Abstract
Microbial transglutaminase (MTGase)-catalyzed interaction and gelation of mixed myofibrillar (MPI)/soy (SPI) protein isolates were investigated at varying ionic strengths and MPI:SPI ratios, with or without SPI being preheated (80 °C). MTGase treatments in deionized water converted myosin heavy chain and actin into lower molecular-weight polypeptides, which gradually diminished as the ionic strength increased up to 0.6 M NaCl. A reduced intensity in the electrophoretic bands of soy proteins (7S and 11S except the basic subunits) was observed in all treatments, suggesting cross-linking with MPI. The enzyme treatment slightly increased the thermal transition (denaturation) temperatures of MPI/SPI but greatly enhanced (P <0.05) the elasticity of the mixed protein gels when compared with untreated samples, independent of incubation time.
| Original language | English |
|---|---|
| Pages (from-to) | 899-907 |
| Number of pages | 9 |
| Journal | Meat Science |
| Volume | 65 |
| Issue number | 2 |
| DOIs | |
| State | Published - Oct 2003 |
Keywords
- Gelation
- Myofibrillar proteins
- Soy proteins
- Transglutaminase
ASJC Scopus subject areas
- Food Science
Fingerprint
Dive into the research topics of 'Effect of transglutaminase-induced cross-linking on gelation of myofibrillar/soy protein mixtures'. Together they form a unique fingerprint.Cite this
- APA
- Author
- BIBTEX
- Harvard
- Standard
- RIS
- Vancouver