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@ARTICLE{Romano:602185,
      author       = {Romano, Alon and Engelberg, Yizhaq and Landau, Meytal and
                      Lesmes, Uri},
      title        = {{A}lpha-lactalbumin amyloid-like fibrils for intestinal
                      delivery: {F}ormation, physiochemical characterization, and
                      digestive fate of capsaicin-loaded fibrils},
      journal      = {Food hydrocolloids},
      volume       = {136},
      issn         = {0268-005X},
      address      = {Amsterdam},
      publisher    = {Elsevier},
      reportid     = {PUBDB-2024-00511},
      pages        = {108248},
      year         = {2023},
      abstract     = {Engineering protein architectures offers numerous
                      opportunities to deliver consumers with added values yet
                      mandates careful screening of possible risks. This study
                      explores the fabrication of bovine alpha-lactalbumin (ALA)
                      amyloid-like fibrils (AF) for gastro-intestinal delivery of
                      capsaicin (CAP), a pungent compound which possesses health
                      beneficial virtues. Acidic incubation of ALA with CAP
                      accelerates formation of ALA-AF, as confirmed by
                      transmission electron microscope, with a size increase from
                      3.7 ± 0.4 nm to 175 ± 58 nm and a melting temperature
                      shift from T$_m$ = 61.8 °C to T$_m$ = 89.9 °C for native
                      ALA and ALA-AF entrapping 200 μM CAP, respectively. In
                      addition to encapsulation efficiency and loading capacity
                      measurements, this work provides evidence that fibrillation
                      attenuates the in vitro digestive proteolysis of ALA and
                      diminishes the levels of bioaccessible bioactive peptides by
                      an order of magnitude compared to native ALA. This is
                      accompanied by sustained release of 7.8 ± 1.7\% to 55.7 ±
                      12.3\% CAP under gastric and intestinal conditions. Overall,
                      this work presents a new possible avenue for designing
                      protein structures to entrap bioactive moieties along-side a
                      call to interrogate the possible ramifications to protein
                      digestion and consumer health.},
      cin          = {CSSB-F},
      ddc          = {640},
      cid          = {I:(DE-H253)CSSB-F-20230420},
      pnm          = {633 - Life Sciences – Building Blocks of Life: Structure
                      and Function (POF4-633)},
      pid          = {G:(DE-HGF)POF4-633},
      experiment   = {EXP:(DE-MLZ)NOSPEC-20140101},
      typ          = {PUB:(DE-HGF)16},
      UT           = {WOS:001017491100001},
      doi          = {10.1016/j.foodhyd.2022.108248},
      url          = {https://bib-pubdb1.desy.de/record/602185},
}