Cysteine Mediated Formation of N-ε -Carboxymethyllysine (CML) on Proteins
The reaction of glyoxal with nucleophilic amino acids was monitored for β-casein as well as β-lactoglobulin. As predicted from previous experiments with hippuryl amino acids, a measurable decrease of arginine can be found in the thiol-free β-casein, while the lysine content remained almost unchanged...
| Main Authors: | , |
|---|---|
| Format: | Article |
| Language: | English |
| Published: |
Czech Academy of Agricultural Sciences
2009-06-01
|
| Series: | Czech Journal of Food Sciences |
| Subjects: | |
| Online Access: | https://cjfs.agriculturejournals.cz/artkey/cjf-200910-0021_cysteine-mediated-formation-of-n-epsilon-carboxymethyllysine-cml-on-proteins.php |
| _version_ | 1797899806392188928 |
|---|---|
| author | U. Schwarzenbolz T. Henle |
| author_facet | U. Schwarzenbolz T. Henle |
| author_sort | U. Schwarzenbolz |
| collection | DOAJ |
| description | The reaction of glyoxal with nucleophilic amino acids was monitored for β-casein as well as β-lactoglobulin. As predicted from previous experiments with hippuryl amino acids, a measurable decrease of arginine can be found in the thiol-free β-casein, while the lysine content remained almost unchanged. For β-lactoglobulin, the incubation with glyoxal led to a slight decrease in the lysine content, while the arginine residues remained unmodified. Here, in accordance with nucleophilicity, it is suggested, that mainly cystein residues react with glyoxal. In solutions containing β-casein with or without glutathione, the effects were less pronounced and regarding the lysine and arginine content, the influence of thiols could hardly be recorded on a significant level. However, comparing the CML levels in the different incubations, it becomes obvious, that glutathione is favouring CML formation in a concentration depended manner. Therefore, the use of CML as an indicator, e.g. for the Maillard reaction, must be related to the composition of the reaction system. |
| first_indexed | 2024-04-10T08:34:45Z |
| format | Article |
| id | doaj.art-52cf82ce1e9b489f97de3a68ae1c4230 |
| institution | Directory Open Access Journal |
| issn | 1212-1800 1805-9317 |
| language | English |
| last_indexed | 2024-04-10T08:34:45Z |
| publishDate | 2009-06-01 |
| publisher | Czech Academy of Agricultural Sciences |
| record_format | Article |
| series | Czech Journal of Food Sciences |
| spelling | doaj.art-52cf82ce1e9b489f97de3a68ae1c42302023-02-23T03:27:31ZengCzech Academy of Agricultural SciencesCzech Journal of Food Sciences1212-18001805-93172009-06-0127Special Issue 1S156S15910.17221/1106-CJFScjf-200910-0021Cysteine Mediated Formation of N-ε -Carboxymethyllysine (CML) on ProteinsU. SchwarzenbolzT. Henle0Institute of Food Chemistry, Technische Universität Dresden, D-01062 Dresden, Germany *E-mail: uwe.schwarzenbolz@chemie.tu-dresden.deThe reaction of glyoxal with nucleophilic amino acids was monitored for β-casein as well as β-lactoglobulin. As predicted from previous experiments with hippuryl amino acids, a measurable decrease of arginine can be found in the thiol-free β-casein, while the lysine content remained almost unchanged. For β-lactoglobulin, the incubation with glyoxal led to a slight decrease in the lysine content, while the arginine residues remained unmodified. Here, in accordance with nucleophilicity, it is suggested, that mainly cystein residues react with glyoxal. In solutions containing β-casein with or without glutathione, the effects were less pronounced and regarding the lysine and arginine content, the influence of thiols could hardly be recorded on a significant level. However, comparing the CML levels in the different incubations, it becomes obvious, that glutathione is favouring CML formation in a concentration depended manner. Therefore, the use of CML as an indicator, e.g. for the Maillard reaction, must be related to the composition of the reaction system.https://cjfs.agriculturejournals.cz/artkey/cjf-200910-0021_cysteine-mediated-formation-of-n-epsilon-carboxymethyllysine-cml-on-proteins.phpn-ε-carboxymethyllysinecmlcysteineprotein modifications |
| spellingShingle | U. Schwarzenbolz T. Henle Cysteine Mediated Formation of N-ε -Carboxymethyllysine (CML) on Proteins Czech Journal of Food Sciences n-ε -carboxymethyllysine cml cysteine protein modifications |
| title | Cysteine Mediated Formation of N-ε -Carboxymethyllysine (CML) on Proteins |
| title_full | Cysteine Mediated Formation of N-ε -Carboxymethyllysine (CML) on Proteins |
| title_fullStr | Cysteine Mediated Formation of N-ε -Carboxymethyllysine (CML) on Proteins |
| title_full_unstemmed | Cysteine Mediated Formation of N-ε -Carboxymethyllysine (CML) on Proteins |
| title_short | Cysteine Mediated Formation of N-ε -Carboxymethyllysine (CML) on Proteins |
| title_sort | cysteine mediated formation of n ε carboxymethyllysine cml on proteins |
| topic | n-ε -carboxymethyllysine cml cysteine protein modifications |
| url | https://cjfs.agriculturejournals.cz/artkey/cjf-200910-0021_cysteine-mediated-formation-of-n-epsilon-carboxymethyllysine-cml-on-proteins.php |
| work_keys_str_mv | AT uschwarzenbolz cysteinemediatedformationofnecarboxymethyllysinecmlonproteins AT thenle cysteinemediatedformationofnecarboxymethyllysinecmlonproteins |