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...
Main Authors: | , , , , , , , , , , , , , , , , , , , , , , , , , |
---|---|
Format: | Article |
Language: | English |
Published: |
Wiley
2018-04-01
|
Series: | EFSA Journal |
Subjects: | |
Online Access: | https://doi.org/10.2903/j.efsa.2018.5224 |
_version_ | 1818603756976078848 |
---|---|
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. |
first_indexed | 2024-12-16T13:28:14Z |
format | Article |
id | doaj.art-416d364581a9478a846ee5d1dace2b33 |
institution | Directory Open Access Journal |
issn | 1831-4732 |
language | English |
last_indexed | 2024-12-16T13:28:14Z |
publishDate | 2018-04-01 |
publisher | Wiley |
record_format | Article |
series | EFSA Journal |
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 |
work_keys_str_mv | AT efsapanelonadditivesandproductsorsubstancesusedinanimalfeedfeedap safetyandefficacyofalphaamylasefrombacillusamyloliquefaciensdsm9553bacillusamyloliquefaciensncimb30251aspergillusoryzaecbs58594andaspergillusoryzaeattcsd5374endo14betaglucanasefromtrichodermareeseiatccpta10001trichodermareeseiatccsd6331andaspergillusniger AT guidorychen safetyandefficacyofalphaamylasefrombacillusamyloliquefaciensdsm9553bacillusamyloliquefaciensncimb30251aspergillusoryzaecbs58594andaspergillusoryzaeattcsd5374endo14betaglucanasefromtrichodermareeseiatccpta10001trichodermareeseiatccsd6331andaspergillusniger AT gabrieleaquilina safetyandefficacyofalphaamylasefrombacillusamyloliquefaciensdsm9553bacillusamyloliquefaciensncimb30251aspergillusoryzaecbs58594andaspergillusoryzaeattcsd5374endo14betaglucanasefromtrichodermareeseiatccpta10001trichodermareeseiatccsd6331andaspergillusniger AT giovannaazimonti safetyandefficacyofalphaamylasefrombacillusamyloliquefaciensdsm9553bacillusamyloliquefaciensncimb30251aspergillusoryzaecbs58594andaspergillusoryzaeattcsd5374endo14betaglucanasefromtrichodermareeseiatccpta10001trichodermareeseiatccsd6331andaspergillusniger AT vasileiosbampidis safetyandefficacyofalphaamylasefrombacillusamyloliquefaciensdsm9553bacillusamyloliquefaciensncimb30251aspergillusoryzaecbs58594andaspergillusoryzaeattcsd5374endo14betaglucanasefromtrichodermareeseiatccpta10001trichodermareeseiatccsd6331andaspergillusniger AT mariadelourdesbastos safetyandefficacyofalphaamylasefrombacillusamyloliquefaciensdsm9553bacillusamyloliquefaciensncimb30251aspergillusoryzaecbs58594andaspergillusoryzaeattcsd5374endo14betaglucanasefromtrichodermareeseiatccpta10001trichodermareeseiatccsd6331andaspergillusniger AT georgesbories safetyandefficacyofalphaamylasefrombacillusamyloliquefaciensdsm9553bacillusamyloliquefaciensncimb30251aspergillusoryzaecbs58594andaspergillusoryzaeattcsd5374endo14betaglucanasefromtrichodermareeseiatccpta10001trichodermareeseiatccsd6331andaspergillusniger AT andrewchesson safetyandefficacyofalphaamylasefrombacillusamyloliquefaciensdsm9553bacillusamyloliquefaciensncimb30251aspergillusoryzaecbs58594andaspergillusoryzaeattcsd5374endo14betaglucanasefromtrichodermareeseiatccpta10001trichodermareeseiatccsd6331andaspergillusniger AT piersandrococconcelli safetyandefficacyofalphaamylasefrombacillusamyloliquefaciensdsm9553bacillusamyloliquefaciensncimb30251aspergillusoryzaecbs58594andaspergillusoryzaeattcsd5374endo14betaglucanasefromtrichodermareeseiatccpta10001trichodermareeseiatccsd6331andaspergillusniger AT gerhardflachowsky safetyandefficacyofalphaamylasefrombacillusamyloliquefaciensdsm9553bacillusamyloliquefaciensncimb30251aspergillusoryzaecbs58594andaspergillusoryzaeattcsd5374endo14betaglucanasefromtrichodermareeseiatccpta10001trichodermareeseiatccsd6331andaspergillusniger AT jurgengropp safetyandefficacyofalphaamylasefrombacillusamyloliquefaciensdsm9553bacillusamyloliquefaciensncimb30251aspergillusoryzaecbs58594andaspergillusoryzaeattcsd5374endo14betaglucanasefromtrichodermareeseiatccpta10001trichodermareeseiatccsd6331andaspergillusniger AT boriskolar safetyandefficacyofalphaamylasefrombacillusamyloliquefaciensdsm9553bacillusamyloliquefaciensncimb30251aspergillusoryzaecbs58594andaspergillusoryzaeattcsd5374endo14betaglucanasefromtrichodermareeseiatccpta10001trichodermareeseiatccsd6331andaspergillusniger AT marylinekouba safetyandefficacyofalphaamylasefrombacillusamyloliquefaciensdsm9553bacillusamyloliquefaciensncimb30251aspergillusoryzaecbs58594andaspergillusoryzaeattcsd5374endo14betaglucanasefromtrichodermareeseiatccpta10001trichodermareeseiatccsd6331andaspergillusniger AT secundinolopezpuente safetyandefficacyofalphaamylasefrombacillusamyloliquefaciensdsm9553bacillusamyloliquefaciensncimb30251aspergillusoryzaecbs58594andaspergillusoryzaeattcsd5374endo14betaglucanasefromtrichodermareeseiatccpta10001trichodermareeseiatccsd6331andaspergillusniger AT martalopezalonso safetyandefficacyofalphaamylasefrombacillusamyloliquefaciensdsm9553bacillusamyloliquefaciensncimb30251aspergillusoryzaecbs58594andaspergillusoryzaeattcsd5374endo14betaglucanasefromtrichodermareeseiatccpta10001trichodermareeseiatccsd6331andaspergillusniger AT albertomantovani safetyandefficacyofalphaamylasefrombacillusamyloliquefaciensdsm9553bacillusamyloliquefaciensncimb30251aspergillusoryzaecbs58594andaspergillusoryzaeattcsd5374endo14betaglucanasefromtrichodermareeseiatccpta10001trichodermareeseiatccsd6331andaspergillusniger AT baltasarmayo safetyandefficacyofalphaamylasefrombacillusamyloliquefaciensdsm9553bacillusamyloliquefaciensncimb30251aspergillusoryzaecbs58594andaspergillusoryzaeattcsd5374endo14betaglucanasefromtrichodermareeseiatccpta10001trichodermareeseiatccsd6331andaspergillusniger AT fernandoramos safetyandefficacyofalphaamylasefrombacillusamyloliquefaciensdsm9553bacillusamyloliquefaciensncimb30251aspergillusoryzaecbs58594andaspergillusoryzaeattcsd5374endo14betaglucanasefromtrichodermareeseiatccpta10001trichodermareeseiatccsd6331andaspergillusniger AT mariasaarela safetyandefficacyofalphaamylasefrombacillusamyloliquefaciensdsm9553bacillusamyloliquefaciensncimb30251aspergillusoryzaecbs58594andaspergillusoryzaeattcsd5374endo14betaglucanasefromtrichodermareeseiatccpta10001trichodermareeseiatccsd6331andaspergillusniger AT robertoedoardovilla safetyandefficacyofalphaamylasefrombacillusamyloliquefaciensdsm9553bacillusamyloliquefaciensncimb30251aspergillusoryzaecbs58594andaspergillusoryzaeattcsd5374endo14betaglucanasefromtrichodermareeseiatccpta10001trichodermareeseiatccsd6331andaspergillusniger AT robertjohnwallace safetyandefficacyofalphaamylasefrombacillusamyloliquefaciensdsm9553bacillusamyloliquefaciensncimb30251aspergillusoryzaecbs58594andaspergillusoryzaeattcsd5374endo14betaglucanasefromtrichodermareeseiatccpta10001trichodermareeseiatccsd6331andaspergillusniger AT pieterwester safetyandefficacyofalphaamylasefrombacillusamyloliquefaciensdsm9553bacillusamyloliquefaciensncimb30251aspergillusoryzaecbs58594andaspergillusoryzaeattcsd5374endo14betaglucanasefromtrichodermareeseiatccpta10001trichodermareeseiatccsd6331andaspergillusniger AT paulbrantom safetyandefficacyofalphaamylasefrombacillusamyloliquefaciensdsm9553bacillusamyloliquefaciensncimb30251aspergillusoryzaecbs58594andaspergillusoryzaeattcsd5374endo14betaglucanasefromtrichodermareeseiatccpta10001trichodermareeseiatccsd6331andaspergillusniger AT noelalbertdierick safetyandefficacyofalphaamylasefrombacillusamyloliquefaciensdsm9553bacillusamyloliquefaciensncimb30251aspergillusoryzaecbs58594andaspergillusoryzaeattcsd5374endo14betaglucanasefromtrichodermareeseiatccpta10001trichodermareeseiatccsd6331andaspergillusniger AT jaimeaguilera safetyandefficacyofalphaamylasefrombacillusamyloliquefaciensdsm9553bacillusamyloliquefaciensncimb30251aspergillusoryzaecbs58594andaspergillusoryzaeattcsd5374endo14betaglucanasefromtrichodermareeseiatccpta10001trichodermareeseiatccsd6331andaspergillusniger AT montserratanguita safetyandefficacyofalphaamylasefrombacillusamyloliquefaciensdsm9553bacillusamyloliquefaciensncimb30251aspergillusoryzaecbs58594andaspergillusoryzaeattcsd5374endo14betaglucanasefromtrichodermareeseiatccpta10001trichodermareeseiatccsd6331andaspergillusniger |