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Updated: Oct 15, 2025

Recognition of Epidermal Transglutaminase by IgA and Tissue Transglutaminase 2 Antibodies in a Rare Case of Rhesus Dermatitis
Published on: December 15, 2011
Interplay between transglutaminase treatment and changes in digestibility of dietary proteins
Yuxuan Wang1, Qipu Xin1, Yujia Miao1
1Key Laboratory of Meat Processing and Quality Control, MOE, Jiangsu Collaborative Innovation Center of Meat Production and Processing, Quality and Safety Control, Key Laboratory of Meat Products Processing, MOA, Nanjing Agricultural University, Nanjing 210095, PR China.
Abstract:
The changes in digestibility of TG-treated myofibrillar protein (MP), soybean protein isolate (SPI) and mixed proteins were evaluated by measuring liberation of primary amino groups, monitoring structural changes and investigating peptide fingerprints. TG treatment generally increased gastric digestion of treated proteins, possibly due to the structural changes occurred during TG treatment. In contrast, the initial intestinal digestion was suppressed by TG treatment. Compared with MP, the digestibility and peptide composition of SPI were affected by TG treatment to a larger degree, possibly due to the higher level of glutamine in SPI. Peptidomics analysis indicated that the changes in peptide composition of digests of TG-treated samples were related with the loss of Lys residues during TG treatment. Larger quantities of bioactive peptides KIEFEQFLPM, EVHEPEEKPRPK and TVKEDQVFPMNPPK were released after digestion of TG-treated MP. These results highlighted the complex and substantial influence of TG treatment on the digestibility of dietary proteins.
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