From lemon peels to bioactive peptides: protein recovery by pressurized liquid extraction and hydrolysates characterization by UHPLC-ESI-QTOF-MS/MS
This study aimed to develop a sustainable and efficient method for protein recovery from lemon peels using Pressurized Liquid Extraction (PLE), optimized through experimental design and response surface methodology. The final protocol, employing 18 % (v/v) ethanol, 110 ◦C, and a 7-min extraction tim...
| Autores: | , , , |
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| Tipo de recurso: | artículo |
| Fecha de publicación: | 2025 |
| País: | España |
| Institución: | Universidad Complutense de Madrid (UCM) |
| Repositorio: | Docta Complutense |
| Idioma: | inglés |
| OAI Identifier: | oai:docta.ucm.es:20.500.14352/126351 |
| Acceso en línea: | https://hdl.handle.net/20.500.14352/126351 |
| Access Level: | acceso abierto |
| Palabra clave: | 543 Lemon peels Pressurized liquid extraction Proteins Peptides Bioactivity Mass spectrometry Química analítica (Química) 2301 Química Analítica 2301.03 Análisis Cromatográfico 2301.10 Espectroscopia de Masas |
| Sumario: | This study aimed to develop a sustainable and efficient method for protein recovery from lemon peels using Pressurized Liquid Extraction (PLE), optimized through experimental design and response surface methodology. The final protocol, employing 18 % (v/v) ethanol, 110 ◦C, and a 7-min extraction time, demonstrated high extraction efficiency (66 %) and environmental compatibility, achieving a greenness score of 0.59 (AGREEprep). The optimized protein extract was subsequently hydrolyzed using alcalase and thermolysin, and the resulting peptide fractions were characterized by spectrophotometric methods and by Ultra High-Performance Liquid Chromatography coupled to Electrospray Ionization Quadrupole Time-of-Flight Mass Spectrometry (UHPLC-ESIQTOF-MS/MS). A total of 58 peptides were identified, 39 of which originated from lemon proteins, along with 19 polyphenols, such as vicenin-2, narirutin or subaphylin, and other compounds (e.g., organic acids, amino acids, and purine nucleosides), revealing a diverse and multifunctional bioactive profile. Bioactivity assays demonstrated that the thermolysin hydrolysate exhibited the highest antioxidant (97 ± 1 % inhibition of hydroxyl radicals), antimicrobial (MIC = 0.75 mg/mL against Staphylococcus aureus), and antihypertensive activities (49 ± 3 % angiotensin-converting enzyme inhibition), likely due to the presence of peptides enriched in aromatic amino acids such as phenylalanine and tyrosine. |
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