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Safety and efficacy of alpha‐amylase from Bacillus amyloliquefaciens DSM 9553, Bacillus amyloliquefaciens NCIMB 30251, Aspergillus oryzae CBS 585.94 and Aspergillus oryzae ATTC SD‐5374, endo‐1,4‐beta‐glucanase from Trichoderma reesei ATCC PTA‐10001, Trichoderma reesei ATCC SD‐6331 and Aspergillus niger CBS 120604, endo‐1,4‐beta‐xylanase from Trichoderma koningii MUCL 39203 and Trichoderma citrinoviride CBS 614.94 and endo‐1,3(4)‐beta‐glucanase from Aspergillus tubingensis MUCL 39199 as silage additives for all animal species

A total of 11 enzymes were assessed including alpha‐amylase, endo‐1,4‐beta‐glucanase, endo‐1,4‐beta‐xylanase and endo‐1,3(4)‐beta‐glucanase as silage additives for all animal species. These enzymes are obtained by fermentation of bacterial or fungi non‐genetically modified production strains. Throug...

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Autores principales: Rychen, Guido, Aquilina, Gabriele, Azimonti, Giovanna, Bampidis, Vasileios, Bastos, Maria de Lourdes, Bories, Georges, Chesson, Andrew, Cocconcelli, Pier Sandro, Flachowsky, Gerhard, Gropp, Jürgen, Kolar, Boris, Kouba, Maryline, López Puente, Secundino, López‐Alonso, Marta, Mantovani, Alberto, Mayo, Baltasar, Ramos, Fernando, Saarela, Maria, Villa, Roberto Edoardo, Wallace, Robert John, Wester, Pieter, Brantom, Paul, Dierick, Noël Albert, Aguilera, Jaime, Anguita, Montserrat
Formato: Online Artículo Texto
Lenguaje:English
Publicado: John Wiley and Sons Inc. 2018
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7009625/
https://www.ncbi.nlm.nih.gov/pubmed/32625864
http://dx.doi.org/10.2903/j.efsa.2018.5224
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author Rychen, Guido
Aquilina, Gabriele
Azimonti, Giovanna
Bampidis, Vasileios
Bastos, Maria de Lourdes
Bories, Georges
Chesson, Andrew
Cocconcelli, Pier Sandro
Flachowsky, Gerhard
Gropp, Jürgen
Kolar, Boris
Kouba, Maryline
López Puente, Secundino
López‐Alonso, Marta
Mantovani, Alberto
Mayo, Baltasar
Ramos, Fernando
Saarela, Maria
Villa, Roberto Edoardo
Wallace, Robert John
Wester, Pieter
Brantom, Paul
Dierick, Noël Albert
Aguilera, Jaime
Anguita, Montserrat
author_facet Rychen, Guido
Aquilina, Gabriele
Azimonti, Giovanna
Bampidis, Vasileios
Bastos, Maria de Lourdes
Bories, Georges
Chesson, Andrew
Cocconcelli, Pier Sandro
Flachowsky, Gerhard
Gropp, Jürgen
Kolar, Boris
Kouba, Maryline
López Puente, Secundino
López‐Alonso, Marta
Mantovani, Alberto
Mayo, Baltasar
Ramos, Fernando
Saarela, Maria
Villa, Roberto Edoardo
Wallace, Robert John
Wester, Pieter
Brantom, Paul
Dierick, Noël Albert
Aguilera, Jaime
Anguita, Montserrat
collection PubMed
description A total of 11 enzymes were assessed including alpha‐amylase, endo‐1,4‐beta‐glucanase, endo‐1,4‐beta‐xylanase and endo‐1,3(4)‐beta‐glucanase as silage additives for all animal species. These enzymes are obtained by fermentation of bacterial or fungi non‐genetically modified production strains. Throughout information regarding the production strains of each product were provided, including the origin and history of modifications and allowing their identification. The identification was conclusive for 8 of 10 production strains. For three of the strains, more information/data would still be required in order to conclude. Three of the amylases are produced by bacterial strains that belong to a species that is considered by EFSA to be suitable for the Qualified Presumption of Safety approach to safety assessment. The identity of the strains has been established and the qualifications were met, and consequently, those products were regarded as safe. For the products derived from fungal strains, the strains or resulting products were tested for the presence of secondary metabolites which could be of toxicological concern. These were found to be below the limits of detection or the strain not capable of producing them. Considering all the information provided by the applicant, the Panel concluded that these products can be regarded as safe for the target species, consumer and the environment. In the absence of data, the Panel could not conclude on the skin and eye irritancy or skin sensitisation potential of the products under evaluation. These products should be considered to have the potential to be a respiratory sensitiser. For some of the products under evaluation, the Panel on Additives and Products or Substances used in Animal Feed (FEEDAP) concluded that they have a potential to improve the characteristic of the silage material; for some other products, the Panel could not conclude on their efficacy.
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spelling pubmed-70096252020-07-02 Safety and efficacy of alpha‐amylase from Bacillus amyloliquefaciens DSM 9553, Bacillus amyloliquefaciens NCIMB 30251, Aspergillus oryzae CBS 585.94 and Aspergillus oryzae ATTC SD‐5374, endo‐1,4‐beta‐glucanase from Trichoderma reesei ATCC PTA‐10001, Trichoderma reesei ATCC SD‐6331 and Aspergillus niger CBS 120604, endo‐1,4‐beta‐xylanase from Trichoderma koningii MUCL 39203 and Trichoderma citrinoviride CBS 614.94 and endo‐1,3(4)‐beta‐glucanase from Aspergillus tubingensis MUCL 39199 as silage additives for all animal species Rychen, Guido Aquilina, Gabriele Azimonti, Giovanna Bampidis, Vasileios Bastos, Maria de Lourdes Bories, Georges Chesson, Andrew Cocconcelli, Pier Sandro Flachowsky, Gerhard Gropp, Jürgen Kolar, Boris Kouba, Maryline López Puente, Secundino López‐Alonso, Marta Mantovani, Alberto Mayo, Baltasar Ramos, Fernando Saarela, Maria Villa, Roberto Edoardo Wallace, Robert John Wester, Pieter Brantom, Paul Dierick, Noël Albert Aguilera, Jaime Anguita, Montserrat EFSA J Scientific Opinion A total of 11 enzymes were assessed including alpha‐amylase, endo‐1,4‐beta‐glucanase, endo‐1,4‐beta‐xylanase and endo‐1,3(4)‐beta‐glucanase as silage additives for all animal species. These enzymes are obtained by fermentation of bacterial or fungi non‐genetically modified production strains. Throughout information regarding the production strains of each product were provided, including the origin and history of modifications and allowing their identification. The identification was conclusive for 8 of 10 production strains. For three of the strains, more information/data would still be required in order to conclude. Three of the amylases are produced by bacterial strains that belong to a species that is considered by EFSA to be suitable for the Qualified Presumption of Safety approach to safety assessment. The identity of the strains has been established and the qualifications were met, and consequently, those products were regarded as safe. For the products derived from fungal strains, the strains or resulting products were tested for the presence of secondary metabolites which could be of toxicological concern. These were found to be below the limits of detection or the strain not capable of producing them. Considering all the information provided by the applicant, the Panel concluded that these products can be regarded as safe for the target species, consumer and the environment. In the absence of data, the Panel could not conclude on the skin and eye irritancy or skin sensitisation potential of the products under evaluation. These products should be considered to have the potential to be a respiratory sensitiser. For some of the products under evaluation, the Panel on Additives and Products or Substances used in Animal Feed (FEEDAP) concluded that they have a potential to improve the characteristic of the silage material; for some other products, the Panel could not conclude on their efficacy. John Wiley and Sons Inc. 2018-04-24 /pmc/articles/PMC7009625/ /pubmed/32625864 http://dx.doi.org/10.2903/j.efsa.2018.5224 Text en © 2018 European Food Safety Authority. EFSA Journal published by John Wiley and Sons Ltd on behalf of European Food Safety Authority. This is an open access article under the terms of the http://creativecommons.org/licenses/by-nd/4.0/ License, which permits use and distribution in any medium, provided the original work is properly cited and no modifications or adaptations are made.
spellingShingle Scientific Opinion
Rychen, Guido
Aquilina, Gabriele
Azimonti, Giovanna
Bampidis, Vasileios
Bastos, Maria de Lourdes
Bories, Georges
Chesson, Andrew
Cocconcelli, Pier Sandro
Flachowsky, Gerhard
Gropp, Jürgen
Kolar, Boris
Kouba, Maryline
López Puente, Secundino
López‐Alonso, Marta
Mantovani, Alberto
Mayo, Baltasar
Ramos, Fernando
Saarela, Maria
Villa, Roberto Edoardo
Wallace, Robert John
Wester, Pieter
Brantom, Paul
Dierick, Noël Albert
Aguilera, Jaime
Anguita, Montserrat
Safety and efficacy of alpha‐amylase from Bacillus amyloliquefaciens DSM 9553, Bacillus amyloliquefaciens NCIMB 30251, Aspergillus oryzae CBS 585.94 and Aspergillus oryzae ATTC SD‐5374, endo‐1,4‐beta‐glucanase from Trichoderma reesei ATCC PTA‐10001, Trichoderma reesei ATCC SD‐6331 and Aspergillus niger CBS 120604, endo‐1,4‐beta‐xylanase from Trichoderma koningii MUCL 39203 and Trichoderma citrinoviride CBS 614.94 and endo‐1,3(4)‐beta‐glucanase from Aspergillus tubingensis MUCL 39199 as silage additives for all animal species
title Safety and efficacy of alpha‐amylase from Bacillus amyloliquefaciens DSM 9553, Bacillus amyloliquefaciens NCIMB 30251, Aspergillus oryzae CBS 585.94 and Aspergillus oryzae ATTC SD‐5374, endo‐1,4‐beta‐glucanase from Trichoderma reesei ATCC PTA‐10001, Trichoderma reesei ATCC SD‐6331 and Aspergillus niger CBS 120604, endo‐1,4‐beta‐xylanase from Trichoderma koningii MUCL 39203 and Trichoderma citrinoviride CBS 614.94 and endo‐1,3(4)‐beta‐glucanase from Aspergillus tubingensis MUCL 39199 as silage additives for all animal species
title_full Safety and efficacy of alpha‐amylase from Bacillus amyloliquefaciens DSM 9553, Bacillus amyloliquefaciens NCIMB 30251, Aspergillus oryzae CBS 585.94 and Aspergillus oryzae ATTC SD‐5374, endo‐1,4‐beta‐glucanase from Trichoderma reesei ATCC PTA‐10001, Trichoderma reesei ATCC SD‐6331 and Aspergillus niger CBS 120604, endo‐1,4‐beta‐xylanase from Trichoderma koningii MUCL 39203 and Trichoderma citrinoviride CBS 614.94 and endo‐1,3(4)‐beta‐glucanase from Aspergillus tubingensis MUCL 39199 as silage additives for all animal species
title_fullStr Safety and efficacy of alpha‐amylase from Bacillus amyloliquefaciens DSM 9553, Bacillus amyloliquefaciens NCIMB 30251, Aspergillus oryzae CBS 585.94 and Aspergillus oryzae ATTC SD‐5374, endo‐1,4‐beta‐glucanase from Trichoderma reesei ATCC PTA‐10001, Trichoderma reesei ATCC SD‐6331 and Aspergillus niger CBS 120604, endo‐1,4‐beta‐xylanase from Trichoderma koningii MUCL 39203 and Trichoderma citrinoviride CBS 614.94 and endo‐1,3(4)‐beta‐glucanase from Aspergillus tubingensis MUCL 39199 as silage additives for all animal species
title_full_unstemmed Safety and efficacy of alpha‐amylase from Bacillus amyloliquefaciens DSM 9553, Bacillus amyloliquefaciens NCIMB 30251, Aspergillus oryzae CBS 585.94 and Aspergillus oryzae ATTC SD‐5374, endo‐1,4‐beta‐glucanase from Trichoderma reesei ATCC PTA‐10001, Trichoderma reesei ATCC SD‐6331 and Aspergillus niger CBS 120604, endo‐1,4‐beta‐xylanase from Trichoderma koningii MUCL 39203 and Trichoderma citrinoviride CBS 614.94 and endo‐1,3(4)‐beta‐glucanase from Aspergillus tubingensis MUCL 39199 as silage additives for all animal species
title_short Safety and efficacy of alpha‐amylase from Bacillus amyloliquefaciens DSM 9553, Bacillus amyloliquefaciens NCIMB 30251, Aspergillus oryzae CBS 585.94 and Aspergillus oryzae ATTC SD‐5374, endo‐1,4‐beta‐glucanase from Trichoderma reesei ATCC PTA‐10001, Trichoderma reesei ATCC SD‐6331 and Aspergillus niger CBS 120604, endo‐1,4‐beta‐xylanase from Trichoderma koningii MUCL 39203 and Trichoderma citrinoviride CBS 614.94 and endo‐1,3(4)‐beta‐glucanase from Aspergillus tubingensis MUCL 39199 as silage additives for all animal species
title_sort safety and efficacy of alpha‐amylase from bacillus amyloliquefaciens dsm 9553, bacillus amyloliquefaciens ncimb 30251, aspergillus oryzae cbs 585.94 and aspergillus oryzae attc sd‐5374, endo‐1,4‐beta‐glucanase from trichoderma reesei atcc pta‐10001, trichoderma reesei atcc sd‐6331 and aspergillus niger cbs 120604, endo‐1,4‐beta‐xylanase from trichoderma koningii mucl 39203 and trichoderma citrinoviride cbs 614.94 and endo‐1,3(4)‐beta‐glucanase from aspergillus tubingensis mucl 39199 as silage additives for all animal species
topic Scientific Opinion
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7009625/
https://www.ncbi.nlm.nih.gov/pubmed/32625864
http://dx.doi.org/10.2903/j.efsa.2018.5224
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