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- W2629128516 abstract "Lipoaminoacids, as surfactants, are an excellent option for food industry due to the currently trends in consumption of functional and natural ingredients. Synthesis of lauroyl glycine lipoaminoacid was carried out with a lipase from Pseudomonas stutzeri and a protease from Bacillus subtilis, which were immobilized in octyl-glyoxyl silica and glyoxyl-silica supports, respectively, comparing their catalytic performance. The enzymatic selectivity towards the lipoaminoacid instead of the dipeptide glycylglycine and synthesis yield were evaluated with respect to the characteristics of the immobilized biocatalysts and synthesis conditions. Three solvents were tested as reaction media for evaluating the expressed activity, stability and catalytic behavior during synthesis. Results indicate that both enzymes favor the lauroyl glycine synthesis over the peptide synthesis, but the immobilized protease has the best balance between selectivity and yield: 40% yield for lauroyl glycine and less than 5% for dipeptide after 96 h of synthesis, at 45 °C and acetone as solvent." @default.
- W2629128516 created "2017-06-30" @default.
- W2629128516 creator A5020917721 @default.
- W2629128516 creator A5027496487 @default.
- W2629128516 creator A5053588576 @default.
- W2629128516 creator A5083622532 @default.
- W2629128516 date "2018-01-01" @default.
- W2629128516 modified "2023-10-10" @default.
- W2629128516 title "Selective and eco-friendly synthesis of lipoaminoacid-based surfactants for food, using immobilized lipase and protease biocatalysts" @default.
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- W2629128516 doi "https://doi.org/10.1016/j.foodchem.2017.06.105" @default.
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