Effect of plant protein mixtures on the microstructure and rheological properties of myofibrillar protein gel derived from red sea bream (Pagrosomus major). (November 2019)
- Record Type:
- Journal Article
- Title:
- Effect of plant protein mixtures on the microstructure and rheological properties of myofibrillar protein gel derived from red sea bream (Pagrosomus major). (November 2019)
- Main Title:
- Effect of plant protein mixtures on the microstructure and rheological properties of myofibrillar protein gel derived from red sea bream (Pagrosomus major)
- Authors:
- Lin, Duanquan
Zhang, Longtao
Li, Runjing
Zheng, Baodong
Rea, Mary C.
Miao, Song - Abstract:
- Abstract: In this study, the influence of plant protein mixtures (soy protein isolate (SPI) + peanut protein isolate (PPI), SPI + rice protein isolate (RPI), and PPI + RPI) on the microstructure, rheological properties and molecular driving forces of myofibrillar protein (MP) gels was studied. SPI could form a gel with smoother and denser network, while the structures of PPI and RPI gels were rougher, which led to the network structures of SPI + PPI and SPI + RPI gels but the disrupted structure of PPI + RPI gel. However, the SPI + RPI and PPI + RPI gels with different microstructures exhibited larger gel strength compared to the RPI gel. After mixing MP with the mixture of SPI + PPI and SPI + RPI, the mixed gels became more compact, evener and smoother, while the mixture of PPI + RPI induced more pores to the MP gel. However, G′ values of these three kinds of mixed gels were similar and much larger than that of MP gel. In addition, the molecular driving forces involved in the mixed plant protein gels and mixed MP-plant protein gels were mainly hydrophobic interactions and disulfide bonds. Graphical abstract: Image 1 Highlights: Mixing SPI with PPI or RPI formed gel network while the PPI + RPI gel was disrupted. The mixture of SPI + PPI and SPI + RPI made the MP gel more compact and smoother. The mixture of PPI + RPI induced more pores to the MP gel. Hydrophobic interactions and disulfide bonds were main molecular driving forces in mixed gels.
- Is Part Of:
- Food hydrocolloids. Volume 96(2019)
- Journal:
- Food hydrocolloids
- Issue:
- Volume 96(2019)
- Issue Display:
- Volume 96, Issue 2019 (2019)
- Year:
- 2019
- Volume:
- 96
- Issue:
- 2019
- Issue Sort Value:
- 2019-0096-2019-0000
- Page Start:
- 537
- Page End:
- 545
- Publication Date:
- 2019-11
- Subjects:
- Plant protein gel -- Myofibrillar protein gel -- Rheological property -- Microstructure -- SEM
Hydrocolloids -- Periodicals
Food additives -- Periodicals
Colloïdes -- Périodiques
Aliments -- Additifs -- Périodiques
Colloids
Food additives
Periodicals
Electronic journals
664.06 - Journal URLs:
- http://www.sciencedirect.com/science/journal/0268005X ↗
http://www.elsevier.com/journals ↗ - DOI:
- 10.1016/j.foodhyd.2019.05.043 ↗
- Languages:
- English
- ISSNs:
- 0268-005X
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 3977.556000
British Library DSC - BLDSS-3PM
British Library STI - ELD Digital store - Ingest File:
- 11021.xml