Effects of Selective Enzymatic Hydrolysis on Structural Properties and Gel Properties of Soybean Protein Isolate
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View abstract on PubMed
Summary
This summary is machine-generated.Enzymatic modification of soybean protein isolate (SPI) with papain improved gel texture and stability more than alkaline protease. Papain-treated SPI gels exhibited enhanced water-holding capacity and superior structural and rheological properties.
Area Of Science
- Food Science
- Protein Chemistry
- Biochemistry
Background
- Soybean protein isolate (SPI) gels often have poor stability and texture.
- Enzymatic hydrolysis can improve protein functionality and gel properties.
Purpose Of The Study
- To modify SPI using alkaline protease and papain.
- To evaluate the impact of enzymatic hydrolysis on SPI structure and gel quality.
Main Methods
- Analyzed hydrolysis degree (DH), particle size, and protein purity.
- Examined secondary structure changes (FT-IR), texture, water-holding capacity (WHC), rheology, and microstructure.
- Utilized SDS-PAGE to assess protein hydrolysis.
Main Results
- Papain hydrolysis yielded larger molecular weight peptides compared to alkaline protease.
- Enzymatic modification increased alpha-helix and beta-sheet content.
- Papain-modified SPI gels showed superior WHC, texture, rheology (G'), and microstructure.
Conclusions
- Papain is more effective than alkaline protease for enhancing SPI gel properties.
- Enzymatic modification offers a viable strategy for improving SPI functionality in food applications.
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