Fish are explicitly exempt from transmissible spongiform encephalopathy (TSE) regulations under EU Regulation 722/2012 and FDA guidance because they are not TSE-susceptible species

2026-06-11T13:29:57.011Z https://citation.is/oai

oai:citation.is:claim.300002 2026-06-10 claims salmon_biotech

10.0000/citation.is.claim.300002 citation.is Fish are explicitly exempt from transmissible spongiform encephalopathy (TSE) regulations under EU Regulation 722/2012 and FDA guidance because they are not TSE-susceptible species citation.is 2026 ScientificClaim salmon_biotech Supported Fish are explicitly exempt from transmissible spongiform encephalopathy (TSE) regulations under EU Regulation 722/2012 and FDA guidance because they are not TSE-susceptible species Source document: Salmon-Derived Biotech Product Feasibility Analysis CC BY 4.0 https://b2mbh3cn4a-w6dvs6ghja-uk.a.run.app/audit/270001#claim-300002 https://eur-lex.europa.eu/legal-content/EN/TXT/?uri=CELEX:32012R0722

oai:citation.is:claim.300043 2026-06-10 claims salmon_biotech

10.0000/citation.is.claim.300043 citation.is human growth hormone (hGH) in Escherichia coli BL21(DE3) citation.is 2026 ScientificClaim salmon_biotech Insufficient Evidence human growth hormone (hGH) in Escherichia coli BL21(DE3) Source document: Circular Approach to Biomanufacturing: Enhancing Therapeutic Protein Production Using Chum Salmon Head Peptone. CC BY 4.0 https://b2mbh3cn4a-w6dvs6ghja-uk.a.run.app/audit/270006#claim-300043

oai:citation.is:claim.300037 2026-06-10 claims salmon_biotech

10.0000/citation.is.claim.300037 citation.is chum salmon (Oncorhynchus keta) citation.is 2026 ScientificClaim salmon_biotech Insufficient Evidence chum salmon (Oncorhynchus keta) Source document: Circular Approach to Biomanufacturing: Enhancing Therapeutic Protein Production Using Chum Salmon Head Peptone. CC BY 4.0 https://b2mbh3cn4a-w6dvs6ghja-uk.a.run.app/audit/270006#claim-300037

oai:citation.is:claim.300042 2026-06-10 claims salmon_biotech

10.0000/citation.is.claim.300042 citation.is human growth hormone (hGH) in Escherichia coli BL21(DE3) citation.is 2026 ScientificClaim salmon_biotech Insufficient Evidence human growth hormone (hGH) in Escherichia coli BL21(DE3) Source document: Circular Approach to Biomanufacturing: Enhancing Therapeutic Protein Production Using Chum Salmon Head Peptone. CC BY 4.0 https://b2mbh3cn4a-w6dvs6ghja-uk.a.run.app/audit/270006#claim-300042

oai:citation.is:claim.300039 2026-06-10 claims salmon_biotech

10.0000/citation.is.claim.300039 citation.is The resulting chum salmon head peptone (CSHP) exhibited favorable characteristics, including a low average molecular mass (557 Da) citation.is 2026 ScientificClaim salmon_biotech Insufficient Evidence The resulting chum salmon head peptone (CSHP) exhibited favorable characteristics, including a low average molecular mass (557 Da) Source document: Circular Approach to Biomanufacturing: Enhancing Therapeutic Protein Production Using Chum Salmon Head Peptone. CC BY 4.0 https://b2mbh3cn4a-w6dvs6ghja-uk.a.run.app/audit/270006#claim-300039

oai:citation.is:claim.300038 2026-06-10 claims salmon_biotech

10.0000/citation.is.claim.300038 citation.is Protamex achieved the highest hydrolysis and recovery rates. citation.is 2026 ScientificClaim salmon_biotech Insufficient Evidence Protamex achieved the highest hydrolysis and recovery rates. Source document: Circular Approach to Biomanufacturing: Enhancing Therapeutic Protein Production Using Chum Salmon Head Peptone. CC BY 4.0 https://b2mbh3cn4a-w6dvs6ghja-uk.a.run.app/audit/270006#claim-300038

oai:citation.is:claim.300041 2026-06-10 claims salmon_biotech

10.0000/citation.is.claim.300041 citation.is CSHP was evaluated as a nitrogen source for recombinant protein production and supported higher expression of human superoxide dismutase (hSOD) citation.is 2026 ScientificClaim salmon_biotech Insufficient Evidence CSHP was evaluated as a nitrogen source for recombinant protein production and supported higher expression of human superoxide dismutase (hSOD) Source document: Circular Approach to Biomanufacturing: Enhancing Therapeutic Protein Production Using Chum Salmon Head Peptone. CC BY 4.0 https://b2mbh3cn4a-w6dvs6ghja-uk.a.run.app/audit/270006#claim-300041

oai:citation.is:claim.300040 2026-06-10 claims salmon_biotech

10.0000/citation.is.claim.300040 citation.is a high amino nitrogen content (4.9%) citation.is 2026 ScientificClaim salmon_biotech Insufficient Evidence a high amino nitrogen content (4.9%) Source document: Circular Approach to Biomanufacturing: Enhancing Therapeutic Protein Production Using Chum Salmon Head Peptone. CC BY 4.0 https://b2mbh3cn4a-w6dvs6ghja-uk.a.run.app/audit/270006#claim-300040

oai:citation.is:claim.300035 2026-06-10 claims salmon_biotech

10.0000/citation.is.claim.300035 citation.is Mussel processing wastewater (MPW) was used as a sugar source and tuna peptone (TP) from viscera residue as a protein substrate for the production of hyaluronic acid (HA), biomass and lactic acid (LA) citation.is 2026 ScientificClaim salmon_biotech Insufficient Evidence Mussel processing wastewater (MPW) was used as a sugar source and tuna peptone (TP) from viscera residue as a protein substrate for the production of hyaluronic acid (HA), biomass and lactic acid (LA) by Streptococcus zooepidemicus in batch fermentation. Source document: Hyaluronic acid production by Streptococcus zooepidemicus in marine by-products media from mussel processing wastewaters and tuna peptone viscera. CC BY 4.0 https://b2mbh3cn4a-w6dvs6ghja-uk.a.run.app/audit/270005#claim-300035

oai:citation.is:claim.300036 2026-06-10 claims salmon_biotech

10.0000/citation.is.claim.300036 citation.is Complete residual media achieved high production (3.67, 2.46 and 30.83 g l(-1) of biomass, HA and LA respectively) and a high molecular weight of HA (approximately 2500 kDa). citation.is 2026 ScientificClaim salmon_biotech Insufficient Evidence Complete residual media achieved high production (3.67, 2.46 and 30.83 g l(-1) of biomass, HA and LA respectively) and a high molecular weight of HA (approximately 2500 kDa). Source document: Hyaluronic acid production by Streptococcus zooepidemicus in marine by-products media from mussel processing wastewaters and tuna peptone viscera. CC BY 4.0 https://b2mbh3cn4a-w6dvs6ghja-uk.a.run.app/audit/270005#claim-300036

oai:citation.is:claim.300034 2026-06-10 claims salmon_biotech

10.0000/citation.is.claim.300034 citation.is These peptones were included (in the range of 2.6-11 g/L of soluble protein) as main source of organic nitrogen (protein substrates) in low-cost media for the culture of lactic acid bacteria (LAB), ma citation.is 2026 ScientificClaim salmon_biotech Insufficient Evidence These peptones were included (in the range of 2.6-11 g/L of soluble protein) as main source of organic nitrogen (protein substrates) in low-cost media for the culture of lactic acid bacteria (LAB), marine probiotic bacteria (MPB) and ubiquitous Gram+ bacteria. Source document: Biotechnological Valorization of Food Marine Wastes: Microbial Productions on Peptones Obtained from Aquaculture By-Products. CC BY 4.0 https://b2mbh3cn4a-w6dvs6ghja-uk.a.run.app/audit/270004#claim-300034

oai:citation.is:claim.300033 2026-06-10 claims salmon_biotech

10.0000/citation.is.claim.300033 citation.is These peptones were included (in the range of 2.6-11 g/L of soluble protein) as main source of organic nitrogen (protein substrates) in low-cost media for the culture of lactic acid bacteria (LAB), ma citation.is 2026 ScientificClaim salmon_biotech Insufficient Evidence These peptones were included (in the range of 2.6-11 g/L of soluble protein) as main source of organic nitrogen (protein substrates) in low-cost media for the culture of lactic acid bacteria (LAB), marine probiotic bacteria (MPB) and ubiquitous Gram+ bacteria. Source document: Biotechnological Valorization of Food Marine Wastes: Microbial Productions on Peptones Obtained from Aquaculture By-Products. CC BY 4.0 https://b2mbh3cn4a-w6dvs6ghja-uk.a.run.app/audit/270004#claim-300033

oai:citation.is:claim.300032 2026-06-10 claims salmon_biotech

10.0000/citation.is.claim.300032 citation.is These peptones were included (in the range of 2.6-11 g/L of soluble protein) as main source of organic nitrogen (protein substrates) in low-cost media for the culture of lactic acid bacteria (LAB), ma citation.is 2026 ScientificClaim salmon_biotech Insufficient Evidence These peptones were included (in the range of 2.6-11 g/L of soluble protein) as main source of organic nitrogen (protein substrates) in low-cost media for the culture of lactic acid bacteria (LAB), marine probiotic bacteria (MPB) and ubiquitous Gram+ bacteria. Source document: Biotechnological Valorization of Food Marine Wastes: Microbial Productions on Peptones Obtained from Aquaculture By-Products. CC BY 4.0 https://b2mbh3cn4a-w6dvs6ghja-uk.a.run.app/audit/270004#claim-300032

oai:citation.is:claim.300031 2026-06-10 claims salmon_biotech

10.0000/citation.is.claim.300031 citation.is These peptones were included (in the range of 2.6-11 g/L of soluble protein) as main source of organic nitrogen (protein substrates) in low-cost media for the culture of lactic acid bacteria (LAB), ma citation.is 2026 ScientificClaim salmon_biotech Insufficient Evidence These peptones were included (in the range of 2.6-11 g/L of soluble protein) as main source of organic nitrogen (protein substrates) in low-cost media for the culture of lactic acid bacteria (LAB), marine probiotic bacteria (MPB) and ubiquitous Gram+ bacteria. Source document: Biotechnological Valorization of Food Marine Wastes: Microbial Productions on Peptones Obtained from Aquaculture By-Products. CC BY 4.0 https://b2mbh3cn4a-w6dvs6ghja-uk.a.run.app/audit/270004#claim-300031

oai:citation.is:claim.300030 2026-06-10 claims salmon_biotech

10.0000/citation.is.claim.300030 citation.is wastes generated from the industrial processing of turbot, salmon, trout, seabream and seabass. citation.is 2026 ScientificClaim salmon_biotech Insufficient Evidence wastes generated from the industrial processing of turbot, salmon, trout, seabream and seabass. Source document: Biotechnological Valorization of Food Marine Wastes: Microbial Productions on Peptones Obtained from Aquaculture By-Products. CC BY 4.0 https://b2mbh3cn4a-w6dvs6ghja-uk.a.run.app/audit/270004#claim-300030

oai:citation.is:claim.300029 2026-06-10 claims salmon_biotech

10.0000/citation.is.claim.300029 citation.is wastes generated from the industrial processing of turbot, salmon, trout, seabream and seabass. citation.is 2026 ScientificClaim salmon_biotech Insufficient Evidence wastes generated from the industrial processing of turbot, salmon, trout, seabream and seabass. Source document: Biotechnological Valorization of Food Marine Wastes: Microbial Productions on Peptones Obtained from Aquaculture By-Products. CC BY 4.0 https://b2mbh3cn4a-w6dvs6ghja-uk.a.run.app/audit/270004#claim-300029

oai:citation.is:claim.300024 2026-06-10 claims salmon_biotech

10.0000/citation.is.claim.300024 citation.is thermal processing (105 °C, 60 min) citation.is 2026 ScientificClaim salmon_biotech Insufficient Evidence thermal processing (105 °C, 60 min) Source document: Biotechnological Valorization of Food Marine Wastes: Microbial Productions on Peptones Obtained from Aquaculture By-Products. CC BY 4.0 https://b2mbh3cn4a-w6dvs6ghja-uk.a.run.app/audit/270004#claim-300024

oai:citation.is:claim.300023 2026-06-10 claims salmon_biotech

10.0000/citation.is.claim.300023 citation.is Alcalase hydrolysis (0.1-0.2% v/w, 56-64 °C, pH 8.27-8.98, 3 h) citation.is 2026 ScientificClaim salmon_biotech Supported Alcalase hydrolysis (0.1-0.2% v/w, 56-64 °C, pH 8.27-8.98, 3 h) Source document: Biotechnological Valorization of Food Marine Wastes: Microbial Productions on Peptones Obtained from Aquaculture By-Products. CC BY 4.0 https://b2mbh3cn4a-w6dvs6ghja-uk.a.run.app/audit/270004#claim-300023 https://pubchem.ncbi.nlm.nih.gov/compound/3086051

oai:citation.is:claim.300028 2026-06-10 claims salmon_biotech

10.0000/citation.is.claim.300028 citation.is wastes generated from the industrial processing of turbot, salmon, trout, seabream and seabass. citation.is 2026 ScientificClaim salmon_biotech Insufficient Evidence wastes generated from the industrial processing of turbot, salmon, trout, seabream and seabass. Source document: Biotechnological Valorization of Food Marine Wastes: Microbial Productions on Peptones Obtained from Aquaculture By-Products. CC BY 4.0 https://b2mbh3cn4a-w6dvs6ghja-uk.a.run.app/audit/270004#claim-300028

oai:citation.is:claim.300027 2026-06-10 claims salmon_biotech

10.0000/citation.is.claim.300027 citation.is wastes generated from the industrial processing of turbot, salmon, trout, seabream and seabass. citation.is 2026 ScientificClaim salmon_biotech Insufficient Evidence wastes generated from the industrial processing of turbot, salmon, trout, seabream and seabass. Source document: Biotechnological Valorization of Food Marine Wastes: Microbial Productions on Peptones Obtained from Aquaculture By-Products. CC BY 4.0 https://b2mbh3cn4a-w6dvs6ghja-uk.a.run.app/audit/270004#claim-300027

oai:citation.is:claim.300025 2026-06-10 claims salmon_biotech

10.0000/citation.is.claim.300025 citation.is peptones are produced from the Alcalase hydrolysis (0.1-0.2% v/w, 56-64 °C, pH 8.27-8.98, 3 h) and thermal processing (105 °C, 60 min) of wastes generated from the industrial processing of turbot, sal citation.is 2026 ScientificClaim salmon_biotech Insufficient Evidence peptones are produced from the Alcalase hydrolysis (0.1-0.2% v/w, 56-64 °C, pH 8.27-8.98, 3 h) and thermal processing (105 °C, 60 min) of wastes generated from the industrial processing of turbot, salmon, trout, seabream and seabass. Source document: Biotechnological Valorization of Food Marine Wastes: Microbial Productions on Peptones Obtained from Aquaculture By-Products. CC BY 4.0 https://b2mbh3cn4a-w6dvs6ghja-uk.a.run.app/audit/270004#claim-300025

oai:citation.is:claim.300022 2026-06-10 claims salmon_biotech

10.0000/citation.is.claim.300022 citation.is Alcalase hydrolysis (0.1-0.2% v/w, 56-64 °C, pH 8.27-8.98, 3 h) citation.is 2026 ScientificClaim salmon_biotech Insufficient Evidence Alcalase hydrolysis (0.1-0.2% v/w, 56-64 °C, pH 8.27-8.98, 3 h) Source document: Biotechnological Valorization of Food Marine Wastes: Microbial Productions on Peptones Obtained from Aquaculture By-Products. CC BY 4.0 https://b2mbh3cn4a-w6dvs6ghja-uk.a.run.app/audit/270004#claim-300022

oai:citation.is:claim.300026 2026-06-10 claims salmon_biotech

10.0000/citation.is.claim.300026 citation.is wastes generated from the industrial processing of turbot, salmon, trout, seabream and seabass. citation.is 2026 ScientificClaim salmon_biotech Insufficient Evidence wastes generated from the industrial processing of turbot, salmon, trout, seabream and seabass. Source document: Biotechnological Valorization of Food Marine Wastes: Microbial Productions on Peptones Obtained from Aquaculture By-Products. CC BY 4.0 https://b2mbh3cn4a-w6dvs6ghja-uk.a.run.app/audit/270004#claim-300026

oai:citation.is:claim.300021 2026-06-10 claims salmon_biotech

10.0000/citation.is.claim.300021 citation.is We suggest an enzymatic solution for converting trimethylamine to the odorless trimethylamine N-oxide as a novel strategy to improve the smell quality of marine protein hydrolysates. citation.is 2026 ScientificClaim salmon_biotech Insufficient Evidence We suggest an enzymatic solution for converting trimethylamine to the odorless trimethylamine N-oxide as a novel strategy to improve the smell quality of marine protein hydrolysates. Source document: Use of Flavin-Containing Monooxygenases for Conversion of Trimethylamine in Salmon Protein Hydrolysates. CC BY 4.0 https://b2mbh3cn4a-w6dvs6ghja-uk.a.run.app/audit/270003#claim-300021

oai:citation.is:claim.300013 2026-06-10 claims salmon_biotech

10.0000/citation.is.claim.300013 citation.is Trimethylamine (TMA) is a known contributor to malodor in fish. citation.is 2026 ScientificClaim salmon_biotech Insufficient Evidence Trimethylamine (TMA) is a known contributor to malodor in fish. Source document: Use of Flavin-Containing Monooxygenases for Conversion of Trimethylamine in Salmon Protein Hydrolysates. CC BY 4.0 https://b2mbh3cn4a-w6dvs6ghja-uk.a.run.app/audit/270003#claim-300013

oai:citation.is:claim.300019 2026-06-10 claims salmon_biotech

10.0000/citation.is.claim.300019 citation.is The enzymes were all active from pH 6.0 to 8.5, with functional stability being lowest around the optimal pH. citation.is 2026 ScientificClaim salmon_biotech Insufficient Evidence The enzymes were all active from pH 6.0 to 8.5, with functional stability being lowest around the optimal pH. Source document: Use of Flavin-Containing Monooxygenases for Conversion of Trimethylamine in Salmon Protein Hydrolysates. CC BY 4.0 https://b2mbh3cn4a-w6dvs6ghja-uk.a.run.app/audit/270003#claim-300019

oai:citation.is:claim.300017 2026-06-10 claims salmon_biotech

10.0000/citation.is.claim.300017 citation.is From the 45 bacterial Tmm candidates investigated, eight enzymes from four different taxa were selected for their high activity toward TMA. citation.is 2026 ScientificClaim salmon_biotech Insufficient Evidence From the 45 bacterial Tmm candidates investigated, eight enzymes from four different taxa were selected for their high activity toward TMA. Source document: Use of Flavin-Containing Monooxygenases for Conversion of Trimethylamine in Salmon Protein Hydrolysates. CC BY 4.0 https://b2mbh3cn4a-w6dvs6ghja-uk.a.run.app/audit/270003#claim-300017

oai:citation.is:claim.300020 2026-06-10 claims salmon_biotech

10.0000/citation.is.claim.300020 citation.is All three Tmms, given sufficient NADPH cofactor, were found to generate TMAO in the TMA-rich salmon protein hydrolysate. citation.is 2026 ScientificClaim salmon_biotech Insufficient Evidence All three Tmms, given sufficient NADPH cofactor, were found to generate TMAO in the TMA-rich salmon protein hydrolysate. Source document: Use of Flavin-Containing Monooxygenases for Conversion of Trimethylamine in Salmon Protein Hydrolysates. CC BY 4.0 https://b2mbh3cn4a-w6dvs6ghja-uk.a.run.app/audit/270003#claim-300020

oai:citation.is:claim.300018 2026-06-10 claims salmon_biotech

10.0000/citation.is.claim.300018 citation.is The three most active enzymes were shown to vary in temperature optimum, with the highest being 45°C. citation.is 2026 ScientificClaim salmon_biotech Insufficient Evidence The three most active enzymes were shown to vary in temperature optimum, with the highest being 45°C. Source document: Use of Flavin-Containing Monooxygenases for Conversion of Trimethylamine in Salmon Protein Hydrolysates. CC BY 4.0 https://b2mbh3cn4a-w6dvs6ghja-uk.a.run.app/audit/270003#claim-300018

oai:citation.is:claim.300016 2026-06-10 claims salmon_biotech

10.0000/citation.is.claim.300016 citation.is Purified, recombinant enzymes were assessed for their biocatalytic capacity by monitoring NADPH consumption and TMAO generation. citation.is 2026 ScientificClaim salmon_biotech Insufficient Evidence Purified, recombinant enzymes were assessed for their biocatalytic capacity by monitoring NADPH consumption and TMAO generation. Source document: Use of Flavin-Containing Monooxygenases for Conversion of Trimethylamine in Salmon Protein Hydrolysates. CC BY 4.0 https://b2mbh3cn4a-w6dvs6ghja-uk.a.run.app/audit/270003#claim-300016

oai:citation.is:claim.300014 2026-06-10 claims salmon_biotech

10.0000/citation.is.claim.300014 citation.is we propose a novel enzymatic strategy to convert TMA into the odorless trimethylamine N-oxide (TMAO) using TMA monooxygenases (Tmms). citation.is 2026 ScientificClaim salmon_biotech Insufficient Evidence we propose a novel enzymatic strategy to convert TMA into the odorless trimethylamine N-oxide (TMAO) using TMA monooxygenases (Tmms). Source document: Use of Flavin-Containing Monooxygenases for Conversion of Trimethylamine in Salmon Protein Hydrolysates. CC BY 4.0 https://b2mbh3cn4a-w6dvs6ghja-uk.a.run.app/audit/270003#claim-300014

oai:citation.is:claim.300015 2026-06-10 claims salmon_biotech

10.0000/citation.is.claim.300015 citation.is We identified a diverse set of bacterial Tmms using a sequence similarity network. citation.is 2026 ScientificClaim salmon_biotech Insufficient Evidence We identified a diverse set of bacterial Tmms using a sequence similarity network. Source document: Use of Flavin-Containing Monooxygenases for Conversion of Trimethylamine in Salmon Protein Hydrolysates. CC BY 4.0 https://b2mbh3cn4a-w6dvs6ghja-uk.a.run.app/audit/270003#claim-300015

oai:citation.is:claim.300012 2026-06-10 claims salmon_biotech

10.0000/citation.is.claim.300012 citation.is Secondary product: salmon collagen for nutraceutical, cosmetic, and wound care applications citation.is 2026 ScientificClaim salmon_biotech Insufficient Evidence Secondary product: salmon collagen for nutraceutical, cosmetic, and wound care applications Source document: Salmon-Derived Biotech Product Feasibility Analysis CC BY 4.0 https://b2mbh3cn4a-w6dvs6ghja-uk.a.run.app/audit/270002#claim-300012

oai:citation.is:claim.300011 2026-06-10 claims salmon_biotech

10.0000/citation.is.claim.300011 citation.is Global Atlantic salmon production of approximately 3.0 million tonnes generates 1.5 million tonnes of byproducts annually, containing an estimated 180,000–225,000 tonnes of recoverable protein citation.is 2026 ScientificClaim salmon_biotech Insufficient Evidence Global Atlantic salmon production of approximately 3.0 million tonnes generates 1.5 million tonnes of byproducts annually, containing an estimated 180,000–225,000 tonnes of recoverable protein Source document: Salmon-Derived Biotech Product Feasibility Analysis CC BY 4.0 https://b2mbh3cn4a-w6dvs6ghja-uk.a.run.app/audit/270002#claim-300011

oai:citation.is:claim.300008 2026-06-10 claims salmon_biotech

10.0000/citation.is.claim.300008 citation.is fish are explicitly exempt from transmissible spongiform encephalopathy (TSE) regulations under EU Regulation 722/2012 and FDA guidance because they are not TSE-susceptible species citation.is 2026 ScientificClaim salmon_biotech Insufficient Evidence fish are explicitly exempt from transmissible spongiform encephalopathy (TSE) regulations under EU Regulation 722/2012 and FDA guidance because they are not TSE-susceptible species Source document: Salmon-Derived Biotech Product Feasibility Analysis CC BY 4.0 https://b2mbh3cn4a-w6dvs6ghja-uk.a.run.app/audit/270002#claim-300008

oai:citation.is:claim.300007 2026-06-10 claims salmon_biotech

10.0000/citation.is.claim.300007 citation.is fish-derived peptones match or exceed the performance of bovine and vegetable alternatives citation.is 2026 ScientificClaim salmon_biotech Insufficient Evidence fish-derived peptones match or exceed the performance of bovine and vegetable alternatives Source document: Salmon-Derived Biotech Product Feasibility Analysis CC BY 4.0 https://b2mbh3cn4a-w6dvs6ghja-uk.a.run.app/audit/270002#claim-300007

oai:citation.is:claim.300010 2026-06-10 claims salmon_biotech

10.0000/citation.is.claim.300010 citation.is containing superior methionine and leucine profiles plus omega-3 fatty acids absent from all terrestrial sources citation.is 2026 ScientificClaim salmon_biotech Insufficient Evidence containing superior methionine and leucine profiles plus omega-3 fatty acids absent from all terrestrial sources Source document: Salmon-Derived Biotech Product Feasibility Analysis CC BY 4.0 https://b2mbh3cn4a-w6dvs6ghja-uk.a.run.app/audit/270002#claim-300010

oai:citation.is:claim.300009 2026-06-10 claims salmon_biotech

10.0000/citation.is.claim.300009 citation.is salmon head peptone performs equivalently to commercial animal peptone in recombinant protein production (p > 0.05) and actually outperforms vegetable peptone citation.is 2026 ScientificClaim salmon_biotech Insufficient Evidence salmon head peptone performs equivalently to commercial animal peptone in recombinant protein production (p > 0.05) and actually outperforms vegetable peptone Source document: Salmon-Derived Biotech Product Feasibility Analysis CC BY 4.0 https://b2mbh3cn4a-w6dvs6ghja-uk.a.run.app/audit/270002#claim-300009

oai:citation.is:claim.300004 2026-06-10 claims salmon_biotech

10.0000/citation.is.claim.300004 citation.is containing superior methionine and leucine profiles plus omega-3 fatty acids absent from all terrestrial sources citation.is 2026 ScientificClaim salmon_biotech Insufficient Evidence containing superior methionine and leucine profiles plus omega-3 fatty acids absent from all terrestrial sources Source document: Salmon-Derived Biotech Product Feasibility Analysis CC BY 4.0 https://b2mbh3cn4a-w6dvs6ghja-uk.a.run.app/audit/270001#claim-300004

oai:citation.is:claim.300003 2026-06-10 claims salmon_biotech

10.0000/citation.is.claim.300003 citation.is salmon head peptone performs equivalently to commercial animal peptone in recombinant protein production (p > 0.05) and actually outperforms vegetable peptone citation.is 2026 ScientificClaim salmon_biotech Insufficient Evidence salmon head peptone performs equivalently to commercial animal peptone in recombinant protein production (p > 0.05) and actually outperforms vegetable peptone Source document: Salmon-Derived Biotech Product Feasibility Analysis CC BY 4.0 https://b2mbh3cn4a-w6dvs6ghja-uk.a.run.app/audit/270001#claim-300003

oai:citation.is:claim.300006 2026-06-10 claims salmon_biotech

10.0000/citation.is.claim.300006 citation.is Sequential extraction recovers collagen from skin and bones first, then hydrolyzes residual protein into peptone citation.is 2026 ScientificClaim salmon_biotech Insufficient Evidence Sequential extraction recovers collagen from skin and bones first, then hydrolyzes residual protein into peptone Source document: Salmon-Derived Biotech Product Feasibility Analysis CC BY 4.0 https://b2mbh3cn4a-w6dvs6ghja-uk.a.run.app/audit/270001#claim-300006

oai:citation.is:claim.300005 2026-06-10 claims salmon_biotech

10.0000/citation.is.claim.300005 citation.is Global Atlantic salmon production of approximately 3.0 million tonnes generates 1.5 million tonnes of byproducts annually, containing an estimated 180,000–225,000 tonnes of recoverable protein citation.is 2026 ScientificClaim salmon_biotech Insufficient Evidence Global Atlantic salmon production of approximately 3.0 million tonnes generates 1.5 million tonnes of byproducts annually, containing an estimated 180,000–225,000 tonnes of recoverable protein Source document: Salmon-Derived Biotech Product Feasibility Analysis CC BY 4.0 https://b2mbh3cn4a-w6dvs6ghja-uk.a.run.app/audit/270001#claim-300005

oai:citation.is:claim.300001 2026-06-10 claims salmon_biotech

10.0000/citation.is.claim.300001 citation.is fish-derived peptones match or exceed the performance of bovine and vegetable alternatives citation.is 2026 ScientificClaim salmon_biotech Insufficient Evidence fish-derived peptones match or exceed the performance of bovine and vegetable alternatives Source document: Salmon-Derived Biotech Product Feasibility Analysis CC BY 4.0 https://b2mbh3cn4a-w6dvs6ghja-uk.a.run.app/audit/270001#claim-300001

oai:citation.is:claim.121600 2026-06-03 claims structural_biology

10.0000/citation.is.claim.121600 citation.is It is also important to acknowledge that cycloviolacins, including cycloviolacin O13, have been reported in the literature as membrane-active peptides with antimicrobial and cytotoxic properties, part citation.is 2026 ScientificClaim structural_biology Out of Scope It is also important to acknowledge that cycloviolacins, including cycloviolacin O13, have been reported in the literature as membrane-active peptides with antimicrobial and cytotoxic properties, particularly at higher concentrations50–52. Source document: Computational screening of AI-derived cyclotides as putative VEGFR2 binders for wound-site angiogenesis. CC BY 4.0 https://b2mbh3cn4a-w6dvs6ghja-uk.a.run.app/audit/60110#claim-121600

oai:citation.is:claim.121599 2026-06-03 claims structural_biology

10.0000/citation.is.claim.121599 citation.is In direct contrast, apo-VEGFR2 showed larger drift and expansion (RMSD 0.30–0.55 nm, excursions to 0.60 nm; Rg rising toward 1.82–1.86 nm; 150–200 H-bonds), supporting a ligand-associated stabilizatio citation.is 2026 ScientificClaim structural_biology Out of Scope In direct contrast, apo-VEGFR2 showed larger drift and expansion (RMSD 0.30–0.55 nm, excursions to 0.60 nm; Rg rising toward 1.82–1.86 nm; 150–200 H-bonds), supporting a ligand-associated stabilization of the predicted pocket. Source document: Computational screening of AI-derived cyclotides as putative VEGFR2 binders for wound-site angiogenesis. CC BY 4.0 https://b2mbh3cn4a-w6dvs6ghja-uk.a.run.app/audit/60110#claim-121599

oai:citation.is:claim.121598 2026-06-03 claims structural_biology

10.0000/citation.is.claim.121598 citation.is In direct contrast, apo-VEGFR2 showed larger drift and expansion (RMSD 0.30–0.55 nm, excursions to 0.60 nm; Rg rising toward 1.82–1.86 nm; 150–200 H-bonds), supporting a ligand-associated stabilizatio citation.is 2026 ScientificClaim structural_biology Out of Scope In direct contrast, apo-VEGFR2 showed larger drift and expansion (RMSD 0.30–0.55 nm, excursions to 0.60 nm; Rg rising toward 1.82–1.86 nm; 150–200 H-bonds), supporting a ligand-associated stabilization of the predicted pocket. Source document: Computational screening of AI-derived cyclotides as putative VEGFR2 binders for wound-site angiogenesis. CC BY 4.0 https://b2mbh3cn4a-w6dvs6ghja-uk.a.run.app/audit/60110#claim-121598

oai:citation.is:claim.121597 2026-06-03 claims structural_biology

10.0000/citation.is.claim.121597 citation.is In direct contrast, apo-VEGFR2 showed larger drift and expansion (RMSD 0.30–0.55 nm, excursions to 0.60 nm; Rg rising toward 1.82–1.86 nm; 150–200 H-bonds), supporting a ligand-associated stabilizatio citation.is 2026 ScientificClaim structural_biology Out of Scope In direct contrast, apo-VEGFR2 showed larger drift and expansion (RMSD 0.30–0.55 nm, excursions to 0.60 nm; Rg rising toward 1.82–1.86 nm; 150–200 H-bonds), supporting a ligand-associated stabilization of the predicted pocket. Source document: Computational screening of AI-derived cyclotides as putative VEGFR2 binders for wound-site angiogenesis. CC BY 4.0 https://b2mbh3cn4a-w6dvs6ghja-uk.a.run.app/audit/60110#claim-121597

oai:citation.is:claim.121596 2026-06-03 claims structural_biology

10.0000/citation.is.claim.121596 citation.is In direct contrast, apo-VEGFR2 showed larger drift and expansion (RMSD 0.30–0.55 nm, excursions to 0.60 nm; Rg rising toward 1.82–1.86 nm; 150–200 H-bonds), supporting a ligand-associated stabilizatio citation.is 2026 ScientificClaim structural_biology Ambiguous In direct contrast, apo-VEGFR2 showed larger drift and expansion (RMSD 0.30–0.55 nm, excursions to 0.60 nm; Rg rising toward 1.82–1.86 nm; 150–200 H-bonds), supporting a ligand-associated stabilization of the predicted pocket. Source document: Computational screening of AI-derived cyclotides as putative VEGFR2 binders for wound-site angiogenesis. CC BY 4.0 https://b2mbh3cn4a-w6dvs6ghja-uk.a.run.app/audit/60110#claim-121596 https://www.rcsb.org/search?query=VEGFR2

oai:citation.is:claim.121595 2026-06-03 claims structural_biology

10.0000/citation.is.claim.121595 citation.is In our computational pipeline, cycloviolacin O13 emerged as the lead cyclotide because it combined the strongest docking performance (HADDOCK score − 84.7, ligand RMSD 0.8 nm) with long-timescale comp citation.is 2026 ScientificClaim structural_biology Out of Scope In our computational pipeline, cycloviolacin O13 emerged as the lead cyclotide because it combined the strongest docking performance (HADDOCK score − 84.7, ligand RMSD 0.8 nm) with long-timescale complex persistence during 500 ns MD: complex RMSD stabilized at 0.25–0.45 nm, the binding pose remained tight (ligand RMSD 0.20–0.30 nm), the complex compacted (Rg drifting from 1.83 to 1.88 nm early to 1.72–1.76 nm after ~ 150 ns), and hydrogen-bonding remained sustained (200–260 H-bonds). Source document: Computational screening of AI-derived cyclotides as putative VEGFR2 binders for wound-site angiogenesis. CC BY 4.0 https://b2mbh3cn4a-w6dvs6ghja-uk.a.run.app/audit/60110#claim-121595

oai:citation.is:claim.121594 2026-06-03 claims structural_biology

10.0000/citation.is.claim.121594 citation.is In our computational pipeline, cycloviolacin O13 emerged as the lead cyclotide because it combined the strongest docking performance (HADDOCK score − 84.7, ligand RMSD 0.8 nm) with long-timescale comp citation.is 2026 ScientificClaim structural_biology Out of Scope In our computational pipeline, cycloviolacin O13 emerged as the lead cyclotide because it combined the strongest docking performance (HADDOCK score − 84.7, ligand RMSD 0.8 nm) with long-timescale complex persistence during 500 ns MD: complex RMSD stabilized at 0.25–0.45 nm, the binding pose remained tight (ligand RMSD 0.20–0.30 nm), the complex compacted (Rg drifting from 1.83 to 1.88 nm early to 1.72–1.76 nm after ~ 150 ns), and hydrogen-bonding remained sustained (200–260 H-bonds). Source document: Computational screening of AI-derived cyclotides as putative VEGFR2 binders for wound-site angiogenesis. CC BY 4.0 https://b2mbh3cn4a-w6dvs6ghja-uk.a.run.app/audit/60110#claim-121594