Journal
JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY
Volume 59, Issue 4, Pages 1236-1243Publisher
AMER CHEMICAL SOC
DOI: 10.1021/jf103579u
Keywords
Isopeptide bond; wheat gluten; cross-linking; electron transfer dissociation
Funding
- Research Foundation - Flanders (FWO, Brussels, Belgium)
- COST Action [928]
- K.U.Leuven, Leuven, Belgium
Ask authors/readers for more resources
Results in this paper confirm heat-induced isopeptide bond formation in wheat gluten. Heating (24 h, 130 degrees C). of wheat gluten [moisture content 7.4%] decreased its extractability in sodium dodecyl sulfate containing buffer (pH 6.8), even after reduction of disulfide (SS) bonds. Thus, both SS bonds and non-SS bonds were responsible for the extractability loss. Cross-links of the lysinoalanine and lanthionine type were not present in the heated samples, but heat treatment reduced levels of available amino. groups. Heating of purified and alkylated high molecular weight glutenin subunits (HMW-GS) under similar conditions also resulted in extractability kiss, demonstrating that cross-linking did not solely depend on the availability of cysteine or cystine. These observations indicated that heat treatment had induced isopeptide bond formation, resulting in larger and unextractable molecules. Heating HMW-GS lysine- and glutamine-containing peptides induced the formation of isopeptide bonds, thereby supporting the above hypothesis. The level of isopeptide bond formation increased with heating time.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available