AMSA Announces Symposium Speakers on Oxidation of Muscle Proteins

May 04, 2022

Media Contact: Deidrea Mabry, dmabry@meatscience.org


AMSA Announces Symposium Speakers on Oxidation of Muscle Proteins

Kearney, MO. May 4, 2022 – The American Meat Science Association (AMSA) is pleased to announce Dr. Youling Xiong, Dr. Elisabeth Huff-Lonergan, and Dr. Mark Richards as the featured speakers in the symposium entitled Oxidation of Muscle Proteins” on Monday, June 13, 2022, during the 75th AMSA Reciprocal Meat Conference (RMC). Texas Tech University is the sponsor for this session. 

Youling Xiong, Ph.D., University Research Professor at the University of Kentucky and AMSA 2022 International Lectureship Award Winner, begins this session speaking about “Oxidation and Muscle Protein Functionality: An Evolutionary Global Perspective.” Protein oxidation is a long-neglected phenomenon but is now recognized to occur readily and ubiquitously in postmortem muscle and meat products. Since the beginning of the 1990s, systematically designed studies with robust analytical tools have led to the understanding that oxidatively modified muscle proteins in the presence of reactive oxygen species generated in meat processing have significantly changed gelling, emulsifying, and water-binding properties. Modulating oxidative processes using processing and ingredient strategies makes it possible to mitigate undesirable effects and promote the functionality associated with protein oxidation.

Elisabeth Huff-Lonergan, Ph.D., Professor at Iowa State University, follows with a presentation on “Protein Oxidation and Meat Tenderness.” The tenderization of fresh meat is a very complex process. The industry and the scientific community have long been trying to solve the puzzle that is consistently and efficiently producing high-quality tender meat. Often overlooked is the role that oxidative processes in muscle play in regulating the subsequent tenderness of fresh meat. Dr. Huff-Lonergan will discuss how oxidation processes in antemortem and early postmortem meat can set the stage for subsequent tenderization.

Mark Richards, Ph.D., Professor at the University of Wisconsin-Madison, concludes this session by talking about “Myoglobin and Hemoglobin: Discoloration, Lipid Oxidation and Solvent Access to the Heme Pocket.” Conversion of the heme iron in myoglobin (Mb) and hemoglobin (Hb) from Fe2+ to Fe3+ is a critical step that causes quality deterioration in muscle foods, imparting discoloration, and generation of oxidative species, including dissociated heme, that degrades lipids and myofibrillar proteins. Increased solvent access to the heme crevice has been proposed to cause oxidation of the heme iron and decrease heme affinity, although empirical results are lacking. In this presentation, Dr. Richards will describe findings related to solvent access to the heme crevice of Mb and Hb using plasma-induced modification of biomolecules (PLIMB) followed by LC-MS/MS and a user-friendly software platform to quantify modified amino acid side chains of the heme proteins. Aspects of in-vivo modifications to Mb and Hb (e.g., HNE-adduction, methylations, acetylation) will be described in relation to oxidative stability of the heme proteins postmortem. Finally, some strategies to maintain Mb and Hb in the reduced state to extend storage time of muscle foods will be discussed.

AMSA is an organization recognized for its unmatched competence and commitment to attracting and developing meat industry leaders and providing science-based meat research and information. For more information, please visit www.meatscience.org/rmc or contact Deidrea Mabry at 1-800-517-AMSA ext. 12.



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