A combined enzymatic and ionic cross-linking strategy for pea protein/sodium alginate double-network hydrogel with excellent mechanical properties and freeze-thaw stability. (October 2022)
- Record Type:
- Journal Article
- Title:
- A combined enzymatic and ionic cross-linking strategy for pea protein/sodium alginate double-network hydrogel with excellent mechanical properties and freeze-thaw stability. (October 2022)
- Main Title:
- A combined enzymatic and ionic cross-linking strategy for pea protein/sodium alginate double-network hydrogel with excellent mechanical properties and freeze-thaw stability
- Authors:
- Wang, Yihui
Jiao, Aiquan
Qiu, Chao
Liu, Qing
Yang, Yueyue
Bian, Shichao
Zeng, Fangye
Jin, Zhengyu - Abstract:
- Abstract: While pea protein (PeaP) is considered to be the plant protein with the most potential for use in plant-based meat products, it is limited by poor gel performance. To overcome this issue, a one-pot method was adopted to prepare a double-network (DN) hydrogel based on a transglutaminase-induced cross-linked network of PeaP and a physically cross-linked network of sodium alginate (SA). As SA concentration increased, the layered structure inside the hydrogel first converted into a porous honeycomb-like structure before forming a dense 3D network structure. Mechanical testing results suggested that the Young's Modulus of hydrogel increased from 2.1 MPa to 8.6 MPa at 80% strain as SA increased from 0% to 0.25%. This dense DN structure endowed the hydrogel with great fatigue resistance as well as excellent textural properties. Low-field nuclear magnetic resonance suggested that the DN hydrogel had a higher binding water content than PeaP single-network hydrogel, and showed good freeze-thaw stability. It is believed that this present work can give some insight into existing PeaP gel systems and inspire the development of more PeaP-based DN hydrogel with desired mechanical strength and freeze-thaw stability. Graphical abstract: Image 1 Highlights: Double-network hydrogel based on pea protein and sodium alginate was produced. The Young's Modulus of pea protein-based hydrogel increased from 2.1 to 8.6 MPa. Hydrogel exhibited great fatigue resistance and self-recoveryAbstract: While pea protein (PeaP) is considered to be the plant protein with the most potential for use in plant-based meat products, it is limited by poor gel performance. To overcome this issue, a one-pot method was adopted to prepare a double-network (DN) hydrogel based on a transglutaminase-induced cross-linked network of PeaP and a physically cross-linked network of sodium alginate (SA). As SA concentration increased, the layered structure inside the hydrogel first converted into a porous honeycomb-like structure before forming a dense 3D network structure. Mechanical testing results suggested that the Young's Modulus of hydrogel increased from 2.1 MPa to 8.6 MPa at 80% strain as SA increased from 0% to 0.25%. This dense DN structure endowed the hydrogel with great fatigue resistance as well as excellent textural properties. Low-field nuclear magnetic resonance suggested that the DN hydrogel had a higher binding water content than PeaP single-network hydrogel, and showed good freeze-thaw stability. It is believed that this present work can give some insight into existing PeaP gel systems and inspire the development of more PeaP-based DN hydrogel with desired mechanical strength and freeze-thaw stability. Graphical abstract: Image 1 Highlights: Double-network hydrogel based on pea protein and sodium alginate was produced. The Young's Modulus of pea protein-based hydrogel increased from 2.1 to 8.6 MPa. Hydrogel exhibited great fatigue resistance and self-recovery properties. Hydrogel showed excellent freeze-thaw stability. Hydrogel had good mechanical and textural properties after heating treatment. … (more)
- Is Part Of:
- Food hydrocolloids. Volume 131(2022)
- Journal:
- Food hydrocolloids
- Issue:
- Volume 131(2022)
- Issue Display:
- Volume 131, Issue 2022 (2022)
- Year:
- 2022
- Volume:
- 131
- Issue:
- 2022
- Issue Sort Value:
- 2022-0131-2022-0000
- Page Start:
- Page End:
- Publication Date:
- 2022-10
- Subjects:
- Hydrogel -- Pea protein -- Sodium alginate -- Double-network -- Gel property
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.2022.107737 ↗
- 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:
- 21661.xml