treated milk proteins higher in vitro digestibility. Oxidoreductase-treated proteins were shown to exhibit increased antioxidative capacity. Laccase was demonstrated to generate oligomeric as well as polymeric protein/protein and protein/phenolic acid reaction products.The study characterises enzymatically cross-linked proteins and makes it possible to specifically select modified proteins for industrial applications according to the requirements towards food proteins, weighing changes in techno- and tropho-functional protein properties.     

Encapsulation of eugenol using Maillard-type conjugates to form transparent and heat stable nanoscale dispersions

Maillard-type protein-carbohydrate conjugates are known for their excellent emulsifying properties and have been used to encapsulate volatile oils and flavor compounds. In the present study, eugenol was used as a model compound for encapsulation in conjugates of whey protein isolate (WPI) and maltodextrins (MD) made using different WPI:MD mass ratios and MD chain lengths. The encapsulation involved two steps, emulsifying an oil phase of eugenol dissolved in hexane into an aqueous phase with dissolved conjugates and spray drying the emulsion. Mass yield up to 82.7 g/100 g and encapsulation efficiency as high as 35.7 g/100 g eugenol were observed. After hydrating spray-dried powders, several samples with an eugenol content above its solubility limit demonstrated transparent dispersions at pH 3.0 and 7.0 after heating at 80 °C for 15 min, corresponding to mean diameters smaller than ca. 100 nm. One treatment also showed transparent dispersions after heating at pH 5.0, which is near the isoelectric point of whey proteins, in contrast to gel formation for a control prepared with a mixture of non-conjugated WPI and MD. The present study demonstrates potential to produce food grade nanoscale systems for delivering lipophilic bioactives in functional beverages, without adversely affecting their visual appearance.     

Effects of sucrose on egg white protein and whey protein isolate foams: Factors determining properties of wet and dry foams (cakes)

The effects of sucrose on the physical properties of foams (foam overrun and drainage ½ life), air/water interfaces (interfacial dilational elastic modulus and interfacial pressure) and angel food cakes (cake volume and cake structure) of egg white protein (EWP) and whey protein isolate (WPI) was investigated for solutions containing 10% (w/v) protein. Increasing sucrose concentration (0–63.6 g/100 mL) gradually increased solution viscosity and decreased foam overrun. Two negative linear relationships were established between foam overrun and solution viscosity on a log–log scale for EWP and WPI respectively; while the foam overrun of EWP decreased in a faster rate than WPI with increasing solution viscosity (altered by sucrose). Addition of sucrose enhanced the interfacial dilational elastic modulus (E′) of EWP but reduced E′ of WPI, possibly due to different interfacial pressures. The foam drainage ½ life was proportionally correlated to the bulk phase viscosity and the interfacial elasticity regardless of protein type, suggesting that the foam destabilization changes can be slowed by a viscous continuous phase and elastic interfaces. Incorporation of sucrose altered the volume of angel food cakes prepared from WPI foams but showed no improvement on the coarse structure. In conclusion, sucrose can modify bulk phase viscosity and interfacial rheology and therefore improve the stability of wet foams. However, the poor stability of whey proteins in the conversion from a wet to a dry foam (angel food cake) cannot be changed with addition of sucrose.     

Stabilization of oil-in-water emulsions by enzyme catalyzed oxidative gelation of sugar beet pectin

Enzyme catalyzed oxidative cross-linking of feruloyl groups can promote gelation of sugar beet pectin (SBP). It is uncertain how the enzyme kinetics of this cross-linking reaction are affected in emulsion systems and whether the gelation affects emulsion stability. In this study, SBP (2.5% w/v) was mixed into an oil-in-water emulsion system (4.4% w/w oil, 0.22% w/w whey protein, pH 4.5). Two separate, identically composed, emulsion systems were prepared by different methods of preparation. The emulsions prepared separately and subsequently mixed with SBP (referred as Mix A) produced significantly larger average particle sizes than the emulsions in which the SBP was homogenized into the emulsion system during emulsion preparation (referred as Mix B). Mix B type emulsions were stable. Enzyme catalyzed oxidative gelation of SBP helped stabilize the emulsions in Mix A. The kinetics of the enzyme catalyzed oxidative gelation of SBP was evaluated by small angle oscillatory measurements for horseradish peroxidase (HRP) (EC 1.11.1.7) and laccase (EC 1.10.3.2) catalysis, respectively. HRP catalyzed gelation rates, determined from the slopes of the increase of elastic modulus (G′) with time, were higher (P < 0.05) than the corresponding laccase catalyzed rates, but the final G′ values were higher for laccase catalyzed gels, regardless of the presence of emulsions or type of emulsion preparation (Mix A or Mix B). For both enzymes, rates of gelation in Mix A were higher (P < 0.05) than in Mix B, and higher stress was needed to break the gels in Mix A than in Mix B at similar enzyme dosage levels. These differences may be related to a lower availability of the feruloyl groups for cross-linking when the SBP was homogenized into the emulsion system during preparation.     

Use of applied air pressure to improve the baking properties of whey protein isolates in angel food cakes

Whey protein isolate (WPI) possesses limited application in angel food cake baking compared to liquid egg white (LEW). This study was conducted to determine whether applying air pressure in the oven during baking would improve the baking properties of WPI in angel food cakes. A special oven was designed for baking at oven air pressures up to 1.5 bar. Control angel food cakes were formulated with LEW (100/0) as its protein source and WPI-containing cakes were formulated with a mixture of 75 mL/100 mL LEW and 25 mL/100 mL WPI solution (75/25) or a mixture of 50 mL/100 mL LEW and 50 mL/100 mL WPI solution (50/50). Cakes were baked at atmospheric air pressure (AP) and at constant applied air pressure (CAP) or variable applied air pressure vs. baking time (VAP) to prevent overexpansion and collapse of WPI-containing cake batter. Cakes 75/25 and 50/50 baked at VAP exhibited improved physical, textural and sensory properties compared to those baked at AP or CAP conditions. Cakes 75/25 baked at VAP compared well with control angel food cakes baked at AP. Although 50/50 cakes baked at VAP were improved slightly over those baked at AP, none of them exhibited satisfactory properties. Therefore, additional research is needed to optimize baking conditions for cakes formulated with less than 75 mL/100 mL LEW.     

Characterization of Chemically and Thermally Treated Oil‐in‐Water Heteroaggregates and Comparison to Conventional Emulsions

Heteroaggregated oil‐in‐water (O/W) emulsions formed by targeted combination of oppositely charged emulsion droplets were proposed to be used for the modulation of physical properties of food systems, ideally achieving the formation of a particulate 3‐dimensional network at comparably low‐fat content. In this study, rheological properties of Quillaja saponins (QS), sugar beet pectin (SBP), and whey protein isolate (WPI) stabilized conventional and heteroaggregated O/W emulsions at oil contents of 10% to 60% (w/w) were investigated. Selected systems having an oil content of 30% (w/w) and different particle sizes (d₄₃ ≤ 1.1 or ≥16.7 μm) were additionally subjected to chemical (genipin or glutaraldehyde) and thermal treatments, aiming to increase network stability. Subsequently, their rheological properties and stability were assessed. Yield stresses (τ₀) of both conventional and heteroaggregated O/W emulsions were found to depend on emulsifier type, oil content, and initial droplet size. For conventional emulsions, high yield stresses were only observed for SBP‐based emulsions (τ₀,_SBP approximately 157 Pa). Highest yield stresses of heteroaggregates were observed when using small droplets stabilized by SBP/WPI (approximately 15.4 Pa), being higher than those of QS/WPI (approximately 1.6 Pa). Subsequent treatments led to significant alterations in rheological properties for SBP/WPI systems, with yield stresses increasing 29‐fold (glutaraldehyde) and 2‐fold (thermal treatment) compared to untreated heteroaggregates, thereby surpassing yield stresses of similarly treated conventional SBP emulsions. Genipin‐driven treatments proved to be ineffective. Results should be of interest to food manufacturers wishing to design viscoelastic food emulsion based systems at lower oil droplet contents.