Potential BSE risk posed by the use of ruminant collagen and gelatine in feed for non‐ruminant farmed animals

Abstract

EFSA was requested to estimate the cattle bovine spongiform encephalopathy ( BSE ) risk (C‐, L‐ and H‐ BSE ) posed by ruminant collagen and gelatine produced from raw material fit for human consumption, or from material classified as Category 3 animal by‐products ( ABP ), to be used in feed intended for non‐ruminant animals, including aquaculture animals. Three risk pathways ( RP ) were identified by which cattle could be exposed to ruminant feed cross‐contaminated with ruminant collagen or gelatine: 1) recycled former foodstuffs produced in accordance with Regulation ( EC ) No 853/2004 ( RP 1), 2) technological or nutritional additives or 3) compound feed, produced either in accordance with Regulation ( EC ) No 853/2004 ( RP 2a) or Regulation ( EU ) No 142/2011 ( RP 2b). A probabilistic model was developed to estimate the BSE infectivity load measured in cattle oral ID 50 (Co ID 50 )/kg, in the gelatine produced from the bones and hide of one infected animal older than 30 months with clinical BSE (worst‐case scenario). The amount of BSE infectivity (50th percentile estimate) in a member state ( MS ) with negligible risk status was 7.6 × 10 –2 Co ID 50 /kg, and 3.1 × 10 –4 Co ID 50 /kg in a MS with controlled risk status. The assessment considered the potential contamination pathways and the model results (including uncertainties) regarding the current epidemiological situation in the EU and current statutory controls. Given the estimated amount of BSE infectivity to which cattle would be exposed in a single year, and even if all the estimated undetected BSE cases in the EU were used for the production of collagen or gelatine (either using raw materials fit for human consumption or Category 3 ABP raw materials), it was concluded that the probability that no new case of BSE in the cattle population would be generated through any of the three RP is 99–100% (almost certain).

Collagen for neural tissue engineering: Materials, strategies, and challenges

“…More significantly, collagen originating from animal sources may be risky for disease transmission. Bovine spongiform encephalopathy (BSE) induced by ruminant collagen for human consumption has been investigated as a featured example [ 240 ]. Also commonly employed in dental surgery are bovine-derived collagen grafts, which might pose hazardous transmission of prion to patients [ 241 ].…”

Evaluation of the application for new alternative biodiesel production process for rendered fat including Category 1 animal by‐products (BDI‐RepCat® process, AT)

“…While a few well-characterised rodent-adapted strains were widely used for decontamination/ inactivation studies at the start of the bovine spongiform encephalopathy (BSE) epidemic, it has subsequently been shown that individual strains can respond very differently to different physicochemical processes, and extrapolation from one strain to another should be carried out with extreme caution, unless there are robust parallel studies that allow direct comparisons (EFSA BIOHAZ Panel, 2020a). This also applies to prions derived from naturally occurring TSE.…”

Selection of collagen IV fragments forming the outer sphere of the native protein: Assessment of biological activity for regenerative medicine

“…An additional problem is the source of collagen, which may be associated with an increased risk of transmission of zoonoses. In the case of collagens of porcine and bovine origin, there is increased risk of the transmission of bovine BSE 94,95 …”

“…In the case of collagens of porcine and bovine origin, there is increased risk of the transmission of bovine BSE. 94,95 Of course, the simplest solution would be to use human ECM proteins, but to date, there are no effective biotechnological methods for their production. Currently, the only way to minimize the risk of such complications is to replace the entire native human protein with peptides or a set of peptides with a structure corresponding to the fragments that determine the properties of the proteins.…”