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Updated: Jul 16, 2026

Protein Misfolding Cyclic Amplification of Prions
Published on: November 7, 2012
Prion inactivation by the Maillard reaction.
Kyozo Suyama1, Miyako Yoshioka, Mitsugu Akagawa
1Sports Nutrition Department, Sendai University, Miyagi, Japan.
The Maillard reaction effectively reduces prion protein infectivity in contaminated materials. This method offers a promising decontamination strategy for animal byproducts like meat and bone meal, preventing disease transmission.
Area of Science:
- Veterinary Medicine
- Biochemistry
- Food Safety
Background:
- Variant Creutzfeldt-Jakob disease (vCJD) is linked to bovine spongiform encephalopathy (BSE).
- Prion protein (PrP(Sc)) in contaminated feed, such as meat and bone meal (MBM), poses a transmission risk.
- Effective decontamination methods are crucial for preventing prion disease spread.
Purpose of the Study:
- To investigate the efficacy of the Maillard reaction in reducing prion infectivity.
- To assess the Maillard reaction's potential for decontaminating animal byproducts.
Main Methods:
- Utilized a Maillard reaction with glucose and sodium hydrogen carbonates on scrapie-infected hamster brain homogenate.
- Assessed prion inactivation using a hamster bioassay.
- Employed protein misfolding cyclic amplification (PMCA) as a rapid in vitro test for PrP(Sc) detection.
Main Results:
- The Maillard reaction achieved a significant prion infectivity reduction of approximately 5.9-log.
- PMCA analysis confirmed a substantial decrease in PrP(Sc) levels post-reaction.
- The reaction demonstrated effectiveness in inactivating the infectious agents.
Conclusions:
- The Maillard reaction is a viable method for decontaminating prion-infected materials.
- This technique can be applied to large volumes of byproducts like MBM.
- It offers a potential solution for preventing prion disease transmission through feed.
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