Profiles of gelling characteristics of myofibrillar proteins extracted from chicken breast: Effects of temperatures and phosphates. (July 2020)
- Record Type:
- Journal Article
- Title:
- Profiles of gelling characteristics of myofibrillar proteins extracted from chicken breast: Effects of temperatures and phosphates. (July 2020)
- Main Title:
- Profiles of gelling characteristics of myofibrillar proteins extracted from chicken breast: Effects of temperatures and phosphates
- Authors:
- Shan, Lingyue
Li, Yan
Wang, Qiumin
Wang, Baowei
Guo, Liping
Sun, Jingxin
Xiao, Junxia
Zhu, Yinglian
Zhang, Xuecong
Huang, Ming
Xu, Xinglian
Yu, Jiying
Ho, Harvey
Kang, Dacheng - Abstract:
- Abstract: The systematic effects of temperatures and phosphates (single and compound forms) on gelling characteristics of myofibrillar proteins (MPs) extracted from chicken breast were investigated by texture analysis, Fourier-transform infrared spectroscopy, Raman spectroscopy, low-field nuclear magnetic resonance (NMR), scanning electron microscopy, and rheology. Heating to 60 °C and 80 °C induced the formation of an elastic and hard MP gel, and meanwhile compound phosphate (CP) enhanced gel elasticity and hardness. At 80 °C, the maximum elasticity and hardness of MP gels were determined as 0.81 ± 0.01 and 0.86 ± 0.02 N respectively. Compared to high temperature (100 and 120 °C) groups, the relative composition percentage of immobilized water reached a higher level for low temperature (60 and 80 °C) groups, determined as 95.15 ± 1.07% and 93.40 ± 1.02% respectively, indicating a better water-holding capacity. Raman and low field NMR analysis showed that low temperatures determined the affinity between moisture and MPs, while phosphates may help to protect gels from destruction caused by high temperatures. Hexametaphosphate and pyrophosphate as the composition of CP were liable to produce a desirable MP cross-linking network compared to tripolyphosphate. In addition, CP could strengthen the rheological viscoelasticity of MP gels formed at 80 °C. Highlights: CP promoted the better MP gel network formation. CP prevented MP gels from being destroyed at high temperatures. TheAbstract: The systematic effects of temperatures and phosphates (single and compound forms) on gelling characteristics of myofibrillar proteins (MPs) extracted from chicken breast were investigated by texture analysis, Fourier-transform infrared spectroscopy, Raman spectroscopy, low-field nuclear magnetic resonance (NMR), scanning electron microscopy, and rheology. Heating to 60 °C and 80 °C induced the formation of an elastic and hard MP gel, and meanwhile compound phosphate (CP) enhanced gel elasticity and hardness. At 80 °C, the maximum elasticity and hardness of MP gels were determined as 0.81 ± 0.01 and 0.86 ± 0.02 N respectively. Compared to high temperature (100 and 120 °C) groups, the relative composition percentage of immobilized water reached a higher level for low temperature (60 and 80 °C) groups, determined as 95.15 ± 1.07% and 93.40 ± 1.02% respectively, indicating a better water-holding capacity. Raman and low field NMR analysis showed that low temperatures determined the affinity between moisture and MPs, while phosphates may help to protect gels from destruction caused by high temperatures. Hexametaphosphate and pyrophosphate as the composition of CP were liable to produce a desirable MP cross-linking network compared to tripolyphosphate. In addition, CP could strengthen the rheological viscoelasticity of MP gels formed at 80 °C. Highlights: CP promoted the better MP gel network formation. CP prevented MP gels from being destroyed at high temperatures. The synergistic effect of SPP, TPP and HMP was conformed. Low temperatures greatly impacted gelling properties of MPs compared to phosphates. The conversion of α-helix to β-sheet led to more immobilized water retention. … (more)
- Is Part Of:
- Lebensmittel-Wissenschaft + Technologie =. Volume 129(2020)
- Journal:
- Lebensmittel-Wissenschaft + Technologie =
- Issue:
- Volume 129(2020)
- Issue Display:
- Volume 129, Issue 2020 (2020)
- Year:
- 2020
- Volume:
- 129
- Issue:
- 2020
- Issue Sort Value:
- 2020-0129-2020-0000
- Page Start:
- Page End:
- Publication Date:
- 2020-07
- Subjects:
- Myofibrillar protein gel -- Texture -- Raman spectroscopy -- Water distribution -- Viscoelasticity
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.2020.109525 ↗
- 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:
- 13569.xml