Tailoring the Adsorption of ACE-Inhibiting Peptides by Nitrogen Functionalization of Porous Carbons
Research output: Contribution to journal › Research article › Contributed › peer-review
Contributors
Abstract
Bioactive peptides, such as isoleucyl-tryptophan (IW), exhibit a high potential to inhibit the angiotensin-converting enzyme (ACE). Adsorption on carbon materials provides a beneficial method to extract these specific molecules from the complex mixture of an alpha-lactalbumin hydrolysate. This study focuses on the impact of nitrogen functionalization of porous carbon adsorbents, either via pre- or post-treatment, on the adsorption behavior of the ACE-inhibiting peptide IW and the essential amino acid tryptophan (W). The commercially activated carbon Norit ROX 0.8 is compared with pre- and postsynthetically functionalized N-doped carbon in terms of surface area, pore size, and surface functionality. For prefunctionalization, a covalent triazine framework was synthesized by trimerization of an aromatic nitrile under ionothermal conditions. For the postsynthetic approach, the activated carbon ROX 0.8 was functionalized with the nitrogen-rich molecule melamine. The batch adsorption results using model mixtures containing the single components IW and W could be transferred to a more complex mixture of an alpha-lactalbumin hydrolysate containing a huge number of various peptides. For this purpose, reverse-phase high-pressure liquid chromatography with fluorescence detection was used for identification and quantification. The treatment with the three different carbon materials leads to an increase in the ACE-inhibiting effect in vitro. The modified surface structure of the carbon via pre- or post-treatment allows separation of IW and W due to the certain selectivity for either the amino acid or the dipeptide.
Details
Original language | English |
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Pages (from-to) | 9721-9731 |
Number of pages | 11 |
Journal | Langmuir |
Volume | 35 |
Issue number | 30 |
Publication status | Published - 30 Jul 2019 |
Peer-reviewed | Yes |
External IDs
Scopus | 85070694764 |
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Keywords
Keywords
- ANGIOTENSIN-CONVERTING ENZYME, TRYPTOPHAN-CONTAINING DIPEPTIDES, BIOACTIVE PEPTIDES, ACTIVATED CARBON, FOOD PROTEINS, MILK, HYPERTENSION, HYDROLYSATE, EXTRACTION, REMOVAL