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      Potential Use of Nonanimal-Based Biopolymers as Gelling/Emulsifying Stabilizing Agents to Reduce the Fat Content in Foods: A Review

      1 , 2 , 2 , 3
      ACS Food Science & Technology
      American Chemical Society (ACS)

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          Gelation of gellan – A review

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            Pectin as a rheology modifier: Origin, structure, commercial production and rheology.

            Pectins are a diverse family of biopolymers with an anionic polysaccharide backbone of α-1,4-linked d-galacturonic acids in common. They have been widely used as emulsifiers, gelling agents, glazing agents, stabilizers, and/or thickeners in food, pharmaceutical, personal care and polymer products. Commercial pectin is classified as high methoxy pectin (HMP) with a degree of methylation (DM) >50% and low methoxy pectin (LMP) with a DM <50%. Amidated low methoxy pectins (ALMP) can be obtained through aminolysis of HMP. Gelation of HMP occurs by cross-linking through hydrogen bonds and hydrophobic forces between the methyl groups, assisted by a high co-solute concentration and low pH. In contrast, gelation of LMP occurs by the formation of ionic linkages via calcium bridges between two carboxyl groups from two different chains in close proximity, known as the 'egg-box' model. Pectin gels exhibit Newtonian behaviour at low shear rates and shear-thinning behaviour when the shear rate is increased. An overview of pectin from its origin to its physicochemical properties is presented in this review.
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              Soy protein nanoparticle aggregates as pickering stabilizers for oil-in-water emulsions.

              In recent years, there have been increasing interests in developing food-grade Pickering stabilizers, due to their potential applications in formulations of novel functional foods. The present work was to investigate the potential of soy proteins to be developed into a kind of Pickering-like stabilizer for oil-in-water emulsions. The nanoparticle aggregates of soy protein isolate (SPI) were formed by sequential treatments of heating at 95 °C for 15 min and then electrostatic screening with NaCl addition. The particle size and microstructure of these aggregates were characterized using dynamic light scattering and atomic force microscopy, indicating that the fabricated nanoparticle aggregates were ∼100 nm in size with more surface hydrophobic nature (relative to unheated SPI). The influence of particle concentration (c; 0.5-6.0%, w/w) and increasing oil fraction (ϕ; in the range 0.2-0.6) on the droplet size and coalescence and/or creaming stability of the emulsions stabilized by these nanoparticle aggregates was investigated. The results showed that, at ϕ = 0.2, increasing the c resulted in a progressive but slight decrease in droplet size, and improved the stability against coalescence and creaming; at a specific c, the creaming stability was progressively increased by increasing the ϕ, with better improvement observed at a higher c (e.g., 6.0% vs 2.0%). The improvement of creaming stability was largely associated with the formation of a gel-like network that could entrap the oil droplets within the network. The observations are generally consistent with those observed for the conventional Pickering emulsions, confirming that soy proteins could be applied as a kind of effective Pickering-like stabilizer. The finding may have important implications for the design and fabrication of protein-based emulsion formulations, and even for the development of soy protein products with some unique functions. To the authors' knowledge, this is the first work to report that heat-induced soy protein aggregates exhibit a good potential to act as Pickering-type stabilizers.
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                Author and article information

                Contributors
                (View ORCID Profile)
                Journal
                ACS Food Science & Technology
                ACS Food Sci. Technol.
                American Chemical Society (ACS)
                2692-1944
                2692-1944
                May 20 2022
                May 11 2022
                May 20 2022
                : 2
                : 5
                : 751-762
                Affiliations
                [1 ]Department of Food Science, Université Laval, Quebec, Quebec G1V 0A6, Canada
                [2 ]Institute of Nutrition and Functional Foods (INAF), Université Laval, Quebec, Quebec G1V 0A6, Canada
                [3 ]Department of Soil Sciences and Agri-Food Engineering, Université Laval, Quebec, Quebec G1V 0A6, Canada
                Article
                10.1021/acsfoodscitech.2c00031
                c3499003-709e-464c-9291-e61df5336498
                © 2022

                https://doi.org/10.15223/policy-029

                https://doi.org/10.15223/policy-037

                https://doi.org/10.15223/policy-045

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