Comparison of the Structural and Physical Properties of Two Alginate Ion Complexes with Different Cationic Surfactants
Source abstract
Abstract
Two types of alginate (Alg) ion complexes were prepared from anionic alginate and two cationic surfactants. The surfactants had the same hexadecyl tail chain and different polar cationic groups: hexadecylpyridinium chloride (HDPyCl) and hexadecyltrimethylammonium bromide (HDTMABr). The Alg ion complexes Alg-HDPy (A-HPy) and Alg-HDTMA (A-HTm) were water-insoluble and soluble in ethanol. The transparent films of the A-HPy and A-HTm were obtained from the alcoholic solutions to study and compare their structures and physical properties using scanning electron microscope (SEM), thermogravimetric analysis (TGA), differential scanning calorimetry (DSC), small angle X-ray scattering (SAXS), and tensile test. The results showed that the A-HPy and A-HTm powders and films had distinct structures and physical properties, although they possessed the same alginates and alkyl chains with the same carbon number. This study reports that a variety of cationic moieties have different ion-pair formations and controlled inherent bulk structures and properties. Furthermore, the Alg ion complex films showed antibacterial functions, and there were differences with respect to their biological activities.
Source: openalex_inverted_index · Quality: baseline
Research context
OpenAlex topics: Analytical Chemistry and Chromatography · Biopolymer Synthesis and Applications · Surfactants and Colloidal Systems
SciVX discovery tags are terminology-based. OpenAlex topics are source-provided classifications.
Affiliations
Department of Biobased Materials Science, Kyoto Institute of Technology
Faculty of Fiber Science and Engineering, Kyoto Institute of Technology
References (40)
Show source-provided references
1. (a) E. P. Ivanova, I. Y. Bakunina, O. I. Nedashkovskaya, M. Nataliya M. Gorshkova, Y. V. Alexeeva, E. A. Zelepuga, T. N. Zvaygintseva, D. V. Nicolau, and V. V. Mikhailov, Curr. Microbiol., 46, 6 (2003).10.1007/s00284-002-3794-6 ↗
2. (b) F. Xu, Q.-Q. Cha, and Y.-Z. Zhang, Appl. Environ Microbiol., 87, e00368-21 (2021).
3. (a) C. J. Rivard, W. S. Adney, M. E. Himmel, D. J. Mitchell, T. B. Vinzant, K. Grohmann, L. Moens, and H. Chum, Appl. Biochem. Biotechnol., 34, 725 (1992).10.1007/BF02920592 ↗
4. (b) C. M. Buchanan, R. M. Gardner, and R. J. Komarek, J. Appl. Polym. Sci., 47, 1709 (1993).10.1002/app.1993.070471001 ↗
5. (c) C. Rivard, L. Moens, K. Roberts, J. Brigham, and S. Kelley, Enzym. Microb. Technol., 17, 848 (1995).10.1016/0141-0229(94)00120-G ↗
6. (a) K. Atsuki and Y. Tomada, J. Soc. Chem. Ind. Jpn., 29, 509 (1926). (in Japanese).
7. (b) E. Schmidt, and F. Vocke, Ber., 59, 1585 (1926).10.1002/cber.19260590735 ↗
8. (c) H. G. Mautner, Econ. Bot., 8, 174-192 (1954).10.1007/BF02984737 ↗
9. (d) K. I. Draget, O. Smidsrùd, and G. Skjåk-Brñk, 8, 235, In Biopolymers for medical and pharmaceutical applications. Volume 1: ed by A. Steinbüchel and R. H. Marchessault, Weinheim: Wiley-VCH-Verl., (2005).
10. (a) H. Thiele, Discuss. Faraday Soc., 18, 294 (1954).10.1039/df9541800294 ↗
11. (b) O. Smidsrød and A. Haug, Acta. Chem. Scand., 19, 329 (1965).10.3891/acta.chem.scand.19-0329 ↗
12. (c) I. Braccini and S. Pérez, Biomacromolecules, 2, 1089 (2001).10.1021/bm010008g ↗
13. (a) A. Malovikova, K. Hayakawa, and J. C. T. Kwak, Chapter 15 p 225. In Structure/Performance Relationships in Surfactants.: ed by M. J. Rosen, ACS Sympo. Series (1984).10.1021/bk-1984-0253.ch015 ↗
14. (b) K. Liu, X. Lin, L. Chen, L. Huang, S. Cao, and H. Wang, J. Agric. Food Chem., 61, 6562 (2013).10.1021/jf4010065 ↗
15. (a) J. Witt, N. Ramji, R. Gibb, J. Dunavent, J. Flood, and J. Barnes, J. Contemp. Dent. Pract., 6, 1 (2005).10.5005/jcdp-6-1-1 ↗
16. (b) S. Haps, D. E. Slot, C. E. Berchier, and G. A. Van der Weijden, Int. J. Dent. Hyg., 6, 290 (2008).10.1111/j.1601-5037.2008.00344.x ↗
17. (c) R. Michael E. Richards, James Z. Xing, and Kirsty M. B. Mackay, Pharm. Res., 13, 1258 (1996).10.1023/A:1016084824877 ↗
18. (a) M. Singh, V. S. Gill, H. Thippareddi, R. K. Phebus, J. L. Marsden, T. J. Herald, and A. L. Nutsch, J. Food Prot., 68, 1823 (2005).10.4315/0362-028X-68.9.1823 ↗
19. (b) K. Lim and A. Mustapha, Food Microbiol., 24, 89 (2007).10.1016/j.fm.2006.04.005 ↗
20. (a) J. Mirtič, K. Kogej, S. Baumgartner, G. Smistad, J. Kristl, and M. Hiorth, Int. J. Pharm., 511, 774 (2016).10.1016/j.ijpharm.2016.07.065 ↗
21. (b) J. Mirtič, A. Paudel, P. Laggner, S. Hudoklin, M. E. Kreft, and J. Kristl, Int. J. Pharm., 580, 119199 (2020).10.1016/j.ijpharm.2020.119199 ↗
22. (a) P. Degen, M. Paulus, E. Zwar, V. Jakobi, S. Dogan, M. Tolan, and H. Rehage, Surf. Interface Anal., 51, 1051 (2019).10.1002/sia.6691 ↗
23. (b) M. A. Hoque, S. Mahbub, M. A. Khan, and G. E. Eldesoky, J. Disp. Sci. Technol., 43, 1039 (2020).10.1080/01932691.2020.1847661 ↗
24. (a) D. H.A. Abdelsalam and T. Aoki, J. Fiber Sci. Tech., 79, 250 (2023).10.2115/fiberst.2023-0027 ↗
25. (b) D. H. A. Abdelsalam, R. Yamakita, and T. Aoki, J. Fiber Sci. Tech., 80, 50 (2024).10.2115/fiberst.2024-0007 ↗
26. T. Kobayashi, K. Mao, S.-G. Wang, V. S.-Y. Lin, and M. Pruski, Solid State Nucl. Magn. Reson., 39, 65 (2011).10.1016/j.ssnmr.2011.02.001 ↗
27. P. T. Jacobs and E. W. Anacker, J. Colloid Interface Sci., 44, 505 (1973).10.1016/0021-9797(73)90328-7 ↗
28. E. R. Berg, D. D. Green, D. C. Moliva A., B. T. Bjerke, M. W. Gealy, and D. J. Ulness, J. Phys. Chem. A, 112, 833 (2008).10.1021/jp076260l ↗
29. S. G. Slade, M. Raupach, and W. W. Emerson, Clays Clay Miner., 26, 125 (1978).10.1346/CCMN.1978.0260207 ↗
30. J. Bors, Á. Patzkób, and I. Dékány, Appl. Clay Sci., 19, 27 (2001).10.1016/S0169-1317(01)00060-6 ↗
31. R. Chitrakar, Y. Makita, A. Sonoda, and T. Hirotsu. Appl. Clay Sci., 51, 375 (2011).10.1016/j.clay.2010.11.033 ↗
32. R. Russo, M. Malinconico, and G. Santagata, Biomacromolecules, 8, 3193 (2007).10.1021/bm700565h ↗
33. H. Zhou, N. Yang, J. Hou, C. Yu, Z. Jin, P. Zeng, L. Yang, Y. Fu, Y. Shen, and S. Guo, Food Packaging and Shelf Life, 34, 100935 (2022).10.1016/j.fpsl.2022.100935 ↗
34. A. Togo, Y. Enomoto, A. Takemura, and T. Iwata, J. Wood Sci., 65, 66 (2019).10.1186/s10086-019-1845-x ↗
35. S. Fujita, Y. Wakuda, M. Matsumura, and S. Suye, J. Mater. Chem. B, 7, 6556 (2019).10.1039/C9TB01353A ↗
36. L. Hou and P. Wu, Carbohydrate Polym., 205, 420 (2019).10.1016/j.carbpol.2018.10.091 ↗
37. I. M. Asher and I. W. Levin, Biochim. Biophys. Acta - Biomembranes, 468, 63 (1977).10.1016/0005-2736(77)90151-1 ↗
38. A. Harada, K. Okuyama, A. Kumano, T. Kajiyama, M. Takayanagi, and T. Kunitake, Polym. J., 18, 281 (1986).10.1295/polymj.18.281 ↗
39. E. A. Ponomarenko, A. J. Waddon, K. N. Bakeev, D. A. Tirrell, and W. J. MacKnight, Macromolecules, 29, 4340 (1996).10.1021/ma951088h ↗
40. A. R. Bucci, L. Marcelino, R. K. Mendes, and A. Etchegaray, World J. Microbiol. Biotechnol., 34, 86 (2018).10.1007/s11274-018-2472-1 ↗