BINDING ISOTHERMS SURFACTANT-PROTEINS
The interactions between surfactants and proteins shows some similarities with interactions between surfactants and polymers, but the hydrophobic amphoteric nature of proteins and their secondary and tertiary structure components make them different from conventional polymer systems. Many studies fr...
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| Format: | Article |
| Language: | English |
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Alma Mater Publishing House "Vasile Alecsandri" University of Bacau
2011-12-01
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| Series: | Scientific Study & Research: Chemistry & Chemical Engineering, Biotechnology, Food Industry |
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| Online Access: | http://pubs.ub.ro/dwnl.php?id=CSCC6201104V04S01A0015 |
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| author | Elena Irina Moater Cristiana Radulescu Ionica Ionita |
| author_facet | Elena Irina Moater Cristiana Radulescu Ionica Ionita |
| author_sort | Elena Irina Moater |
| collection | DOAJ |
| description | The interactions between surfactants and proteins shows some similarities with interactions between surfactants and polymers, but the hydrophobic amphoteric nature of proteins and their secondary and tertiary structure components make them different from conventional polymer systems. Many studies from the past about surfactant - proteins bonding used the dialysis techniques. Other techniques used to determine the binding isotherm, included ultrafiltration, ultracentrifugation, potentiometry, ion-selective electrode method and surface tension. High affinity isotherms which are typical of an anionic surfactant - protein bonding, exhibit an initial increase steep followed by a slow growth region and then a vertical growth above a certain concentration. This isotherm is typical of ionic surfactant to protein binding. Often the high affinity initial bond appears at very low concentrations of surfactant and therefore in some protein-surfactant systems, the exact shape of the isotherm in this region may be missing. The surfactant - protein binding is influenced by a number of variables such as the nature and chain length of surfactant, pH, ionic strength, temperature, nature of this protein and additives. |
| format | Article |
| id | doaj-art-e8b42d09f2c24c82a8b251aa10b0f7af |
| institution | DOAJ |
| issn | 1582-540X |
| language | English |
| publishDate | 2011-12-01 |
| publisher | Alma Mater Publishing House "Vasile Alecsandri" University of Bacau |
| record_format | Article |
| series | Scientific Study & Research: Chemistry & Chemical Engineering, Biotechnology, Food Industry |
| spelling | doaj-art-e8b42d09f2c24c82a8b251aa10b0f7af2025-08-20T03:09:51ZengAlma Mater Publishing House "Vasile Alecsandri" University of BacauScientific Study & Research: Chemistry & Chemical Engineering, Biotechnology, Food Industry1582-540X2011-12-01124429433BINDING ISOTHERMS SURFACTANT-PROTEINSElena Irina MoaterCristiana RadulescuIonica IonitaThe interactions between surfactants and proteins shows some similarities with interactions between surfactants and polymers, but the hydrophobic amphoteric nature of proteins and their secondary and tertiary structure components make them different from conventional polymer systems. Many studies from the past about surfactant - proteins bonding used the dialysis techniques. Other techniques used to determine the binding isotherm, included ultrafiltration, ultracentrifugation, potentiometry, ion-selective electrode method and surface tension. High affinity isotherms which are typical of an anionic surfactant - protein bonding, exhibit an initial increase steep followed by a slow growth region and then a vertical growth above a certain concentration. This isotherm is typical of ionic surfactant to protein binding. Often the high affinity initial bond appears at very low concentrations of surfactant and therefore in some protein-surfactant systems, the exact shape of the isotherm in this region may be missing. The surfactant - protein binding is influenced by a number of variables such as the nature and chain length of surfactant, pH, ionic strength, temperature, nature of this protein and additives.http://pubs.ub.ro/dwnl.php?id=CSCC6201104V04S01A0015binding isothermCMCdialysis techniqueproteinsurfactant |
| spellingShingle | Elena Irina Moater Cristiana Radulescu Ionica Ionita BINDING ISOTHERMS SURFACTANT-PROTEINS Scientific Study & Research: Chemistry & Chemical Engineering, Biotechnology, Food Industry binding isotherm CMC dialysis technique protein surfactant |
| title | BINDING ISOTHERMS SURFACTANT-PROTEINS |
| title_full | BINDING ISOTHERMS SURFACTANT-PROTEINS |
| title_fullStr | BINDING ISOTHERMS SURFACTANT-PROTEINS |
| title_full_unstemmed | BINDING ISOTHERMS SURFACTANT-PROTEINS |
| title_short | BINDING ISOTHERMS SURFACTANT-PROTEINS |
| title_sort | binding isotherms surfactant proteins |
| topic | binding isotherm CMC dialysis technique protein surfactant |
| url | http://pubs.ub.ro/dwnl.php?id=CSCC6201104V04S01A0015 |
| work_keys_str_mv | AT elenairinamoater bindingisothermssurfactantproteins AT cristianaradulescu bindingisothermssurfactantproteins AT ionicaionita bindingisothermssurfactantproteins |