The regulatory mechanisms for beef tenderization by the calcium-independent phospholipase A2 activity of Peroxiredoxin 6
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Updated: May 30, 2025

Evaluation of Protein–Protein Interactions using an On-Membrane Digestion Technique
Published on: July 19, 2019
Xinyi Wang1, Jitong Liu2, Benjamin W B Holman3
1Lab of Meat Processing and Quality Control, College of Food Science and Engineering, Shandong Agricultural University, Tai'an, Shandong 271018, PR China; Key Laboratory of Endocrine Glucose & Lipids Metabolism and Brain Aging, Ministry of Education; Department of Endocrinology, Shandong Provincial Hospital Affiliated to Shandong First Medical University, Jinan, Shandong 250021, PR China.
Abstract:
This study investigated the effect of the inhibition of the activity of Ca2+-independent Phospholipase A2 (iPLA2) of Peroxiredoxin 6 (Prdx6) on beef tenderization in the early post-mortem period. Longissimus lumborum (LL) were incubated with or without the inhibitor of iPLA2 activity of Prdx6 (MJ33) for 1, 6, 12, 24, or 36 h, followed by incubation with or without the H2O2. iPLA2 activity, troponin T and desmin, Ca2+ concentration, calpain-1, caspases, apoptosis rate, and cell morphology were examined. It was found that the reduction of the iPLA2 activity of Prdx6 was found to promote degradation of cytoskeletal proteins (troponin T, desmin). The inhibition of the iPLA2 activity of Prdx6 suppressed the caspases activation. This reduced the apoptotic rate, but increased Ca2+ concentrations and calpain-1 activation, outcomes that promoted beef tenderization. This mechanistic characterization confirms the application of Prdx6 as a biomarker for beef of high quality and consumer acceptance.
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