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<p>Despite its relative heat resistance than globular proteins, casein is susceptible to irreversible aggregation and sedimentation under the extreme thermal conditions of retorting, which remains a technological challenge for shelf-stable, protein-enriched beverage formulations. This study aims to enhance the stability of casein-based dispersions under retort sterilization conditions by developing an integrated strategy combining cold atmospheric plasma (CAP) and putative dextrin conjugation. Response surface methodology (RSM) with Box–Behnken design optimized plasma processing parameters (10–30&#xa0;min, 30–90&#xa0;°C, 8–16&#xa0;kV) using changes in solubility and viscosity before and after thermal sterilization (121&#xa0;°C, 15&#xa0;min) as response variables. At the same time, the effects of dextrin conjugation (dextrose equivalent 5–10) on grafting behavior and physicochemical properties were evaluated. Structural–functional relationships were characterized by particle size distribution, zeta potential, Fourier transform infrared spectroscopy (FTIR), and differential scanning calorimetry (DSC), and principal component analysis (PCA) was used to elucidate structure–function relationships. According to the results, plasma treatment reduced particle size and zeta potential while increasing size heterogeneity, indicating disruption and reassembly of casein aggregates as suggested by FTIR-revealed conformational changes in casein structure. Dextrin conjugation improved thermal stability, with higher dry-state thermal transition temperatures (Td = 126–128&#xa0;°C), whereas plasma treatment alone increased Td in the dry state to ≈147&#xa0;°C. Under optimized conditions (30&#xa0;min, 66&#xa0;°C, 8&#xa0;kV), the combined treatment improved retention of solubility and viscosity after sterilization, indicating improved process stability during thermal sterilization. Findings provide proof-of-concept for a combined CAP-glycation bioprocessing strategy to enhance the thermal stability of casein-based systems under simulated retort sterilization conditions, with potential future applications in thermally processed, protein-enriched food systems pending scale-up validation.</p> Graphical Abstract <p></p>

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Combined Cold Atmospheric Plasma-Dextrin Conjugation to Improve Thermal Stability of Casein Dispersions

  • 期刊论文

  • 发表日期：

    2026年7月31日

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  • Kuo-Ching Jan,
  • Chun-Hsiang Chiu,
  • Mohsen Gavahian

摘要

Despite its relative heat resistance than globular proteins, casein is susceptible to irreversible aggregation and sedimentation under the extreme thermal conditions of retorting, which remains a technological challenge for shelf-stable, protein-enriched beverage formulations. This study aims to enhance the stability of casein-based dispersions under retort sterilization conditions by developing an integrated strategy combining cold atmospheric plasma (CAP) and putative dextrin conjugation. Response surface methodology (RSM) with Box–Behnken design optimized plasma processing parameters (10–30 min, 30–90 °C, 8–16 kV) using changes in solubility and viscosity before and after thermal sterilization (121 °C, 15 min) as response variables. At the same time, the effects of dextrin conjugation (dextrose equivalent 5–10) on grafting behavior and physicochemical properties were evaluated. Structural–functional relationships were characterized by particle size distribution, zeta potential, Fourier transform infrared spectroscopy (FTIR), and differential scanning calorimetry (DSC), and principal component analysis (PCA) was used to elucidate structure–function relationships. According to the results, plasma treatment reduced particle size and zeta potential while increasing size heterogeneity, indicating disruption and reassembly of casein aggregates as suggested by FTIR-revealed conformational changes in casein structure. Dextrin conjugation improved thermal stability, with higher dry-state thermal transition temperatures (Td = 126–128 °C), whereas plasma treatment alone increased Td in the dry state to ≈147 °C. Under optimized conditions (30 min, 66 °C, 8 kV), the combined treatment improved retention of solubility and viscosity after sterilization, indicating improved process stability during thermal sterilization. Findings provide proof-of-concept for a combined CAP-glycation bioprocessing strategy to enhance the thermal stability of casein-based systems under simulated retort sterilization conditions, with potential future applications in thermally processed, protein-enriched food systems pending scale-up validation.

Graphical Abstract