1. Formation and characterization of thiol-modified fibrillated whey protein isolate solution with enhanced functionalities
- Author
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Faridah Abas, Tai Boon Tan, Hon Weng Chang, Chin Ping Tan, Oi Ming Lai, Imededdine Arbi Nehdi, and Phui Yee Tan
- Subjects
chemistry.chemical_classification ,biology ,Stability index ,Chemistry ,Propanethiol ,macromolecular substances ,04 agricultural and veterinary sciences ,02 engineering and technology ,Repulsion force ,021001 nanoscience & nanotechnology ,Ph changes ,Fibril ,040401 food science ,Whey protein isolate ,chemistry.chemical_compound ,0404 agricultural biotechnology ,Chemical engineering ,Zeta potential ,biology.protein ,Thiol ,Organic chemistry ,0210 nano-technology ,Food Science - Abstract
The effect of thiolation using propanethiol on the functionalities of fibrillated whey protein isolate (WPI) solution at different pH values was studied. Fibrillated WPI solutions were thiolated at different molar ratios of propanethiol:carboxyl group (0.5:1, 1:1, 2:1, 3:1, 4:1) and the highest esterification extent ratio was obtained at 4:1 (pH 9). We also found that the thiolation process improved the foaming capacity and foam stability. TEM micrographs evidenced aggregation of thiol-modified fibrillated WPI. A network of shortened fibrils attached to each other was formed upon thiolation, suggesting good physical interaction. This was coherent with the increment of zeta potential values, indicating a greater repulsion force to retard fibrils aggregation. Thiolation enhanced emulsifying stability index of thiol-modified fibrillated WPI solution (pH 8) and diminished its susceptibility to pH changes. This has broadened the potential application of fibrils as food ingredients.
- Published
- 2017
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