Effect of l-histidine and l-lysine on the properties of oil-in-water emulsions stabilized by porcine myofibrillar proteins at low/high ionic strength. (April 2021)
- Record Type:
- Journal Article
- Title:
- Effect of l-histidine and l-lysine on the properties of oil-in-water emulsions stabilized by porcine myofibrillar proteins at low/high ionic strength. (April 2021)
- Main Title:
- Effect of l-histidine and l-lysine on the properties of oil-in-water emulsions stabilized by porcine myofibrillar proteins at low/high ionic strength
- Authors:
- Guo, Xiuyun
Gao, Feng
Zhang, Yawei
Peng, Zengqi
Jamali, Muneer Ahmed - Abstract:
- Abstract: The effects of l -histidine (His) and l -lysine (Lys) on the emulsifying and interfacial properties of porcine myofibrillar proteins (MPs) at low/high ionic strength were investigated to improve physical stability of MPs emulsion at low ionic strength. Results showed that His and Lys increased emulsion stability index, and decreased creaming index at low ionic strength, but caused no significant changes in both indexes at high ionic strength. Additionaly, His and Lys increased the emulsifying activity and apparent viscosity, but decreased the droplet size at both ionic strength. His and Lys also promoted the diffusion of MPs and increased the interfacial pressure. Meanwhile, the interfacial loading of MPs was increased (p < 0.05) by 16.07% and 12.79% at low ionic strength, and by 8.85% and 8.24% at high ionic strength in the presence of Lys and His, respectively. Raman spectra revealed that the α-helix content of MPs was decreased (p < 0.05) by 5.05% and 11.79% at low ionic strength, and by 12.14% and 7.23% at high ionic strength in the presence of Lys and His, respectively. In summary, His and Lys enhanced the stability of MPs emulsion at low ionic strength via changing the structure and interfacial behaviour of MPs. Highlights: Histidine/Lysine causes the unfolding of porcine myofibrillar proteins. Histidine/Lysine promotes the adsorption of myofibrillar proteins on the oil surface. Histidine/Lysine decreases the interfacial tension. Histidine/Lysine decreasesAbstract: The effects of l -histidine (His) and l -lysine (Lys) on the emulsifying and interfacial properties of porcine myofibrillar proteins (MPs) at low/high ionic strength were investigated to improve physical stability of MPs emulsion at low ionic strength. Results showed that His and Lys increased emulsion stability index, and decreased creaming index at low ionic strength, but caused no significant changes in both indexes at high ionic strength. Additionaly, His and Lys increased the emulsifying activity and apparent viscosity, but decreased the droplet size at both ionic strength. His and Lys also promoted the diffusion of MPs and increased the interfacial pressure. Meanwhile, the interfacial loading of MPs was increased (p < 0.05) by 16.07% and 12.79% at low ionic strength, and by 8.85% and 8.24% at high ionic strength in the presence of Lys and His, respectively. Raman spectra revealed that the α-helix content of MPs was decreased (p < 0.05) by 5.05% and 11.79% at low ionic strength, and by 12.14% and 7.23% at high ionic strength in the presence of Lys and His, respectively. In summary, His and Lys enhanced the stability of MPs emulsion at low ionic strength via changing the structure and interfacial behaviour of MPs. Highlights: Histidine/Lysine causes the unfolding of porcine myofibrillar proteins. Histidine/Lysine promotes the adsorption of myofibrillar proteins on the oil surface. Histidine/Lysine decreases the interfacial tension. Histidine/Lysine decreases droplet size but increases apparent viscosity of emulsion. Histidine/Lysine increases the emulsion stability index of myofibrillar proteins. … (more)
- Is Part Of:
- Lebensmittel-Wissenschaft + Technologie =. Volume 141(2021)
- Journal:
- Lebensmittel-Wissenschaft + Technologie =
- Issue:
- Volume 141(2021)
- Issue Display:
- Volume 141, Issue 2021 (2021)
- Year:
- 2021
- Volume:
- 141
- Issue:
- 2021
- Issue Sort Value:
- 2021-0141-2021-0000
- Page Start:
- Page End:
- Publication Date:
- 2021-04
- Subjects:
- Amino acid -- Myofibrillar proteins -- Physical stability -- Conformational characteristics -- Interfacial properties
Food industry and trade -- Periodicals
Food -- Composition -- Periodicals
Microbiology -- Periodicals
Nutrition -- Periodicals
664.005 - Journal URLs:
- http://www.sciencedirect.com/science/journal/00236438 ↗
http://www.elsevier.com/journals ↗ - DOI:
- 10.1016/j.lwt.2021.110883 ↗
- Languages:
- English
- ISSNs:
- 0023-6438
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 3983.070000
British Library DSC - BLDSS-3PM
British Library HMNTS - ELD Digital store - Ingest File:
- 25576.xml