Gelation behavior and mechanism of low methoxyl pectin in the presence of erythritol and sucrose: The role of co-solutes.

Co-solutes such as sucrose and sugar alcohol play a significant part in low methoxyl pectin (LMP) gelation. To explore their gelation mechanism, we investigated the gelation behavior of LMP in the presence of erythritol and sucrose with Ca. Results revealed that the introduction of erythritol and sucrose improved the hardness of the gels, fixed more free water, accelerated the rate of gel structuring, and enhanced the gel strength.

Effect of enzymatic de-esterification and RG-I degradation of high methoxyl pectin (HMP) on sugar-acid gel properties.

The influence of RG-I domains on high methoxyl pectin (HMP) sugar-acid gel properties has rarely been reported. In our work, HMP was modified by enzymatic de-esterification and degradation of RG-I domains to compare and analyze the relationship between the structure and final sugar-acid gel properties. The results showed that the degree of esterification (DE) of REP (pectin degraded by rhamnosidase) and GEP (pectin debranched by galactosidase) was the same as that of untreated HMP, whereas the DE of PMEP (pectin de-esterified by pectin methyl esterase) decreased from 59.

Pectin gels based on H/(NH)SO and its potential in sustained release of NH.

A gelling strategy for HP was proposed in this study, ammonium sulfate (AS) as a co-solute could induce the gelling of HP in acidic environment. The solubility and Zeta potential of HP dramatically decreased in AS solution, which indicated AS could promote the aggregation of HP. The rheological results confirmed the gelling of HP (G' > G″) with AS: 25-30 wt% and pH ≤ 3.

Physicochemical characteristics and functional properties of high methoxyl pectin with different degree of esterification.

Moderate alkali de-esterification can change the physicochemical characteristics and thus the functional properties of high methoxyl pectin (HMP). The results revealed that de-esterification could increase negative charges (Zeta potential from -21 to -31 mV), decrease molecular weight (from 448 to 136 kDa) and apparent viscosity of HMP. Homogalacturonan (HG) content decreased (from 62% to 49%) while rhamnogalacturonan Ⅰ (RG-Ⅰ) content increased (from 32% to 46%) after de-esterification.

Citrus fiber for the stabilization of O/W emulsion through combination of Pickering effect and fiber-based network.

In this study, oil-in-water emulsions stabilized by citrus fiber were prepared and characterized. We found that citrus fiber can produce stable gel-like, surfactant-free O/W emulsions with microscale droplet sizes at fiber concentrations upon 2% (W/V) using 25% (V/V) oil. The interfacial framework, citrus fiber partition between the continuous phase and state of the droplets of emulsions were visualized by confocal laser scanning microscopy (CLSM), confirming that in addition to Pickering stabilization, the citrus fiber-based network also contributed to stabilization of the emulsions.

Structural characterization of pectin-bismuth complexes and their aggregation in acidic conditions.

Bismuth-contained therapies are effective in treating gastric ulcer and eliminating Helicobacter pylori (Hp). Anion polysaccharides ligand could reduce the intake of bismuth, and enhance drug efficacy of bismuth compounds. In this study, pectin-bismuth (PB) was prepared and the changes of PB structure in acidic environment were reported for the first time.

Emulsifying properties of high methoxyl pectins in binary systems of water-ethanol.

Pectin is widely distributed in plant cell wall, most of which have limited emulsifying properties. Ethanol could alter the solubility of pectin, and affect its emulsifying properties. No creaming and breaking of emulsion appeared in 21% (v/v) ethanol contained emulsion.

Pea soluble polysaccharides obtained from two enzyme-assisted extraction methods and their application as acidified milk drinks stabilizers.

The objective of this work was characterize and evaluate the protein-stabilizing property of pea soluble polysaccharide (PSPS) extracted from pea by-products using spray-drying and ethanol precipitation oven drying, obtaining PSPS-A and PSPS-B, respectively. The weight average molecular weight (Mw) of PSPS-A and PSPS-B were 625 kDa and 809 kDa, respectively. The results of Fourier transform infrared spectroscopy (FT-IR) analysis indicated that PSPS-A, PSPS-B and soybean soluble polysaccharide (SSPS) contained the same functional groups.

The influence of heat treatment on acid-tolerant emulsions prepared from acid soluble soy protein and soy soluble polysaccharide complexes.

This research presents a green procedure to prepare oil in water (O/W) emulsion from acid soluble soy protein (ASSP) and soy soluble polysaccharide (SSPS), a long-term stable nanoscale system for delivering the lipophilic components. The emulsion technique involved the preparation complexion using ASSP and SSPS by electrostatic and hydrophobic interactions as well as high pressure homogenization. The average diameter of the droplet of emulsions (fresh and heated) is 263±2nm.

Subcritical Water Induced Complexation of Soy Protein and Rutin: Improved Interfacial Properties and Emulsion Stability.

Rutin is a common dietary flavonoid with important antioxidant and pharmacological activities. However, its application in the food industry is limited mainly because of its poor water solubility. The subcritical water (SW) treatment provides an efficient technique to solubilize and achieve the enrichment of rutin in soy protein isolate (SPI) by inducing their complexation.

Fabrication and characterization of Pickering emulsions and oil gels stabilized by highly charged zein/chitosan complex particles (ZCCPs).

Herein, we reported a facile method to fabricate ultra-stable, surfactant- and antimicrobial-free Pickering emulsions by designing and modulating emulsions' interfaces via zein/chitosan colloid particles (ZCCPs). Highly charged ZCCPs with neutral wettability were produced by a facile anti-solvent procedure. The ZCCPs were shown to be effective Pickering emulsifiers because the emulsions formed were highly resistant to coalescence over a 9-month storage period.

Fabrication and Characterization of Stable Soy β-Conglycinin-Dextran Core-Shell Nanogels Prepared via a Self-Assembly Approach at the Isoelectric Point.

The preparation of soy β-conglycinin-dextran nanogels (∼90 nm) went through two stages, which are safe, facile, and green. First, amphiphilic graft copolymers were formed by dextran covalently attaching to β-conglycinin via Maillard dry-heating reaction. Second, the synthesized conjugates were heated above the denaturation temperature at the isoelectric point (pH4.

Soy lipophilic protein nanoparticles as a novel delivery vehicle for conjugated linoleic acid.

Soy lipophilic protein nanoparticles (LPP), which present a novel delivery vehicle for conjugated linoleic acid (CLA), were fabricated by ultrasonication of the soy lipophilic protein (LP), which exhibits unique characteristics including a high loading capacity, oxidation protection and a sustained releasing profile in vitro for CLA. The CLA-loaded LPP exhibited a mean diameter of 170 ± 0.63 nm and a loading capacity of 26.

Formation of soy protein isolate-dextran conjugates by moderate Maillard reaction in macromolecular crowding conditions.

Background: Several methods have been reported for the conjugation of proteins with polysaccharides. Protein-polysaccharide conjugates can be formed by traditional dry heating, but this process is not attractive from an industrial viewpoint, and no commercial conjugates have been manufactured in this way. In the present study, in order to develop a more practical reaction method, macromolecular crowding was used to attach polysaccharides to proteins.

Adsorption and dilatational rheology of heat-treated soy protein at the oil-water interface: relationship to structural properties.

We evaluated the influence of heat treatment on interfacial properties (adsorption at the oil-water interface and dilatational rheology of interfacial layers) of soy protein isolate. The related structural properties of protein affecting these interfacial behaviors, including protein unfolding and aggregation, surface hydrophobicity, and the state of sulfhydryl group, were also investigated. The structural and interfacial properties of soy protein depended strongly on heating temperature (90 and 120 °C).

In vitro assessment of the bioaccessibility of fatty acids and tocopherol from soybean oil body emulsions stabilized with ι-carrageenan.

The present investigation aimed to expand the knowledge of the in vitro bioaccessibility of fatty acids and tocopherol from natural soybean oil body emulsions stabilized with different concentrations of ι-carrageenan. Several physicochemical parameters including proteolysis of the interfacial layer, interfacial composition, and microstructure were evaluated with regard to their impact on the bioaccessibility of fatty acids and tocopherol. Results from simulated human digestion in vitro indicated that the bioaccessibility of total fatty acids and tocopherol decreased (62.

Growth kinetics of amyloid-like fibrils derived from individual subunits of soy β-conglycinin.

The amyloid-like fibrillation of soy β-conglycinin subunits (α, α', and β) upon heating (0-20 h) at 85 °C and pH 2.0 was characterized using dynamic light scattering, circular dichroism (CD), binding to amyloid dyes (Thioflavin T and Congo red), and atomic force microscopy. The fibrillation of all three subunits was accompanied by progressive polypeptide hydrolysis.

Physicochemical and structural characterisation of protein isolate, globulin and albumin from soapnut seeds (Sapindus mukorossi Gaertn.).

The amino acid (AA) composition and physicochemical and conformational properties of protein isolate (SNPI), globulin (SNG) and albumin (SNA) fractions from soapnut seeds were evaluated. The essential AA of SNG, SNA and SNPI (except sulfur-containing AA) are sufficient for the FAO/WHO suggested requirements for 2-5year old infants. SNG and SNPI showed similar electrophoresis patterns and AA compositions, the subunit of those proteins consisted of two polypeptides linked by disulfide bonds.