AI Article Synopsis
- The study identifies new types of bonds and cross-links formed in two food proteins (bovine serum albumin and wheat gliadin) after being heated with excess water for an extended time.
- Advanced techniques like liquid chromatography and mass spectrometry were used to analyze the changes in these proteins, particularly focusing on the reactions involving amino acids due to heat treatment.
- Key findings include the formation of specific bonds, such as lanthionine and lysinoalanine, which are believed to play an important role in the texture of food products.
Article Abstract
The present manuscript reports on the identification of various dehydroamino acid-derived bonds and cross-links resulting from thermal treatment (excess water, 240 min, 130 °C) of two model food proteins, bovine serum albumin, and wheat gliadin. S-Carbamidomethylated tryptic and chymotryptic digests of unheated (control) and heated serum albumin and gliadin, respectively, were analyzed by liquid chromatography coupled to tandem mass spectrometry (LC-ESI-MS/MS) with higher-energy collisional dissociation (HCD). Heat-induced β-elimination of cystine, serine and threonine, and subsequent Michael addition of cysteine and lysine to dehydroalanine and 3-methyl-dehydroalanine were demonstrated. Lanthionine, lysinoalanine, 3-methyl-lanthionine, and 3-methyl-lysinoalanine were identified. The detection of inter-chain lanthionine in both bovine serum albumin and wheat gliadin suggests the significance of these cross-links for food texture.
Download full-text PDF |
Source |
|---|---|
| http://dx.doi.org/10.1007/s00726-015-2139-2 | DOI Listing |
Publication Analysis
Top Keywords
Similar Publications
Want AI Summaries of new PubMed Abstracts delivered to your In-box?
Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!