Improving resistant starch content of cassava starch by pulsed electric field-assisted esterification.

This study aims to investigate the effect of pulsed electric field (PEF) assisted OSA esterification treatment on the multi-scale structure and digestive properties of cassava starch and structure-digestion relationships. The degree of substitution (DS) of starch dually modified at 1.5-4.5 kV/cm was 37.6-55.3 % higher than that of starch modified by the conventional method. Compared with native starch, the resistant starch (RS) content of esterified starch treated with 3 kV/cm significantly increased by 17.13 %, whereas that of starch produced by the conventional method increased by only 5.91 %. Furthermore, assisted esterification at low electric fields (1.5-3 kV/cm) promotes ester carbonyl grafting on the surface of starch granules, increases steric hindrance and promotes the rearrangement of the amorphous regions of starch, which increases the density of the double-helical structure. These structural changes slow down starch digestion and increase the RS content. Therefore, this study presents a potential method for increasing the RS content of starch products using PEF to achieve the desired digestibility.

Adenosine monophosphate boosts the cryoprotection of ultrasound-assisted freezing to frozen surimi: Insights into protein structures and gelling behaviors.

Ultrasound-assisted freezing (UAF) is a clean technique for meat cryoprotections; however, its effectiveness is still limited compared to conventional cryoprotectants, e.g., sugars, polyols, especially at high dosages. To resolve this problem, a synergistic cryoprotection strategy was developed in this study. Adenosine monophosphate (AMP), an adenosine-type food additive, was introduced into frozen surimi at a considerably reduced content (0.08%), yet substantially enhanced the efficiency of UAF to comparable levels of commercial cryoprotectant (4% sucrose with 4% sorbitol). Specifically, UAF/AMP treatment retarded denaturation of surimi myofibrillar protein (MP) during 60-day frozen storage, as evidenced by its increased solubility, Ca2+-ATPase activity, sulfhydryl content, declined surface hydrophobicity, particle size, and stabilized protein conformation. Gels of UAF/AMP-treated surimi also demonstrated more stabilized microstructures, uniform water distributions, enhanced mechanical properties and water-holding capacities. This study provided a feasible approach to boost the cryoprotective performance of UAF, thus expanding its potential applications in frozen food industry.

Inducing the structural interplay of binary pulse protein complex to stimulate the solubilization of chickpea (Cicer arietinum L.) protein isolate.

Chickpea protein (CP) is an exceptional nutrient-dense pulse protein prevailing in the development of plant-based foods. However, its relatively low solubility, compared to other legume proteins, hinders the practical uses of CP in food matrix. To resolve this problem, pea protein (PP), another popular pulse protein, was co-assembled with CP to form a binary complex during the alkaline pH-shifting process. Results indicated that the complexed CP exhibited significantly increased solubility to that of the pristine protein (more than 50%), whose aqueous stability was also enhanced against different environmental stresses (pH, salt, heat/frozen treatment, and centrifugation). Structural and morphology analysis confirmed the interplay between unfolded CP and PP during pH shifting, which enabled their resistance to acid-induced structural over-folding. Our experiments that induce the co-assembling of two pulse proteins provide a novel routine and scientific basis for tailoring CP functionalities, as well as the formulation of pulse protein-based products.

Pulse Protein Isolates as Competitive Food Ingredients: Origin, Composition, Functionalities, and the State-of-the-Art Manufacturing.

The ever-increasing world population and environmental stress are leading to surging demand for nutrient-rich food products with cleaner labeling and improved sustainability. Plant proteins, accordingly, are gaining enormous popularity compared with counterpart animal proteins in the food industry. While conventional plant protein sources, such as wheat and soy, cause concerns about their allergenicity, peas, beans, chickpeas, lentils, and other pulses are becoming important staples owing to their agronomic and nutritional benefits. However, the utilization of pulse proteins is still limited due to unclear pulse protein characteristics and the challenges of characterizing them from extensively diverse varieties within pulse crops. To address these challenges, the origins and compositions of pulse crops were first introduced, while an overarching description of pulse protein physiochemical properties, e.g., interfacial properties, aggregation behavior, solubility, etc., are presented. For further enhanced functionalities, appropriate modifications (including chemical, physical, and enzymatic treatment) are necessary. Among them, non-covalent complexation and enzymatic strategies are especially preferable during the value-added processing of clean-label pulse proteins for specific focus. This comprehensive review aims to provide an in-depth understanding of the interrelationships between the composition, structure, functional characteristics, and advanced modification strategies of pulse proteins, which is a pillar of high-performance pulse protein in future food manufacturing.

Pulsed electric field-assisted esterification improves the freeze-thaw stability of corn starch gel by changing its molecular structure.

The influence of pulsed electric field (PEF) combined with octenyl succinic anhydride (OSA) on the freeze-thaw stability of corn starch gel was investigated. After five freeze-thaw cycles, the syneresis value of OSA starch treated with PEF-assisted esterification for 15 min was lower by 29.5 %, while that of OSA starch without PEF treatment was lower by 10.17 %, compared to that of native starch. Low-field nuclear magnetic resonance data showed that the introduction of OSA groups greatly increased the water-holding capacity of starch. Results from differential scanning calorimetry (DSC) and X-ray diffraction (XRD) showed that the PEF-assisted esterification markedly hindered the re-formation of the helical structure of starch during freeze-thaw cycles. Moreover, PEF-assisted esterification improved the viscoelastic properties of the starch gel. It is found that the freeze-thaw stability of the PEF-modified starch depends not only on the degree of substitution but also on the starch molecular fine structure. PEF-assisted OSA starch with a high degree of substitution, a low content of amylose, and a high content of short amylopectin chains were found to have high freeze-thaw stability. This study shows that PEF-assisted esterification is a promising technique that should be used for preserving the quality of frozen foods.

Enhanced encapsulation of lutein using soy protein isolate nanoparticles prepared by pulsed electric field and pH shifting treatment.

In this study, soy protein isolate (SPI) was modified by a pulsed electric field (PEF) combined with pH shifting treatment (10 kV/cm, pH 11) to prepare SPI nanoparticles (PSPI11) for efficient loading of lutein. The results showed that when the mass ratio of SPI to lutein was 25:1, the encapsulation efficiency of lutein in PSPI11 increased from 54% to 77%, and the loading capacity increased by 41% compared to the original SPI. The formed SPI-lutein composite nanoparticles (PSPI11-LUTNPs) had smaller, more homogeneous sizes and larger negative charges than SPI7-LUTNPs. The combined treatment favored the unfolding of the SPI structure and could expose its interior hydrophobic groups to bind with lutein. Nanocomplexation with SPIs significantly improved the solubility and stability of lutein, with PSPI11 showing the greatest improvement. As a result, PEF combined with pH shifting pretreatment is an effective method for developing SPI nanoparticles loaded and protected with lutein.

Pulsed electric field improves the EGCG binding ability of pea protein isolate unraveled by multi-spectroscopy and computer simulation.

Understanding molecular mechanisms during protein modification is critical for expanding the application of plant proteins. This study investigated the conformational change and molecular mechanism of pea protein isolate (PPI) under pulsed electric field (PEF)-assisted (-)-Epigallocatechin-Gallate (EGCG) modification. The flexibility of PPI was significantly enhanced after PEF treatment (10 kV/cm) with decrease (23.25 %) in α-helix and increase (117.25 %) in random coil. The binding constant and sites of PEF-treated PPI with EGCG were increased by 2.35 times and 10.00 % (308 K), respectively. Molecular docking verified that PEF-treated PPI had more binding sites with EGCG (from 4 to 10). The number of amino acid residues involved in hydrophobic interactions in PEF-treated PPI-EGCG increased from 5 to 13. PEF-treated PPI-EGCG showed a significantly increased antioxidant activity compared to non-PEF-treated group. This work revealed the molecular level of PEF-assisted EGCG modification of PPI, which will be significant for the application of PPI in food industry.

Development of multi-layered gastric floating tablets based on konjac glucomannan: a modified calcium supplement with enhanced bioavailability.

This study developed a gastric-floating delivery system of calcium based on konjac glucomannan (KGM). The developed calcium tablets, consisting of one core layer coated with two barrier layers, were fabricated with a facile method. The role of KGM within the tablets was evaluated from characteristics including swelling behavior, hydrated gel properties, floating ability and release profiles of calcium (Ca). The results indicated that upregulating the KGM fraction accelerated the formation of a more compact gel network in gastric conditions, which prolonged both the floating lag time and floating duration, which resulted in a more sustained swelling behavior and a slower release of calcium. Among all the formulations, a core tablet containing 20% KGM (K20) was selected as the optimized one as it could quickly float up in 7.21 s, exhibited an almost linear release and obtained a release amount of 87.73% within 12 h. Finally, a comparison of in vivo calcium bioavailability between a KGM-based calcium tablet and a commercial calcium tablet (Caltrate®) was carried out by monitoring the serum calcium concentration after administration in rabbits. The results suggested that, after having the KGM-based calcium tablet, the changes of serum calcium levels were gentler due to a sustained-release property. The difference integral value between profile K20 and the baseline was 1.4358, larger than that of Caltrate® (1.1808), suggesting the higher absorption efficiency of KGM-based calcium tablets.