Interplay between transglutaminase treatment and changes in digestibility of dietary proteins

Yuxuan Wang; Qipu Xin; Yujia Miao; Xianming Zeng; Hao Li; Kai Shan; Yingqun Nian; Di Zhao; Juqing Wu; Chunbao Li

doi:10.1016/j.foodchem.2021.131446

Interplay between transglutaminase treatment and changes in digestibility of dietary proteins

Food Chem. 2022 Mar 30;373(Pt A):131446. doi: 10.1016/j.foodchem.2021.131446. Epub 2021 Oct 21.

Authors

Yuxuan Wang¹, Qipu Xin¹, Yujia Miao¹, Xianming Zeng¹, Hao Li¹, Kai Shan¹, Yingqun Nian¹, Di Zhao², Juqing Wu³, Chunbao Li¹

Affiliations

¹ Key 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.
² Key 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. Electronic address: zhaodi@njau.edu.cn.
³ Key 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. Electronic address: wujuqing@njau.edu.cn.

PMID: 34715626
DOI: 10.1016/j.foodchem.2021.131446

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.

Keywords: Peptidomics; Protein digestibility; Transglutaminase.

MeSH terms

Dietary Proteins
Digestion*
Peptides
Soybean Proteins
Transglutaminases*

Substances

Dietary Proteins
Peptides
Soybean Proteins
Transglutaminases