Fabrication of soy protein-polyphenol covalent complex nanoparticles with improved wettability to stabilize high-oil-phase curcumin emulsions.

BACKGROUND: Recent studies have shown that the wettability of protein-based emulsifiers is critical for emulsion stability. However, few studies have been conducted to investigate the effects of varying epigallocatechin gallate (EGCG) concentrations on the wettability of protein-based emulsifiers. Additionally, limited studies have examined the effectiveness of soy protein-EGCG covalent complex nanoparticles with improved wettability as emulsifiers for stabilizing high-oil-phase (≥ 30%) curcumin emulsions. RESULTS: Soy protein isolate (SPI)-EGCG complex nanoparticles (SPIEn) with improved wettability were fabricated to stabilize high-oil-phase curcumin emulsions. The results showed that EGCG forms covalent bonds with SPI, which changes its secondary structure, enhances its surface charge, and improves its wettability. Moreover, SPIEn with 2.0 g L -1 EGCG (SPIEn-2.0) exhibited a better three-phase contact angle (56.8 ± 0.3o) and zeta potential (-27 mV) than SPI. SPIEn-2.0 also facilitated the development of curcumin emulsion gels at an oil volume fraction of 0.5. Specifically, the enhanced network between droplets as a result of the packing effects and SPIEn-2.0 with inherent antioxidant function was more effective at inhibiting curcumin degradation during long-term storage and ultraviolet light exposure. CONCLUSION: The results of the present study indicate that SPIEn with 2.0 g L -1 EGCG (SPIEn-2.0) comprises the optimum conditions for fabricating emulsifiers with improved wettability. Additionally, SPIEn-0.2 can improve the physicochemical stability of high-oil-phase curcumin emulsions, suggesting a novel strategy to design and fabricate high-oil-phase emulsion for encapsulating bioactive compounds. © 2024 Society of Chemical Industry.

Effect of sodium metabisulfite-mediated self-assembly on the quality of silver carp myofibrillar protein-EGCG composite gels.

Myofibrillar protein (MP) gels are susceptible to oxidation, which can be prevented by complexing with hydrophilic polyphenols, but may cause gel deterioration. Sodium metabisulfite (Na2S2O5) has been used to induce self-assembly of MP and analyze the impact of self-assembly on the quality of composite gels containing high amounts of (-)-epigallocatechin gallate (EGCG). Hydrophobic forces were confirmed as the main driver of self-assembly. Self-assembly reduced the size of the MP-EGCG complex to approximately 670 nm and increased the gel's hydrophobic force by approximately 3.6-fold. The maximum hardness of the Na2S2O5-treated MP-EGCG composite gel was 52.43 g/kg, which was approximately 49% greater than pure MP gel. After oxidative treatment, the Na2S2O5-treated MP-EGCG composite gel had considerably lower carbonyl and dityrosine levels (2.47-µmol/g protein and 450 a.u.) than the control (8.37-µmol/g protein and 964 a.u.). Therefore, Na2S2O5 shows potential as a cost-effective additive for alleviating MP limitations in the food industry.

Modulation of fried spring roll wrapper quality upon treatment of batter with maltogenic amylase, transglutaminase and bromelain.

BACKGROUND: Fried foods are favored for their unique crispiness, golden color and flavor, but they also face great challenge because of their high oil content, high calories and the existence of compounds such as acrylamide and polycyclic aromatic hydrocarbons. Long-term consumption of fried foods may adversely affect health. Therefore, it is necessary to explore fried foods with lower oil contents and a high quality to meet the demand. RESULTS: A method of enzyme treatment was explored to investigate the effects of maltogenic amylase (MA), transglutaminase (TG) and bromelain (BRO) on the physicochemical properties of the batter and the quality of fried spring roll wrapper (FSRW). The results showed that the MA-, TG- or BRO-treated batters had a significant shear-thinning behavior, especially with an increase in viscosity upon increasing TG contents. FSRW enhanced its fracturability from 419.19 g (Control) to 616.50 g (MA-6 U g-1), 623.49 g (TG-0.75 U g-1) and 644.96 g (BRO-10 U g-1). Meanwhile, in comparison with BRO and MA, TG-0.5 U g-1 endowed batter with the highest density and thermal stability. MA-15 U g-1 and TG-0.5 U g-1 displayed FSRW with uniform and dense pores, and significantly reduced its oil content by 18.05% and 25.02%, respectively. Moreover, compared to MA and TG, BRO-50 U g-1 improved the flavor of FSRW. CONCLUSION: MA, TG or BRO played a key role in affecting the physicochemical properties of the batter and the quality of FSRW. TG-0.5 U g-1 remarkly reduced the oil content of FSRW with a great potential in practical application. © 2024 Society of Chemical Industry.

Comparisons in phytochemical components and in vitro digestion properties of corresponding peels, flesh and seeds separated from two blueberry cultivars.

Highbush blueberries (HB) and rabbiteye blueberries (RB) were separated into peels, flesh, and seeds to assess the compositions of nutriment, anthocyanins, soluble sugars and fatty acids, and the in vitro digesting abilities. Total phenolics contents (TPC) of 51-56 mg GAE/g DW were found in blueberry peels. Compared with HB peels, RB peels showed much higher TPC, but only contained 35 phenolics and lacked peonidin-3-O-rutinoside. Glucose, fructose, and sucrose were all present in HB and RB, but RB flesh had a higher acid-sugar ratio. Unsaturated fatty acid concentrations in HB and RB seeds were comparable (26.65 and 26.43 mg/g, respectively). However, HB seeds have 35 fatty acids, but RB seeds lacked cis-4,7,10,13,16,19-docosahexaenoic acid and cis-10-pentadecenoic acid. The in vitro digestion test showed that the whole fruit/peels/flesh of RB had a higher recovery and bioavailability index of phenolics and anthocyanins. Therefore, the reuse of blueberry pomace needs to be emphasized. Supplementary Information: The online version contains supplementary material available at 10.1007/s10068-023-01326-w.

Fabrication and characterization of soy protein isolation-ferulic acid antioxidant hydrogels.

BACKGROUND: Soy protein gel products are prone to direct oxidation by reactive oxygen during processing and transportation, thus reducing their functional properties and nutritional values. A covalent complex was prepared with soy protein isolate (SPI) and ferulic acid (FA) catalyzed by laccase (LC). The complex was further treated with microbial transglutaminase (TGase) to form hydrogels. The structural changes of the covalent complex (SPI-FA) and the properties and antioxidant stability of hydrogel were investigated. RESULTS: The SPI-FA complexes were demonstrated to be covalently bound by sodium dodecyl sulfate-polyacrylamide gel electrophoresis, and they had the least hydrophobic and free sulfhydryl groups at a 1.0 mg mL-1 FA concentration. The α-helix of complexes increased from 11.50% to 27.39%, and random coil dropped from 26.06% to 14.44%. The addition of FA caused SPI fluorescence quenching and redshift. The hydrogel was formed after the complex was induced with TGase, and its hardness and water holding capacity was increased by 50.61% and 26.21%, respectively. Scanning electron microscopy showed that a layered and ordered gel structure was formed. After in vitro digestion, the complex hydrogels maintained stable antioxidant activity, and the free radical scavenging rates of DPPH and ABTS reached 87.65% and 84.45%, respectively. CONCLUSION: SPI-FA covalent complexes were prepared under laccase catalysis, and complex hydrogels were formed by TGase. Hydrogels have stable antioxidant activity, which provides application prospects for the antioxidant development of food. © 2023 Society of Chemical Industry.

Self-assembled pea vicilin nanoparticles as nanocarriers for improving the antioxidant activity, environmental stability and sustained-release property of curcumin.

BACKGROUND: The application of curcumin (Cur) in the food industry is usually limited by its low water solubility and poor stability. This study aimed to fabricate self-assembled nanoparticles using pea vicilin (7S) through a pH-shifting method (pH 7-pH 12-pH 7) to develop water-soluble nanocarriers of Cur. RESULTS: Intrinsic fluorescence, far-UV circular dichroism spectra and transmission electron microscopy analysis demonstrated that the structure of 7S could be unfolded at pH 12.0 and refolded when the pH shifted to 7.0. The assembled 7S-Cur exhibited a high loading ability of 81.63 µg mg-1 for Cur and homogeneous particle distribution. Cur was encapsulated in the 7S hydrophobic nucleus in an amorphous form and combined through hydrophobic interactions and hydrogen bonding, resulting in the static fluorescence quenching of 7S. Compared with free Cur, the retention rates of Cur in 7S-Cur were approximately 1.12 and 1.70 times higher under UV exposure at 365 nm or heating at 75 °C for 120 min, respectively, as well as 7S-Cur showing approximately 1.50 times higher antioxidant activity. During simulated gastrointestinal experiments, 7S-Cur exhibited a better sustained-release property than free Cur. CONCLUSION: The self-assembled 7S nanocarriers prepared using a pH-shifting method effectively improved the antioxidant activity, environmental stability and sustained-release property of Cur. Therefore, 7S isolated from pea protein could be used as potential nanocarriers for Cur. © 2023 Society of Chemical Industry.

Preparation of high complex concentration emulsion stabilized by soy protein/dextran sulfate composite particles.

BACKGROUND: Soy protein isolate (SPI) can be used as an emulsifier to stabilize emulsions, though SPI is unstable under low acidic conditions. Stable composite particles of SPI and dextran sulfate (DS) can be formed by the electrostatic interaction at the pH 3.5. Furthermore, the SPI/DS composite particles can be used to prepare a high complex concentration emulsion. The stabilization properties of the high complex concentration emulsion were investigated. RESULTS: Compared to uncompounded SPI, the particle size of SPI/DS composite particles was smaller at 1.52 µm, and the absolute value of the potential increased to 19.9 mV when the mass ratio of SPI to DS was 1:1 and the pH was 3.5. With the DS ratio increased, the solubility of the composite particles increased to 14.44 times of the untreated protein at pH 3.5, while the surface hydrophobicity decreased. Electrostatic interactions and hydrogen bonds were the main forces between SPI and DS, and DS was electrostatically adsorbed on the surface of SPI. The emulsion stability significantly enhanced with the increase of complex concentration (38.88 times higher than at 1% concentration), the emulsion average droplet size was the lowest (9.64 µm), and the absolute value of potential was the highest (46.67 mV) when the mass ratio of SPI to DS was 1:1 and the complex concentration of 8%. The stability of the emulsion against freezing was improved. CONCLUSION: The SPI/DS complex has high solubility and stability under low acidic conditions, and the emulsion of the SPI/DS complex has good stability. © 2023 Society of Chemical Industry.

Infrared radiation blanching-inhibited browning and extended shelf life of pecan kernels.

To evaluate infrared radiation (IR) blanching in comparison to conventional hot water (HW) blanching in inhibiting the browning and extending the shelf life of pecan kernels, the technology of IR blanching at 500-700 W for 90-45 s or HW blanching at 90°C for 60 s, and subsequently drying with hot air at 60, 70, and 80°C, respectively, was used, and then the activities of lipoxidase (LOX) and polyphenol oxidase (PPO), antioxidant capacities, color change, microscopic structure, and the shelf life of kernels were analyzed. Results showed that IR blanching not only significantly decreased the subsequent drying time but also effectively inactivated the activities of LOX and PPO, showing a lower residual activity of 15.74%-40.41% and 16.75%-56.25%, respectively. A higher retention of total phenolics was observed in kernels subjected to IR blanching, from 25.03 ± 0.04 to 29.50 ± 0.96 mg GAE/g compared with HW blanching (14.43 ± 0.07 mg GAE/g). Meanwhile, IR-blanched samples showed lower peroxide values, p-anisidine values, total color difference values, browning index, quinones contents, and lipofuscin-like pigments levels but had higher 2,2-diphenyl-1-picrylhydrazyl inhibition rate and better storage stabilities than HW-blanched samples. The technology of IR blanching at 600 W for 60 s followed by drying with hot air at 70°C for 40 min is suitable for producing pecan kernels with better qualities and a longer shelf life, through inactivating the endogenous enzymatic reactions and inhibiting the formation of lipofuscin-like pigments. PRACTICAL APPLICATION: Blanching is an essential pretreatment of food processing. Conventional blanching is achieved by hot water, which has some disadvantages of low-intensity enzyme inactivation, loss of water-soluble substances, etc. In this study, the potential of using infrared blanching, prior to drying, was studied to find solutions to improve the nutritional value, and the shelf life of pecan kernels. The results showed that infrared blanching at 600 W for 60 s followed by drying with hot air at 70°C for 40 min could inhibit the color degradation, improve the oxidation resistance, and prolong the shelf life of kernels.

Effect of sodium trimetaphosphate on the physicochemical properties of modified soy protein isolates and its lutein-loaded emulsion.

Due to people's pursuit of healthy and green life, soy protein isolate (SPI) is occupying a larger and larger market share. However, the low solubility of SPI affects its development in the field of food and medicine. This paper aimed to investigate the effects of sodium trimetaphosphate (STMP) on the functional properties and structures of phosphorylated SPI and its lutein-loaded emulsion. After modification by STMP, the phosphorus content of phosphorylated SPI reached 1.2-3.61 mg/g. Infrared spectrum and X-ray photoelectron spectrum analysis confirmed that PO4 3- had phosphorylation with -OH in serine of SPI molecule. X-ray diffraction analysis showed that phosphorylation destroyed the crystal structure of protein molecules. Zeta potential value of phosphorylated SPI decreased significantly. When STMP addition was 100 g/kg, particle size of protein solution decreased to 203 nm, and solubility increased to 73.5%. Furthermore, emulsifying activity and emulsifying stability increased by 0.51 times and 8 times, respectively. At the same protein concentration (1%-3% [w/w]), lutein-loaded emulsion prepared by phosphorylated SPI had higher absolute potential and smaller particle size. The phosphorylated protein emulsion at 2% concentration had the best emulsion stability after storage for 17 days. PRACTICAL APPLICATION: Phosphorylation significantly improved the emulsifying properties and solubility of SPI. Phosphorylated SPI significantly improved the stability of lutein-loaded emulsion. It provides theoretical basis for the application of phosphorylated SPI as emulsifier in delivery system and broadens the development of lutein in food and medicine field.

The preparation of soy glycinin/sugar beet pectin complex network gels catalyzed by laccase under weakly acidic conditions.

BACKGROUND: Traditional soy protein gel products such as tofu, formed from calcium sulfate or magnesium chloride, have poor textural properties and water retention capacity. Soy glycinin (SG) is the main component affecting the gelation of soy protein and can be cross-linked with polysaccharides, such as sugar beet pectin (SBP), and can be modified by changing system factors (e.g., pH) to improve the gel's properties. Soy glycinin/sugar beet pectin (SG/SBP) complex double network gels were prepared under weakly acidic conditions using laccase cross-linking and heat treatment. The structural changes in SG and the properties of complex gels were investigated. RESULTS: Soy glycinin exposed more hydrophobic groups and free sulfhydryl groups at pH 5.0. Under the action of laccase cross-linking, SBP could promote the unfolding of SG tertiary structures. The SG/SBP complex gels contained 46.77% ß-fold content and had good gelling properties in terms of hardness 290.86 g, adhesiveness 26.87, and springiness 96.70 mm at pH 5.0. The T22 relaxation time had the highest peak, and magnetic resonance imaging (MRI) showed that the gel had even water distribution. Scanning electron microscopy (SEM) and confocal scanning laser microscopy (CLSM) indicated that the SG/SBP complex network structure was uniform, and the pore walls were thicker and contained filamentous structures. CONCLUSION: Soy glycinin/ sugar beet pectin complex network gels have good water-holding, rheological, and textural properties at pH 5.0. The properties of soy protein gels can be improved by binding to polysaccharides, with laccase cross-linked, and adjusting the pH of the solution. © 2022 Society of Chemical Industry.

Glycated Soy ß-Conglycinin Nanoparticle for Efficient Nanocarrier of Curcumin: Formation Mechanism, Thermal Stability, and Storage Stability.

In this study, soy ß-conglycinin (7S) was glycated with dextran of different molecular masses (40, 70, 150, 500 kDa) by the dry-heating method to synthesize soy ß-conglycinin-dextran (7S-DEX) conjugates. The curcumin (Cur) loaded nanocomplexes were prepared based on 7S-DEX conjugates by a pH-driven self-assemble strategy to enhance the solubility and thermal stability of curcumin. Results showed that the 7S-150 conjugates (glycated from 7S with dextran (150 kDa)) could remain stable in the pH 3.0-pH 8.0 range and during the heat treatment. The results of fluorescence quenching and FT-IR indicated that glycated 7S were combined with curcumin mainly by hydrogen bonding and hydrophobic interaction, and 7S-150 conjugates had higher binding affinity than natural 7S for curcumin. The loading capacity (µg/mg) and encapsulation efficiency (EE%) of 7S-150-Cur were 16.06 µg/mg and 87.51%, respectively, significantly higher than that of 7S-Cur (12.41 µg/mg, 51.15%). The XRD spectrum showed that curcumin was exhibited in an amorphous state within the 7S-150-Cur nanocomplexes. After heating at 65 °C for 30 min, the curcumin retention of the 7S-150-Cur nanocomplexes was about 1.4 times higher than that of free curcumin. The particle size of 7S-150-Cur nanocomplexes was stable (in the range of 10-100 nm) during the long storage time (21 days).

Microencapsulation of blueberry anthocyanins by spray drying with soy protein isolates/high methyl pectin combination: Physicochemical properties, release behavior in vitro and storage stability.

Eleven anthocyanins in the blueberry anthocyanins powders (BAP) were identified and quantified by HPLC-DAD-ESI-MS. BAP microcapsules (MBAP) were produced by spray drying using high methyl pectin (HMP) combined with whey protein isolates (WPI) or soy protein isolates (SPI) in different proportions as wall materials. Generally, SPI/HMP combination was more efficient in increasing the encapsulation efficiency and Tg, and in decreasing the particle size and hygroscopicity of the microcapsules than WPI or HMP or WPI/HMP combination. Microcapsules created with 4% SPI + 2% HMP combination (MBAPc), possessed superior anthocyanin release behavior and antioxidant stability to those produced with 4% SPI alone (MBAPs). Both MBAPc and MBAPs had continuous release of anthocyanins throughout the simulated gastrointestinal digestion, and exhibited two first-order kinetics, but MBAPc exhibited higher stability than MBAPs and BAP, because it showed the longest half-life and the lowest anthocyanin degradation rate at 25 °C and 35 °C during 6-months' storage.

Fabrication and characterization of soy ß-conglycinin-dextran-polyphenol nanocomplexes: Improvement on the antioxidant activity and sustained-release property of curcumin.

In this study, glycated soy ß-conglycinin (ß-CG) stabilized curcumin (Cur) composites were fabricated by a unique reversible self-assembly character of ß-conglycinin-dextran conjugates (ß-CG-DEX). Intrinsic fluorescence and far-UV CD spectra revealed that glycation did not affect the self-assembly property of ß-CG in the pH-shifting treatment. The structure of ß-CG-DEX could be unfolded at pH 12.0 and reassembled during acidification (from pH 12.0 to 7.0). Meanwhile, ß-CG-DEX-3d, which was incubated at 60 °C for 3 days, exhibited a high loading capacity (123.4 mg/g) for curcumin, which far exceeds that (74.90 mg/g) of ß-CG-Cur. Moreover, the reassembled ß-CG-DEX-3d-Cur showed eminent antioxidant activity of approximately 1.5 times higher than that of free curcumin. During the simulated gastrointestinal condition, compared with ß-CG-Cur, ß-CG-DEX-3d-Cur nanoparticles showed a more stable and sustained release of curcumin. Thus, ß-CG-DEX has immense potential to become a new delivery carrier for hydrophobic food components by means of a self-assembly strategy.

Encapsulation of curcumin in soluble soybean polysaccharide-coated gliadin nanoparticles: interaction, stability, antioxidant capacity, and bioaccessibility.

BACKGROUND: Gliadin nanoparticles are used as a delivery system for active substances because of their amphiphilicity and bioavailability. However, they are susceptible to destabilization by external agents. In this study, gliadin nanoparticles stabilized by soluble soybean polysaccharide (SSPS) were prepared by antisolvent precipitation. Formed stable complex nanoparticles were applied to protect and deliver curcumin (Cur). RESULTS: Gliadin/SSPS nanoparticles with the smallest particle size (196.66 nm, polydispersity index < 0.2) were fabricated when the mass ratio of gliadin to SSPS was 1:1 at pH 5.0. SSPS-stabilized gliadin nanoparticles had excellent stability at pH 3.0-8.0, 0.02-0.1 mol L-1 NaCl and at 90 °C heat. Gliadin/SSPS nanoparticles were used to encapsulate the Cur. The encapsulation efficiency of the Cur-loaded gliadin/SSPS nanoparticles was 84.59%. Fourier transform infrared spectroscopy and fluorescence spectrophotometry showed that the main forces were hydrogen bonds, electrostatic interactions and hydrophobic interactions between gliadin and SSPS. The X-ray diffraction patterns exhibited that the crystalline form of Cur converted to an amorphous substance. The retention rates of Cur-loaded gliadin/SSPS nanoparticles reached 79.03%, 73.43% and 87.92% after ultraviolet irradiation for 4 h, heating at 90 °C and storage at 25 °C for 15 days, respectively. Additionally, simulated digestion demonstrated that the bioavailability of gliadin/SSPS-Cur nanoparticles was four times higher than that of free Cur. CONCLUSION: This study showed that SSPS improved the stability of gliadin nanoparticles. Gliadin/SSPS nanoparticles have the function of loading and delivering Cur. © 2022 Society of Chemical Industry.

Modification of the structural and functional properties of wheat gluten protein using a planetary ball mill.

The modification of the structure and function of wheat gluten because of planetary ball milling was investigated. Reduced SDS-PAGE revealed that the subunit compositions and bands of gluten did not change with an increase in grinding time. FTIR analysis showed that α-helices and ß-sheets decreased, whereas ß-turns increased, indicating that the secondary structure of gluten became looser and more disorderly. Owing to the mechanical force of planetary ball milling constantly breaking the disulfide bonds in gluten, the number of free sulfhydryl groups increased, and surface hydrophobicity increased from 940.97 to 1197.50 after 20 min ball-milling treatments, whereas the foaming capacity was improved from 8.7 to 31 cm3. After 40 min, mastersizer analysis showed that particle size decreased from 85.9 to 32.3 µm, and the whiteness increased from 49.51 to 65.59. These results indicate that planetary grinding technology improves the functional properties of wheat gluten and expands its application potential.

Properties of transglutaminase-induced myofibrillar/wheat gluten gels.

Gelation properties of myofibrillar protein (MP)/wheat gluten (WG) induced by glutamine transaminase (TGase) were studied. Results showed that the inclusion of transglutaminase increased the gel strength, water-holding capacity (WHC), and nonfreezable water (Wnf) of MP/WG mixture. Circular dichroism (CD) analysis showed that the ß-sheet and random coil content of the MP/WG treated with TGase addition increased by 12.1% and 3.7%, while the α-helix and ß-turn content decreased by 14.2% and 1.8%. Rheological measurements showed that TGase induced higher energy storage modulus value during the MP/WG gel heating-cooling cycle. the hydrogen bond and hydrophobic interaction content of the MP/WG gels increased by 80 and 120 ug/L, and the disulfide bond decreased by 200 ug/L, with TGase addition was increased from 0 to 120 U/g protein. Scanning electron microscope (SEM) showed that MP/WG gel with TGase had uniform and dense network structure. PRACTICAL APPLICATION: The properties of myofibrillar/wheat gluten gel induced by TGase crosslinking was studied. The gel structure and water holding capacity of MP/WG were improved by the cross-linking of TGase. The study of the gel properties of MP/WG induced by TGase crosslinking also can provide a theoretical basis for analyzing the effect of TGase on the application of gluten protein in complex meat emulsion system.

Study on preparation of acylated soy protein and stability of emulsion.

BACKGROUND: Protein can be used as an emulsifier to improve emulsion stability at the interface of water-in-oil emulsion. However, natural soybean protein isolate (SPI) does not meet the high demands as an emulsifier in the food industry. The effect of acylation modification by ethylenediaminetetraacetic dianhydride (EDTAD; 0-300 g kg-1 ) on the physicochemical properties of SPI was studied. RESULTS: The results of the Fourier transform infrared spectra analyses showed that carboxyl groups were introduced into the SPI structure by the EDTAD treatment. The carboxyl concentration of SPI was increased by 30-74.07% with an increase in EDTAD addition from 50 to 300 g kg-1 . When 150 g kg-1 EDTAD was added, the surface hydrophobicity, the emulsifying activity, and the absolute value of the zeta potential were increased by 213%, 120%, and 68% respectively, and the particle size decreased to 247 nm. The droplet size of emulsion decreased to 10 µm when pH was 6. At the same concentration of SPI and pH, the absolute value of zeta potential of the emulsion was biggest. A comparison of the emulsions during storage showed the improvement of emulsion stability was related to the increase in the zeta potential and the decrease in the average particle size. The experimental group showed no destabilization on day 21, and no obvious aggregation phenomenon was observed. CONCLUSION: Acylation modification by EDTAD changed the emulsifying properties of SPI and enhanced the stability of the SPI emulsion. © 2021 Society of Chemical Industry.

Pectin-peptide complexes ameliorated physicochemical stabilities and in vitro digestion abilities of ß-carotene loaded emulsions.

To improve the stabilities of low methoxy pectin (LMP) stabilized O/W emulsions for the delivery of bioactive substances, LMP was firstly modified with soy peptide (SP), corn peptide (CP) and whey protein peptide (WPP), respectively, by using dry-heat method, then the properties of LMP-peptide complexes stabilized O/W emulsions were characterized and the in vitro digestion of emulsions with ß-carotene was test to evaluate the potential applications. LMP-peptide complexes were formed by covalent bonds according to FT-IR spectroscopy. Compared to LMP stabilized emulsions, LMP-peptide complexes stabilized emulsions had smaller droplet sizes and higher stabilities in the changed pH value, temperature and ionic strength. Based on the results of in vitro digestion tests, LMP-SP and LMP-WPP obtained by incubating LMP with peptides at 60 °C for 12 h at the weight ratio of 4:1 were more suitable for the preparation of O/W emulsions to deliver camellia oil and ß-carotene.

Effects of tea polyphenol ester with different fatty acid chain length on camellia oil-based oleogels preparation and its effects on cookies properties.

Oleogels were prepared by emulsion template method through 3.0% tea polyphenol ester (Tp-ester) particles with four fatty acid chain length (Tp-laurate [C12], Tp-myristate [C14], Tp-palmitate [C16], and Tp-stearate [C18]) and 2.5% citrus pectin, and then were used in cookie production as fat replacer. Effects of the fatty acid chain length on the hydrophilicity/hydrophobicity of Tp-ester, on the appearance, microstructure, and firmness of dried products, on rheological features of oleogels, on the dynamic viscoelasticity and textural characteristics of cookies dough, and on cookies qualities were revealed. With the increase in the fatty acid chain length, the θo and θw values of four Tp-esters increased, the firmness of dried products with smaller oil droplets got larger, and the gel intensity of oleogels increased, but the quality scores, spread ratio, and break strength of the cookies did not change significantly. With the increase in the replacement levels of butter with oleogels, the harder cookie dough with weaker gel strength and the softer cookies with lower hedonic scores and crispness were found. At 25% and 50% replacement levels, cookies prepared with oleogels using Tp-palmitate or Tp-stearate particles exhibited similar hedonic scores, break strength, spread ratio, and storage stabilities to that of butter cookies. PRACTICAL APPLICATION: Cookies are relished by all age groups due to their taste and crispness, but include high content of saturated fatty acids that are harmful to people's health. The result of this study will help the industry to better design cookies through oleogels with tea polyphenols ester and pectin, and will provide healthy cookies with little or no butter for consumers.

Secretion of Bacillus amyloliquefaciens γ-Glutamyltranspeptidase from Bacillus subtilis and Its Application in Enzymatic Synthesis of l-Theanine.

In this study, the gene of γ-glutamyltranspeptidase (GGT) from Bacillus amyloliquefaciens (BaGGT) controlled by the Plac promoter was cloned into Bacillus subtilis to construct two recombinant vectors with either one or two signal peptides to drive extracellular secretion. After optimization, 90 ± 0.2 mg/L BaGGT was obtained when the inducing conditions were 24 h and 80 µM (IPTG). The properties of BaGGT were measured, showing that the optimal reaction conditions were 40 °C and pH 9.0 with 55.0 ± 0.5 U/mg enzymatic activity. Km and Vmax were 0.214 mM and 88.13 µmol/min/mg. BaGGT could be stored for 72 h with 90% of the initial activity at 40 °C and retained more than 50% of the initial activity after being maintained at different pH values for 24 h. Finally, enzymatic synthesis of l-theanine was performed with the optimal conditions: 20 mM l-Gln, 100 mM ethylamine HCl, 0.5 U/mL BaGGT, incubated at 40 °C for 6 h, 200 rpm.