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

Abstract 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 strain...

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Main Authors: EFSA Panel on Additives and Products or Substances used in Animal Feed (FEEDAP), Guido Rychen, Gabriele Aquilina, Giovanna Azimonti, Vasileios Bampidis, Maria de Lourdes Bastos, Georges Bories, Andrew Chesson, Pier Sandro Cocconcelli, Gerhard Flachowsky, Jürgen Gropp, Boris Kolar, Maryline Kouba, Secundino López Puente, Marta López‐Alonso, Alberto Mantovani, Baltasar Mayo, Fernando Ramos, Maria Saarela, Roberto Edoardo Villa, Robert John Wallace, Pieter Wester, Paul Brantom, Noël Albert Dierick, Jaime Aguilera, Montserrat Anguita
Format: Article
Language:English
Published: Wiley 2018-04-01
Series:EFSA Journal
Subjects:
Online Access:https://doi.org/10.2903/j.efsa.2018.5224
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author EFSA Panel on Additives and Products or Substances used in Animal Feed (FEEDAP)
Guido Rychen
Gabriele Aquilina
Giovanna Azimonti
Vasileios Bampidis
Maria de Lourdes Bastos
Georges Bories
Andrew Chesson
Pier Sandro Cocconcelli
Gerhard Flachowsky
Jürgen Gropp
Boris Kolar
Maryline Kouba
Secundino López Puente
Marta López‐Alonso
Alberto Mantovani
Baltasar Mayo
Fernando Ramos
Maria Saarela
Roberto Edoardo Villa
Robert John Wallace
Pieter Wester
Paul Brantom
Noël Albert Dierick
Jaime Aguilera
Montserrat Anguita
author_facet EFSA Panel on Additives and Products or Substances used in Animal Feed (FEEDAP)
Guido Rychen
Gabriele Aquilina
Giovanna Azimonti
Vasileios Bampidis
Maria de Lourdes Bastos
Georges Bories
Andrew Chesson
Pier Sandro Cocconcelli
Gerhard Flachowsky
Jürgen Gropp
Boris Kolar
Maryline Kouba
Secundino López Puente
Marta López‐Alonso
Alberto Mantovani
Baltasar Mayo
Fernando Ramos
Maria Saarela
Roberto Edoardo Villa
Robert John Wallace
Pieter Wester
Paul Brantom
Noël Albert Dierick
Jaime Aguilera
Montserrat Anguita
author_sort EFSA Panel on Additives and Products or Substances used in Animal Feed (FEEDAP)
collection DOAJ
description Abstract 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 doaj.art-416d364581a9478a846ee5d1dace2b332022-12-21T22:30:09ZengWileyEFSA Journal1831-47322018-04-01164n/an/a10.2903/j.efsa.2018.5224Safety 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 speciesEFSA Panel on Additives and Products or Substances used in Animal Feed (FEEDAP)Guido RychenGabriele AquilinaGiovanna AzimontiVasileios BampidisMaria de Lourdes BastosGeorges BoriesAndrew ChessonPier Sandro CocconcelliGerhard FlachowskyJürgen GroppBoris KolarMaryline KoubaSecundino López PuenteMarta López‐AlonsoAlberto MantovaniBaltasar MayoFernando RamosMaria SaarelaRoberto Edoardo VillaRobert John WallacePieter WesterPaul BrantomNoël Albert DierickJaime AguileraMontserrat AnguitaAbstract 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.https://doi.org/10.2903/j.efsa.2018.5224technological additivessilage additivesafetyefficacyenzymes
spellingShingle EFSA Panel on Additives and Products or Substances used in Animal Feed (FEEDAP)
Guido Rychen
Gabriele Aquilina
Giovanna Azimonti
Vasileios Bampidis
Maria de Lourdes Bastos
Georges Bories
Andrew Chesson
Pier Sandro Cocconcelli
Gerhard Flachowsky
Jürgen Gropp
Boris Kolar
Maryline Kouba
Secundino López Puente
Marta López‐Alonso
Alberto Mantovani
Baltasar Mayo
Fernando Ramos
Maria Saarela
Roberto Edoardo Villa
Robert John Wallace
Pieter Wester
Paul Brantom
Noël Albert Dierick
Jaime Aguilera
Montserrat Anguita
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
EFSA Journal
technological additives
silage additive
safety
efficacy
enzymes
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 technological additives
silage additive
safety
efficacy
enzymes
url https://doi.org/10.2903/j.efsa.2018.5224
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