7
views
0
recommends
+1 Recommend
0 collections
    0
    shares
      • Record: found
      • Abstract: not found
      • Article: not found

      Water-soluble myofibrillar protein–pectin complex for enhanced physical stability near the isoelectric point: Fabrication, rheology and thermal property

      , , , ,
      International Journal of Biological Macromolecules
      Elsevier BV

      Read this article at

      ScienceOpenPublisherPubMed
      Bookmark
          There is no author summary for this article yet. Authors can add summaries to their articles on ScienceOpen to make them more accessible to a non-specialist audience.

          Abstract

          <p class="first" id="d12825626e101">This study tested the potential of forming soluble complex with pectin (PEC) on enhancing physical stability of water-soluble myofibrillar protein (WSMP) near the isoelectric point (pI, pH 5.00-5.50). After incorporation of PEC at the mixing ratio of 10:1 and 5:1, WSMP suspension maintained transparent state at 0.05 wt% while a homogeneous monophase at 1.00 wt% around pI, indicating the formation of soluble WSMP-PEC complex. When mixing the two biopolymers, charge neutralization was observed, revealing the electrostatic attraction between positively charged patches of WSMP and negatively charged carboxyl sites of PEC. Steady shear results showed a reduced viscosity of WSMP-PEC complex when dropping the pH to 5.00, this may be related to the declined biopolymer net charge and water trapping. Oscillatory data suggest the formation of highly-interconnected network in soluble WSMP-PEC complex, thus decreasing pH or biopolymer ratio can enhance their interactions and thereby lead to stronger and more stable microstructure. Thermal denaturation temperature of WSMP was significantly enhanced through the formation of WSMP-PEC soluble complexes. Overall, complexation with PEC improved the colloidal and thermal stability of WSMP around the pI, which evidenced the potential of applying tailor designed protein-polysaccharide complex in formulating muscle protein-based beverages. </p>

          Related collections

          Author and article information

          Journal
          International Journal of Biological Macromolecules
          International Journal of Biological Macromolecules
          Elsevier BV
          01418130
          October 2019
          October 2019
          Article
          10.1016/j.ijbiomac.2019.10.003
          31622714
          22718f90-c72c-4aab-a5e1-0788929dea46
          © 2019

          https://www.elsevier.com/tdm/userlicense/1.0/

          History

          Comments

          Comment on this article