Ethyl acetate (EA) is a popular solvent and diluent in many products and one of the most ubiquitous organic pollutants of indoor air. Although EA’s ascertained toxicity is classified as low, exposure to its vapors at concentrations ⩾400 ppm causes serious problems in humans. EA is thus a frequent target in testing novel technologies for air purification. We report here an investigation of EA oxidative degradation in air at room temperature and atmospheric pressure induced by corona discharges. Three corona regimes, dc−, dc+ and pulsed +, were tested in the same reactor under various experimental conditions with regard to EA initial concentration ( C ₀ ) and the presence of humidity in the system. The EA degradation process was monitored by gas chromatography (GC)–flame ionization detection, GC–mass spectrometry and Fourier transform infrared spectroscopy analysis of the treated gas. These analyses yielded the concentration of residual EA (C) and those of its major products of oxidation (CO ₂ , CO) and revealed a few organic reaction intermediates formed along the oxidation chain. The process energy efficiency was determined as energy constant, k _E (kJ ⁻¹ l) and as energy yield, EY (g kW ⁻¹ h ⁻¹ ). The efficiency depends on the type of corona (pulsed + >dc− >dc+), on the presence of humidity in the air (improvement in the case of dc−, little or no effect for dc+) and on C ₀ ( k _E increases linearly with 1/ C ₀ ). CO ₂ and CO were the major carbon containing products, confirming the strong oxidizing power of air non-thermal plasma. Acetic acid and acetaldehyde were detected in very small amounts as reaction intermediates. The experimental results obtained in this work support the conclusion that different reactive species are involved in the initial step of EA oxidation in the case of dc− and dc+ corona air non-thermal plasma.

Lactopontin (LPN) is a bioactive milk protein of increasing interest for nutritional applications. While traditionally sourced from bovine milk, precision fermentation now provides an alternative means of producing recombinant human lactopontin (rhLPN). This study compared the gastrointestinal digestion and intestinal interaction characteristics of rhLPN and commercially available bmLPN within a representative nutritional matrix using complementary in vitro gastrointestinal models. Protein digestion was initially characterised using the INFOGEST static digestion protocol, followed by evaluation in the MuCo-Absorb+ model, which combines simulated gastrointestinal digestion with a mucus-covered differentiated Caco-2 epithelial interface to assess post-digestive epithelial interaction and transepithelial transport. Digestion products were characterised by Western blotting, SDS-PAGE, size-exclusion HPLC and LC-MS/MS, while epithelial compatibility was assessed by transepithelial electrical resistance (TEER) and cell viability. Within both models, rhLPN and bmLPN exhibited highly comparable digestion behaviour and peptide molecular weight distributions across all concentrations and manufacturing scales evaluated. Differences in peptide molecular weight distributions were observed between the INFOGEST and MuCo-Absorb+ models, demonstrating that digestion model configuration had a greater influence on digestion outcome than protein source, concentration or manufacturing scale. No intact lactopontin was detected in the basolateral compartment by Western blotting, RP-HPLC or LC-MS/MS. However, low-molecular-weight peptides derived from the nutritional matrix were detected following transepithelial transport. This pattern is consistent with loss of the intact integrin-binding region during intestinal digestion. Digestion products from both protein sources maintained epithelial barrier integrity and cell viability throughout the transport experiment. Collectively, these findings demonstrate that precision-fermented rhLPN undergoes gastrointestinal processing and intestinal interaction comparable to commercially available bmLPN, supporting its application as an alternative source of dietary lactopontin while highlighting the importance of model selection when evaluating the digestive fate of bioactive food proteins.