Peptidomic analysis characterising proteolysis in thaw-aging of beef short plate

Yuri Kominami; Tatsuya Hayashi; Tetsuji Tokihiro; Hideki Ushio

doi:10.1016/j.fochms.2021.100051

Peptidomic analysis characterising proteolysis in thaw-aging of beef short plate

Food Chem (Oxf). 2021 Nov 18:3:100051. doi: 10.1016/j.fochms.2021.100051. eCollection 2021 Dec 30.

Authors

Yuri Kominami¹, Tatsuya Hayashi², Tetsuji Tokihiro³, Hideki Ushio¹

Affiliations

¹ Department of Aquatic Bioscience, Graduate School of Agricultural and Life Sciences, The University of Tokyo, 1-1-1, Yayoi, Bunkyo-ku, Tokyo 113-865, Japan.
² Division of Computer Science and Information Technology, Graduate School of Information Science and Technology, Hokkaido University, Kita 14, Nishi 9, Kita-ku, Sapporo, Hokkaido 060-0814, Japan.
³ Department of Mathematical Sciences, Graduate School of Mathematical Sciences, The University of Tokyo, 3-8-1 Komaba, Meguro-ku, Tokyo 153-8914, Japan.

Abstract

Recent studies have suggested that thaw-aging can improve sensory attributes of freeze-thawed meat. Acceleration of proteolysis is expected to promote tenderisation and improve taste; however, the details of protein degradation, including substrate proteins and cleavage sites, remain unclear. Here, we report a time course overview of the peptidome of beef short plates during thaw-aging. The accelerated degradation of key proteins for meat tenderisation, such as troponin T and desmin, was confirmed. Additionally, 11 cleavage sites in troponin T related to taste-active peptide generation were identified. Terminome analysis showed that the contribution of each protease varies depending on the substrate proteins and the thaw-aging period. Based on our results; proteases, not only calpains, but also others contributed to the degradation of myofibrillar proteins. The techniques employed indicate that meat proteolysis during thaw-aging is not constant but dynamic.

Keywords: IDA, information-dependent acquisition; Linear regression model; Meat proteolysis; Peptidomics; SWATH, the sequential window acquisition of all theoretical mass spectra; Terminome analysis; Thaw-aging; XIC, extracted ion chromatogram.