| Literature DB >> 32145238 |
Farhad Alavi1, Zahra Emam-Djomeh2, Maryam Salami1, Mehdi Mohammadian1.
Abstract
In the current study, the impact of microbial transglutaminase (MTGase)-mediated crosslinking on the thermally denatured egg white protein (TD-EWP) made in alkaline pH in relation to their gelling properties of in gel and emulsion gel systems was investigated. Unlike native EWP that was not a good substrate for MTGase due to its compact structure, SDS-PAGE and gel solubility data showed the TD-EWP was sufficiently cross-linked by MTGase. The MTGase significantly (p < 0.05) increased the gel strength, fracture stress, fracture strain, and TPA parameters and decreased the frequency dependence of elastic modulus and stress dependence of creep compliance of TD-EWP gel and emulsion gel samples. The enhanced mechanical properties of the TE-EWP gelled samples treated with MTGase may be suitable for delivering sensitive compounds as well as in fabricating tailored scaffolds in tissue engineering and biomedical products.Entities:
Keywords: Cold gelation; Egg white protein; Rheology; Transglutaminase
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Year: 2020 PMID: 32145238 DOI: 10.1016/j.ijbiomac.2020.03.008
Source DB: PubMed Journal: Int J Biol Macromol ISSN: 0141-8130 Impact factor: 6.953