Universal Strategy for Regulating Protein‐Based High Internal Phase Emulsions as 3D Printing Materials
Source abstract
Abstract
Abstract Protein‐stabilized high internal phase emulsions (HIPEs), which are pseudoplastic fluids with shear thinning and high viscoelasticity, are suitable for 3D printing inks. However, owing to the lack of a universal approach to the 3D printing of HIPEs, existing printing materials are unable to meet the developmental, biocompatibility, and safety requirements of various applications. Herein, it is demonstrated that post‐acidification of protein HIPEs enhances 3D printing performance. This method has the advantage of breaking through protein limitations, pH, and other environmental factors. The self‐supporting property required for 3D printing is achieved through the self‐assembly of continuous‐phase proteins into particle aggregates, and interfacial stability is maintained owing to the constant interfacial tension and contact angle. The acid‐induced protein aggregates in the continuous phase do not affect the stability of the modified HIPEs. This work provides a valuable new idea for advancing the application of protein HIPEs in 3D printing through a post‐acidification strategy.
Source: crossref · Quality: baseline
Research context
OpenAlex topics: Proteins in Food Systems · Pickering emulsions and particle stabilization · Polysaccharides Composition and Applications
SciVX discovery tags are terminology-based. OpenAlex topics are source-provided classifications.
Affiliations
National Engineering Research Center of Seafood Collaborative Innovation Center of Provincial and Ministerial Co‐construction for Seafood Deep Processing School of Food Science and Technology Dalian Polytechnic University Dalian 116034 P. R. China
Funding
National Natural Science Foundation of China
References (36)
Show source-provided references
1. 10.1016/j.tifs.2012.04.00610.1016/j.tifs.2012.04.006 ↗
2. 10.15171/bi.2018.0910.15171/bi.2018.09 ↗
3. 10.1111/ijfs.1539110.1111/ijfs.15391 ↗
4. 10.1016/j.tifs.2020.11.02310.1016/j.tifs.2020.11.023 ↗
5. 10.1016/j.cofs.2020.01.00910.1016/j.cofs.2020.01.009 ↗
6. 10.1021/acs.langmuir.1c0259910.1021/acs.langmuir.1c02599 ↗
7. 10.1021/acs.jafc.1c0187710.1021/acs.jafc.1c01877 ↗
8. 10.1039/C5RA01859E10.1039/C5RA01859E ↗
9. 10.1098/rsta.2017.003910.1098/rsta.2017.0039 ↗
10. 10.1016/j.foodhyd.2018.04.00610.1016/j.foodhyd.2018.04.006 ↗
11. 10.1016/j.foodhyd.2022.10755410.1016/j.foodhyd.2022.107554 ↗
12. 10.1021/acsami.0c1143410.1021/acsami.0c11434 ↗
13. 10.1002/adfm.20210174910.1002/adfm.202101749 ↗
14. 10.1016/j.carbpol.2021.11858610.1016/j.carbpol.2021.118586 ↗
15. 10.1016/j.foodhyd.2021.10699710.1016/j.foodhyd.2021.106997 ↗
16. Pan H. · J. Food Eng. · 2022 · 334
17. Liu H. · Adv. Colloid Interface Sci. · 2022 · 311
18. 10.1111/j.1365-2621.2002.tb11370.x10.1111/j.1365-2621.2002.tb11370.x ↗
19. 10.3390/nano1217294910.3390/nano12172949 ↗
20. 10.1016/j.foodchem.2016.10.01910.1016/j.foodchem.2016.10.019 ↗
21. 10.1016/j.tifs.2017.08.01810.1016/j.tifs.2017.08.018 ↗
22. 10.3390/foods1113190210.3390/foods11131902 ↗
23. 10.1016/j.foodhyd.2022.10796910.1016/j.foodhyd.2022.107969 ↗
24. 10.1146/annurev-food-081114-11082210.1146/annurev-food-081114-110822 ↗
25. 10.1016/j.cocis.2021.10150910.1016/j.cocis.2021.101509 ↗
26. 10.1021/acs.langmuir.0c0195510.1021/acs.langmuir.0c01955 ↗
27. 10.1016/j.tifs.2022.05.01810.1016/j.tifs.2022.05.018 ↗
28. 10.1002/adfm.20210174910.1002/adfm.202101749 ↗
29. 10.1016/S0377-0257(02)00141-610.1016/S0377-0257(02)00141-6 ↗
30. 10.1016/j.foodres.2020.11007610.1016/j.foodres.2020.110076 ↗
31. 10.1016/j.foodhyd.2021.10696210.1016/j.foodhyd.2021.106962 ↗
32. 10.1016/j.progpolymsci.2022.10158010.1016/j.progpolymsci.2022.101580 ↗
33. 10.1021/la052207h10.1021/la052207h ↗
34. 10.1016/j.foodres.2014.03.00210.1016/j.foodres.2014.03.002 ↗
35. 10.1016/S0963-9969(98)00015-510.1016/S0963-9969(98)00015-5 ↗
36. 10.1093/icb/icp01010.1093/icb/icp010 ↗