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@ARTICLE{Saha:1046472,
      author       = {Saha, Debasish and Kumar, Sugam and Dubey, Purushottam S.
                      and Mata, Jitendra P. and Whitten, Andrew E. and
                      Kohlbrecher, Joachim and Frielinghaus, Henrich and Aswal,
                      Vinod K.},
      title        = {{C}ontrolling the {C}old-{S}et {G}elation of {B}ovine
                      {S}erum {A}lbumin {P}rotein using {A}lcohol and {I}onic
                      {S}urfactant},
      journal      = {Food hydrocolloids},
      volume       = {172},
      issn         = {0268-005X},
      address      = {Amsterdam},
      publisher    = {Elsevier},
      reportid     = {FZJ-2025-03824},
      pages        = {111991},
      year         = {2026},
      abstract     = {Heating of globular protein solutions usually leads to
                      protein denaturation and subsequent gelation at high
                      temperatures. Under “cold gelation”, protein forms a gel
                      at a much lower temperature than its original gelation
                      temperature (TG), which can be achieved by modifying various
                      physicochemical conditions such as the pH of the solution,
                      the presence of salts, etc. In this study, we investigated
                      the cold gelation of Bovine Serum Albumin (BSA) protein
                      induced by ethanol and controlled by ionic surfactant, using
                      small-angle neutron scattering (SANS), dynamic light
                      scattering (DLS), and rheology The results show that the TG
                      of the protein with ethanol is systematically decreased as
                      compared to the that of pure BSA solutions (~80 ◦C),
                      reaching ~60 ◦C at 10 $wt\%$ ethanol, ~55 ◦C at 20
                      $wt\%$ and finally as low as ~38 ◦C in presence of 30
                      $wt\%$ ethanol in the solution. Rheo-logical measurements
                      demonstrate a significant strengthening of the gel network,
                      with the enhancement in storage modulus (G′) from ~20 Pa
                      at 0 $wt\%$ to ~250 Pa at 30 $wt\%$ ethanol. Structural
                      characterization reveals an increase in fractal dimension
                      with rising ethanol content, indicating denser and more
                      branched gel networks. Interestingly, the addition of the
                      anionic surfactant sodium dodecyl sulfate (SDS) inhibits the
                      alcohol-assisted cold gelation of BSA protein, depending
                      upon the relative amount of ethanol and SDS in solution. The
                      results are explained based on the interplay of interactions
                      in the protein, manipulated by the presence of alcohol,
                      elevated temperatures, and ionic surfactant. Our study
                      highlights the tunability of gelation pathways and offers
                      useful inputs for controlled protein gelation in biomaterial
                      and food industry.},
      cin          = {JCNS-FRM-II / MLZ / JCNS-4},
      ddc          = {640},
      cid          = {I:(DE-Juel1)JCNS-FRM-II-20110218 / I:(DE-588b)4597118-3 /
                      I:(DE-Juel1)JCNS-4-20201012},
      pnm          = {6G4 - Jülich Centre for Neutron Research (JCNS) (FZJ)
                      (POF4-6G4) / 632 - Materials – Quantum, Complex and
                      Functional Materials (POF4-632)},
      pid          = {G:(DE-HGF)POF4-6G4 / G:(DE-HGF)POF4-632},
      experiment   = {EXP:(DE-MLZ)NOSPEC-20140101},
      typ          = {PUB:(DE-HGF)16},
      doi          = {10.1016/j.foodhyd.2025.111991},
      url          = {https://juser.fz-juelich.de/record/1046472},
}