Characterization and optimization of extracellular enzymes production by Aspergillus niger strains isolated from date by-products
Background This work aims to study the optimal conditions of the fermentation culture medium used for the production of extracellular enzymes (amylase, cellulase, lipase, and protease) from previously isolated Aspergillus niger strains in date by-products. Results The five most powerful isolates sel...
Saved in:
Published in | Journal of Genetic Engineering and Biotechnology Vol. 19; no. 1; pp. 50 - 8 |
---|---|
Main Authors | , , , , , , , |
Format | Journal Article |
Language | English |
Published |
Berlin/Heidelberg
Springer Berlin Heidelberg
31.03.2021
Springer Springer Nature B.V Elsevier |
Subjects | |
Online Access | Get full text |
ISSN | 1687-157X 2090-5920 |
DOI | 10.1186/s43141-021-00145-y |
Cover
Loading…
Abstract | Background
This work aims to study the optimal conditions of the fermentation culture medium used for the production of extracellular enzymes (amylase, cellulase, lipase, and protease) from previously isolated
Aspergillus niger
strains in date by-products.
Results
The five most powerful isolates selected based on the zone of degradation formed on Petri plates by the substrate were subjected to the quantitative evaluation of their enzymatic production. All five strains showed almost similar API-ZYM profiles, with minor variations observed at the level of some specific enzyme expression. The production of cellulase and amylase was depending on pH and incubation temperatures. ASP2 strain demonstrated the high production rate of amylase (at pH 5 and 30 °C) and cellulase (at pH 6 and 30 °C) for 96 h of incubation.
Conclusion
The
A. niger
showed the ability to produce several extracellular enzymes and can be used in the valorization of different agroindustrial residues. |
---|---|
AbstractList | This work aims to study the optimal conditions of the fermentation culture medium used for the production of extracellular enzymes (amylase, cellulase, lipase, and protease) from previously isolated Aspergillus niger strains in date by-products.
The five most powerful isolates selected based on the zone of degradation formed on Petri plates by the substrate were subjected to the quantitative evaluation of their enzymatic production. All five strains showed almost similar API-ZYM profiles, with minor variations observed at the level of some specific enzyme expression. The production of cellulase and amylase was depending on pH and incubation temperatures. ASP2 strain demonstrated the high production rate of amylase (at pH 5 and 30 °C) and cellulase (at pH 6 and 30 °C) for 96 h of incubation.
The A. niger showed the ability to produce several extracellular enzymes and can be used in the valorization of different agroindustrial residues. Background This work aims to study the optimal conditions of the fermentation culture medium used for the production of extracellular enzymes (amylase, cellulase, lipase, and protease) from previously isolated Aspergillus niger strains in date by-products. Results The five most powerful isolates selected based on the zone of degradation formed on Petri plates by the substrate were subjected to the quantitative evaluation of their enzymatic production. All five strains showed almost similar API-ZYM profiles, with minor variations observed at the level of some specific enzyme expression. The production of cellulase and amylase was depending on pH and incubation temperatures. ASP2 strain demonstrated the high production rate of amylase (at pH 5 and 30 °C) and cellulase (at pH 6 and 30 °C) for 96 h of incubation. Conclusion The A. niger showed the ability to produce several extracellular enzymes and can be used in the valorization of different agroindustrial residues. Background This work aims to study the optimal conditions of the fermentation culture medium used for the production of extracellular enzymes (amylase, cellulase, lipase, and protease) from previously isolated Aspergillus niger strains in date by-products. Results The five most powerful isolates selected based on the zone of degradation formed on Petri plates by the substrate were subjected to the quantitative evaluation of their enzymatic production. All five strains showed almost similar API-ZYM profiles, with minor variations observed at the level of some specific enzyme expression. The production of cellulase and amylase was depending on pH and incubation temperatures. ASP2 strain demonstrated the high production rate of amylase (at pH 5 and 30 °C) and cellulase (at pH 6 and 30 °C) for 96 h of incubation. Conclusion The A. niger showed the ability to produce several extracellular enzymes and can be used in the valorization of different agroindustrial residues. Abstract Background This work aims to study the optimal conditions of the fermentation culture medium used for the production of extracellular enzymes (amylase, cellulase, lipase, and protease) from previously isolated Aspergillus niger strains in date by-products. Results The five most powerful isolates selected based on the zone of degradation formed on Petri plates by the substrate were subjected to the quantitative evaluation of their enzymatic production. All five strains showed almost similar API-ZYM profiles, with minor variations observed at the level of some specific enzyme expression. The production of cellulase and amylase was depending on pH and incubation temperatures. ASP2 strain demonstrated the high production rate of amylase (at pH 5 and 30 °C) and cellulase (at pH 6 and 30 °C) for 96 h of incubation. Conclusion The A. niger showed the ability to produce several extracellular enzymes and can be used in the valorization of different agroindustrial residues. BackgroundThis work aims to study the optimal conditions of the fermentation culture medium used for the production of extracellular enzymes (amylase, cellulase, lipase, and protease) from previously isolated Aspergillus niger strains in date by-products.ResultsThe five most powerful isolates selected based on the zone of degradation formed on Petri plates by the substrate were subjected to the quantitative evaluation of their enzymatic production. All five strains showed almost similar API-ZYM profiles, with minor variations observed at the level of some specific enzyme expression. The production of cellulase and amylase was depending on pH and incubation temperatures. ASP2 strain demonstrated the high production rate of amylase (at pH 5 and 30 °C) and cellulase (at pH 6 and 30 °C) for 96 h of incubation.ConclusionThe A. niger showed the ability to produce several extracellular enzymes and can be used in the valorization of different agroindustrial residues. This work aims to study the optimal conditions of the fermentation culture medium used for the production of extracellular enzymes (amylase, cellulase, lipase, and protease) from previously isolated Aspergillus niger strains in date by-products. The five most powerful isolates selected based on the zone of degradation formed on Petri plates by the substrate were subjected to the quantitative evaluation of their enzymatic production. All five strains showed almost similar API-ZYM profiles, with minor variations observed at the level of some specific enzyme expression. The production of cellulase and amylase was depending on pH and incubation temperatures. ASP2 strain demonstrated the high production rate of amylase (at pH 5 and 30 °C) and cellulase (at pH 6 and 30 °C) for 96 h of incubation. The A. niger showed the ability to produce several extracellular enzymes and can be used in the valorization of different agroindustrial residues. |
ArticleNumber | 50 |
Audience | Academic |
Author | Hasnaoui, Amina Ghabbour, Nabil Asehraou, Abdeslam Bechchari, Abdelmajid Bellaouchi, Reda Hakkou, Abdelkader Rokni, Yahya Abouloifa, Houssam |
Author_xml | – sequence: 1 givenname: Reda orcidid: 0000-0002-3619-4877 surname: Bellaouchi fullname: Bellaouchi, Reda email: r.bellaouchi@ump.ac.ma organization: Laboratory of Bioresources, Biotechnology, Ethnopharmacology and Health, Faculty of Sciences, Mohammed Premier University – sequence: 2 givenname: Houssam surname: Abouloifa fullname: Abouloifa, Houssam organization: Laboratory of Bioresources, Biotechnology, Ethnopharmacology and Health, Faculty of Sciences, Mohammed Premier University – sequence: 3 givenname: Yahya surname: Rokni fullname: Rokni, Yahya organization: Laboratory of Bioresources, Biotechnology, Ethnopharmacology and Health, Faculty of Sciences, Mohammed Premier University – sequence: 4 givenname: Amina surname: Hasnaoui fullname: Hasnaoui, Amina organization: Laboratory of Bioresources, Biotechnology, Ethnopharmacology and Health, Faculty of Sciences, Mohammed Premier University – sequence: 5 givenname: Nabil surname: Ghabbour fullname: Ghabbour, Nabil organization: Laboratory of Bioresources, Biotechnology, Ethnopharmacology and Health, Faculty of Sciences, Mohammed Premier University – sequence: 6 givenname: Abdelkader surname: Hakkou fullname: Hakkou, Abdelkader organization: Laboratory of Bioresources, Biotechnology, Ethnopharmacology and Health, Faculty of Sciences, Mohammed Premier University – sequence: 7 givenname: Abdelmajid surname: Bechchari fullname: Bechchari, Abdelmajid organization: National Institute of Agronomic Research (INRA), Oujda Center – sequence: 8 givenname: Abdeslam surname: Asehraou fullname: Asehraou, Abdeslam organization: Laboratory of Bioresources, Biotechnology, Ethnopharmacology and Health, Faculty of Sciences, Mohammed Premier University |
BackLink | https://www.ncbi.nlm.nih.gov/pubmed/33788044$$D View this record in MEDLINE/PubMed |
BookMark | eNp9kktv1DAUhSNURIehf4AFisSGTYqvH0m8QRqNeFSqxAYkdpad2FOPEnuwM4jpjn_OnUcL7aKOLEc33znxtc_L4izEYIviNZBLgLZ-nzkDDhWhOAlwUe2eFTNKJKmEpOSsmEHdNhWI5sd5cZHzmuAQvAUBL4pzxpq2JZzPij_LG510N9nkb_XkYyh16Mu4mfx4V4iutL8nhOwwbAedShtud6PN5SbFftsdGLMrF3lj08ojk8vgVzaVGUU-5NLnOOjJ9qVLcSx7fEW-Oqnzq-K500O2F6d1Xnz_9PHb8kt1_fXz1XJxXXU10KkSVpiurV0rDdC6lgJc31ljpSOOAXSubaBnYHjbm05qRowgzHBpiXTcaMvmxdXRt496rTbJjzrtVNReHQoxrZROk-8Gq3rKO3BN6ygFTnuQDePGcGaYkLUVHL0-HL02WzNa3EfAVocHpg-_BH-jVvGXaglQ3uwN3p0MUvy5tXlSo8_7A9bBxm1WDATDWwaoEX37CF3HbQp4VIo2VArGJcLz4vJIrTQ24IOL-xvDp7ej7zA6zmN9UTcoaCQ0KHjzfwv3e7-LBgL0CHQp5pysu0eAqH0E1TGCCiOoDhFUOxS1j0Sdnw4x2mdheFrKjtKM_wmYn399PqH6CwJZ88g |
CitedBy_id | crossref_primary_10_3390_plants12244158 crossref_primary_10_1016_j_mtbio_2023_100823 crossref_primary_10_1016_j_scp_2023_101127 crossref_primary_10_1039_D2RA00304J crossref_primary_10_1155_tswj_2296078 crossref_primary_10_1007_s13205_022_03456_0 crossref_primary_10_1080_14786451_2024_2345735 crossref_primary_10_1016_j_etap_2023_104209 crossref_primary_10_3389_fagro_2022_948309 crossref_primary_10_1007_s42360_022_00465_0 crossref_primary_10_1016_j_biortech_2024_131165 crossref_primary_10_3390_su15043590 crossref_primary_10_1016_j_fuel_2024_132593 crossref_primary_10_1007_s11274_021_03116_0 crossref_primary_10_1007_s13399_023_04603_0 crossref_primary_10_1039_D2RA06138D crossref_primary_10_1007_s12649_024_02879_5 crossref_primary_10_1080_17597269_2022_2123938 crossref_primary_10_1186_s13068_021_02074_x crossref_primary_10_1007_s11869_024_01631_1 crossref_primary_10_1007_s13762_024_05808_0 crossref_primary_10_1007_s10123_024_00609_4 crossref_primary_10_3390_jof10040298 crossref_primary_10_36868_IJCS_2023_04_02 crossref_primary_10_21931_RB_2023_08_04_31 crossref_primary_10_1016_j_psep_2023_11_053 crossref_primary_10_3390_fermentation10050226 crossref_primary_10_1186_s40643_025_00852_1 crossref_primary_10_1111_1750_3841_16748 crossref_primary_10_21931_RB_CSS_2023_08_03_96 |
Cites_doi | 10.1016/j.fgb.2008.07.020 10.1016/j.jfoodeng.2005.01.009 10.1021/ac60147a030 10.3923/tasr.2007.23.27 10.3923/biotech.2008.551.556 10.3891/acta.chem.scand.03-1405 10.1016/j.heliyon.2020.e05668 10.1016/j.bcab.2016.01.005 10.1016/S0141-0229(96)00225-6 10.1007/BF00443941 10.1007/s00284-020-02036-w 10.1016/j.bcab.2019.101256 10.3923/jbs.2002.73.75 10.1128/MMBR.65.4.497-522.2001 10.1128/AEM.34.1.1-6.1977 10.17485/ijst/2012/v5i7.4 10.1016/j.biortech.2005.05.022 10.1128/aem.34.1.1-6.1977 |
ContentType | Journal Article |
Copyright | The Author(s) 2021 COPYRIGHT 2021 Springer The Author(s) 2021. This work is published under http://creativecommons.org/licenses/by/4.0/ (the “License”). Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License. |
Copyright_xml | – notice: The Author(s) 2021 – notice: COPYRIGHT 2021 Springer – notice: The Author(s) 2021. This work is published under http://creativecommons.org/licenses/by/4.0/ (the “License”). Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License. |
DBID | C6C AAYXX CITATION NPM 8FE 8FG 8FH ABJCF ABUWG AFKRA AZQEC BBNVY BENPR BGLVJ BHPHI CCPQU DWQXO GNUQQ HCIFZ L6V LK8 M7P M7S PHGZM PHGZT PIMPY PKEHL PQEST PQGLB PQQKQ PQUKI PRINS PTHSS 7S9 L.6 5PM DOA |
DOI | 10.1186/s43141-021-00145-y |
DatabaseName | Springer Nature Link CrossRef PubMed ProQuest SciTech Collection ProQuest Technology Collection ProQuest Natural Science Collection ProQuest SciTech Premium Collection Technology Collection Materials Science & Engineering Database ProQuest Central (Alumni) ProQuest Central UK/Ireland ProQuest Central Essentials ProQuest SciTech Premium Collection Natural Science Collection Biological Science Collection ProQuest Central Database Suite (ProQuest) ProQuest Technology Collection Natural Science Collection ProQuest One ProQuest Central ProQuest Central Student SciTech Collection (ProQuest) ProQuest Engineering Collection Biological Sciences Biological Science Database (ProQuest) Engineering Database ProQuest Central Premium ProQuest One Academic (New) ProQuest - Publicly Available Content Database ProQuest One Academic Middle East (New) ProQuest One Academic Eastern Edition (DO NOT USE) ProQuest One Applied & Life Sciences ProQuest One Academic ProQuest One Academic UKI Edition ProQuest Central China Engineering Collection AGRICOLA AGRICOLA - Academic PubMed Central (Full Participant titles) DOAJ Directory of Open Access Journals |
DatabaseTitle | CrossRef PubMed Publicly Available Content Database ProQuest Central Student Technology Collection ProQuest One Academic Middle East (New) ProQuest Central Essentials ProQuest Central (Alumni Edition) SciTech Premium Collection ProQuest One Community College ProQuest Natural Science Collection ProQuest Central China ProQuest Central ProQuest One Applied & Life Sciences ProQuest Engineering Collection Natural Science Collection ProQuest Central Korea Biological Science Collection ProQuest Central (New) Engineering Collection Engineering Database ProQuest Biological Science Collection ProQuest One Academic Eastern Edition ProQuest Technology Collection Biological Science Database ProQuest SciTech Collection ProQuest One Academic UKI Edition Materials Science & Engineering Collection ProQuest One Academic ProQuest One Academic (New) AGRICOLA AGRICOLA - Academic |
DatabaseTitleList | PubMed Publicly Available Content Database AGRICOLA |
Database_xml | – sequence: 1 dbid: C6C name: Springer Nature OA Free Journals url: http://www.springeropen.com/ sourceTypes: Publisher – sequence: 2 dbid: DOA name: DOAJ Directory of Open Access Journals url: https://www.doaj.org/ sourceTypes: Open Website – sequence: 3 dbid: NPM name: PubMed url: https://proxy.k.utb.cz/login?url=http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=PubMed sourceTypes: Index Database – sequence: 4 dbid: 8FG name: ProQuest Technology Collection url: https://search.proquest.com/technologycollection1 sourceTypes: Aggregation Database |
DeliveryMethod | fulltext_linktorsrc |
Discipline | Engineering Biology |
EISSN | 2090-5920 |
EndPage | 8 |
ExternalDocumentID | oai_doaj_org_article_d24c1f78f22142d19734bb43b3596e54 PMC8012474 A679537917 33788044 10_1186_s43141_021_00145_y |
Genre | Journal Article |
GeographicLocations | Morocco Niger India France United States--US |
GeographicLocations_xml | – name: Niger – name: Morocco – name: India – name: United States--US – name: France |
GroupedDBID | C6C --K 0R~ 4.4 457 5VS AAEDT AAEDW AAFWJ AAHBH AAIKJ AAKKN AALRI AAXUO AAYWO AAYXX ABEEZ ABJCF ABMAC ACACY ACGFS ACULB ACVFH ADBBV ADCNI ADEZE ADVLN AEUPX AEXQZ AFGXO AFKRA AFPKN AFPUW AGHFR AIGII AITUG AKBMS AKRWK AKYEP ALMA_UNASSIGNED_HOLDINGS AMRAJ AOIJS APXCP BAWUL BBNVY BENPR BGLVJ BHPHI C24 CCPQU CITATION DIK EBS EJD FDB GROUPED_DOAJ H13 HCIFZ HYE HZ~ IAO IGS IHR IPNFZ ITC IXB KQ8 M41 M7P M7S O-L O9- OK1 PHGZM PHGZT PIMPY PTHSS RIG ROL RPM SOJ SSZ XH2 NPM PMFND 8FE 8FG 8FH ABUWG AZQEC DWQXO GNUQQ L6V LK8 PKEHL PQEST PQGLB PQQKQ PQUKI PRINS 7S9 L.6 PUEGO 5PM |
ID | FETCH-LOGICAL-c612t-5e5bc86f89b1266951fdcebe9f0f311cf871d31b48dbc9a30b503b49e09f4bae3 |
IEDL.DBID | C6C |
ISSN | 1687-157X |
IngestDate | Wed Aug 27 01:25:23 EDT 2025 Thu Aug 21 18:25:21 EDT 2025 Fri Sep 05 08:49:58 EDT 2025 Fri Jul 25 11:52:47 EDT 2025 Tue Jun 10 20:34:18 EDT 2025 Thu Jan 02 22:56:20 EST 2025 Thu Apr 24 23:07:22 EDT 2025 Tue Jul 01 04:06:13 EDT 2025 Fri Feb 21 02:49:32 EST 2025 |
IsDoiOpenAccess | true |
IsOpenAccess | true |
IsPeerReviewed | true |
IsScholarly | true |
Issue | 1 |
Keywords | Enzymes Extracellular Date by-products Aspergillus niger |
Language | English |
License | Open AccessThis article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit http://creativecommons.org/licenses/by/4.0/. |
LinkModel | DirectLink |
MergedId | FETCHMERGED-LOGICAL-c612t-5e5bc86f89b1266951fdcebe9f0f311cf871d31b48dbc9a30b503b49e09f4bae3 |
Notes | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 14 content type line 23 |
ORCID | 0000-0002-3619-4877 |
OpenAccessLink | https://doi.org/10.1186/s43141-021-00145-y |
PMID | 33788044 |
PQID | 2729534915 |
PQPubID | 5642926 |
PageCount | 8 |
ParticipantIDs | doaj_primary_oai_doaj_org_article_d24c1f78f22142d19734bb43b3596e54 pubmedcentral_primary_oai_pubmedcentral_nih_gov_8012474 proquest_miscellaneous_3153186116 proquest_journals_2729534915 gale_infotracacademiconefile_A679537917 pubmed_primary_33788044 crossref_primary_10_1186_s43141_021_00145_y crossref_citationtrail_10_1186_s43141_021_00145_y springer_journals_10_1186_s43141_021_00145_y |
ProviderPackageCode | CITATION AAYXX |
PublicationCentury | 2000 |
PublicationDate | 2021-03-31 |
PublicationDateYYYYMMDD | 2021-03-31 |
PublicationDate_xml | – month: 03 year: 2021 text: 2021-03-31 day: 31 |
PublicationDecade | 2020 |
PublicationPlace | Berlin/Heidelberg |
PublicationPlace_xml | – name: Berlin/Heidelberg – name: Netherlands – name: Cairo |
PublicationTitle | Journal of Genetic Engineering and Biotechnology |
PublicationTitleAbbrev | J Genet Eng Biotechnol |
PublicationTitleAlternate | J Genet Eng Biotechnol |
PublicationYear | 2021 |
Publisher | Springer Berlin Heidelberg Springer Springer Nature B.V Elsevier |
Publisher_xml | – name: Springer Berlin Heidelberg – name: Springer – name: Springer Nature B.V – name: Elsevier |
References | Nahas, Waldemarin (CR17) 2002; 44 Coutinho, Andersen, Kolenova, vanKuyk, Benoit, Gruben, Trejo-Aguilar, Visser, van Solingen, Pakula (CR3) 2009; 46 Mostafa, Abd, Aty, Hamed, Eid, Ibrahim (CR8) 2016; 5 Mitidieri, Martinelli, Schrank, Vainstein (CR20) 2006; 97 Devanathan, Shanmugam, Balasubramanian, Manivannan (CR27) 2007; 2 Shruthi, Achur, Boramuthi (CR9) 2020; 77 Hasnaoui, ElHoumaizi, Asehraou, Sindic, Deroanne, Hakkou (CR6) 2010; 12 CR14 Hernández, Rodriguez, Guerra, Rosés (CR18) 2006; 73 Grover, Maninder, Sarao (CR21) 2013; 2 Yabuki, Ono, Hoshino, Fukui (CR13) 1977; 34 Bridge, Hawksworth (CR15) 1984; 1 Berka, Dunn-Coleman, Ward (CR1) 1992; 23 Sattar, Bibi, Kamran, Aman, Qader (CR12) 2019; 21 Gupta, Gupta, Modi, Yadava (CR24) 2008; 7 Haq, Ashraf, Rani, Qadeer (CR28) 2002; 2 Uguru, Akinyanju, Sani (CR19) 1997; 21 CR2 Williams, Brady, Bridge, Paterson (CR16) 1992; 119 Hasnaoui, Elhoumaizi, Borchani, Attia, Besbes (CR7) 2012; 5 Varalakshmi, Kumudini, Nandini, Solomon, Suhas, Mahesh, Kavitha (CR22) 2009; 58 Alva, Anupama, Savla, Chiu, Vyshali, Shruti, Yogeetha, Bhavya, Purvi, Ruchi (CR23) 2007; 6 CR26 de Vries, Visser (CR4) 2001; 65 Sulyman, Igunnu, Malomo (CR25) 2020; 12 Bellaouchi, Ghomari, Hasnaoui, Hakkou, Bechchari, Chihib, Asehraou (CR5) 2017; 24 Miller (CR11) 1959; 31 Hultin, Nordstrom (CR10) 1949; 3 Gupta (10.1186/s43141-021-00145-y_bib24) 2008; 7 Nahas (10.1186/s43141-021-00145-y_bib17) 2002; 44 10.1186/s43141-021-00145-y_bib2 Sulyman (10.1186/s43141-021-00145-y_bib25) 2020; 12 Miller (10.1186/s43141-021-00145-y_bib11) 1959; 31 Berka (10.1186/s43141-021-00145-y_bib1) 1992; 23 10.1186/s43141-021-00145-y_bib26 Haq (10.1186/s43141-021-00145-y_bib28) 2002; 2 Varalakshmi (10.1186/s43141-021-00145-y_bib22) 2009; 58 Hernández (10.1186/s43141-021-00145-y_bib18) 2006; 73 Mitidieri (10.1186/s43141-021-00145-y_bib20) 2006; 97 Bridge (10.1186/s43141-021-00145-y_bib15) 1984; 1 Shruthi (10.1186/s43141-021-00145-y_bib9) 2020; 77 de Vries (10.1186/s43141-021-00145-y_bib4) 2001; 65 Hultin (10.1186/s43141-021-00145-y_bib10) 1949; 3 Devanathan (10.1186/s43141-021-00145-y_bib27) 2007; 2 Hasnaoui (10.1186/s43141-021-00145-y_bib7) 2012; 5 Grover (10.1186/s43141-021-00145-y_bib21) 2013; 2 Sattar (10.1186/s43141-021-00145-y_bib12) 2019; 21 Coutinho (10.1186/s43141-021-00145-y_bib3) 2009; 46 Hasnaoui (10.1186/s43141-021-00145-y_bib6) 2010; 12 Mostafa (10.1186/s43141-021-00145-y_bib8) 2016; 5 Williams (10.1186/s43141-021-00145-y_bib16) 1992; 119 Uguru (10.1186/s43141-021-00145-y_bib19) 1997; 21 Alva (10.1186/s43141-021-00145-y_bib23) 2007; 6 10.1186/s43141-021-00145-y_bib14 Yabuki (10.1186/s43141-021-00145-y_bib13) 1977; 34 Bellaouchi (10.1186/s43141-021-00145-y_bib5) 2017; 24 |
References_xml | – volume: 1 start-page: 232 issue: 9 year: 1984 end-page: 234 ident: CR15 article-title: The API ZYM enzyme testing system as an aid to the rapid identification of isolates publication-title: Microbiol Sci – volume: 23 start-page: 155 year: 1992 ident: CR1 article-title: Industrial enzymes from species publication-title: Biotechnol – volume: 46 start-page: S161 issue: 1 year: 2009 end-page: S169 ident: CR3 article-title: Post-genomic insights into the plant polysaccharide degradation potential of Aspergillus nidulans and comparison to and publication-title: Fungal Genet Biol doi: 10.1016/j.fgb.2008.07.020 – ident: CR14 – ident: CR2 – volume: 73 start-page: 93 issue: 1 year: 2006 end-page: 100 ident: CR18 article-title: Amylase production by in submerged cultivation on two wastes from food industries publication-title: J Food Eng doi: 10.1016/j.jfoodeng.2005.01.009 – volume: 31 start-page: 426 issue: 3 year: 1959 end-page: 428 ident: CR11 article-title: Use of dinitrosalicylic acid reagent for determination of reducing sugar publication-title: Anal Chem doi: 10.1021/ac60147a030 – volume: 2 start-page: 23 year: 2007 end-page: 27 ident: CR27 article-title: Cellulase production by isolated from coastal mangrove debris publication-title: Trends Appl Sci Res doi: 10.3923/tasr.2007.23.27 – volume: 7 start-page: 551 issue: 3 year: 2008 end-page: 556 ident: CR24 article-title: Production and characterization of α-amylase from publication-title: Biotechnol doi: 10.3923/biotech.2008.551.556 – volume: 3 start-page: 1405 year: 1949 end-page: 1417 ident: CR10 article-title: Investigations on dextranase. I On the occurrence and the assay of dextranase publication-title: Aeta Chem Scand doi: 10.3891/acta.chem.scand.03-1405 – volume: 6 start-page: 576 year: 2007 ident: CR23 article-title: Production and characterization of fungal amylase enzyme isolated from . JGI 12 in solid state culture publication-title: Afr J Biotechnol – volume: 12 start-page: e05668 year: 2020 ident: CR25 article-title: Isolation, purification and characterization of cellulase produced by cultured on Arachis hypogaea shells publication-title: Heliyon doi: 10.1016/j.heliyon.2020.e05668 – volume: 5 start-page: 116 year: 2016 end-page: 122 ident: CR8 article-title: Enzymatic, kinetic and anti-microbial studies on culture filtrate and Allium cepa seeds extract and their potent applications publication-title: Biocatal Agric Biotechnol doi: 10.1016/j.bcab.2016.01.005 – volume: 58 start-page: 29 issue: 1 year: 2009 end-page: 36 ident: CR22 article-title: Production and characterization of a-amylase from JGI 24 isolated in Bangalore publication-title: Pol J Microbiol – volume: 2 start-page: 108 year: 2013 end-page: 124 ident: CR21 article-title: Production of fungal amylase and cellulase enzymes via solid state fermentation using and publication-title: Int J Adv Res Technol – volume: 21 start-page: 48 issue: 1 year: 1997 end-page: 51 ident: CR19 article-title: The use of yam peel for growth of locally isolated and amylase production publication-title: Enzym Microb Technol doi: 10.1016/S0141-0229(96)00225-6 – volume: 119 start-page: 101 issue: 2 year: 1992 end-page: 114 ident: CR16 article-title: Biochemical and physiological tests as aids to identification of section Nigrescentia publication-title: Mycopathologia doi: 10.1007/BF00443941 – volume: 24 start-page: 963 year: 2017 end-page: 969 ident: CR5 article-title: Physico-chemical and microbial properties of undervalued dates and processed dates by-products in Morocco publication-title: Int Food Re J – volume: 77 start-page: 2192 issue: 9 year: 2020 end-page: 2206 ident: CR9 article-title: Optimized solid-state fermentation medium enhances the multienzymes production from and publication-title: Curr Microbiol doi: 10.1007/s00284-020-02036-w – volume: 12 start-page: 311 year: 2010 end-page: 314 ident: CR6 article-title: Chemical composition and microbial quality of dates grown in Figuig oasis of Morocco publication-title: Int J Agric Biol – volume: 21 start-page: 101256 year: 2019 ident: CR12 article-title: Degradation of complex casein polymer: production and optimization of a novel serine metalloprotease from KIBGE-IB36 publication-title: Biocatal Agric Biotechnol doi: 10.1016/j.bcab.2019.101256 – volume: 2 start-page: 73 year: 2002 end-page: 75 ident: CR28 article-title: Biosynthesis of alpha amylase by chemically treated mutant of GCBU-20 publication-title: Pak J Biol Sci doi: 10.3923/jbs.2002.73.75 – volume: 65 start-page: 497 issue: 4 year: 2001 end-page: 522 ident: CR4 article-title: Aspergillus enzymes involved in degradation of plant cell wall polysaccharides publication-title: Microbiol Mol Biol Rev doi: 10.1128/MMBR.65.4.497-522.2001 – volume: 34 start-page: 1 issue: 1 year: 1977 end-page: 6 ident: CR13 article-title: Rapid induction of alpha-amylase by nongrowing mycelia of publication-title: Appl Environ Microbiol doi: 10.1128/AEM.34.1.1-6.1977 – volume: 5 start-page: 2954 year: 2012 end-page: 2960 ident: CR7 article-title: Physico-chemical characterization and associated antioxidant capacity of fiber concentrates from Moroccan date flesh publication-title: Indian J Sci Technol doi: 10.17485/ijst/2012/v5i7.4 – volume: 44 start-page: 5 year: 2002 end-page: 10 ident: CR17 article-title: Control of amylase production and growth characteristics of publication-title: Rev Latinoam Microbiol – ident: CR26 – volume: 97 start-page: 1217 issue: 10 year: 2006 end-page: 1224 ident: CR20 article-title: Enzymatic detergent formulation containing amylase from : a comparative study with commercial detergent formulations publication-title: Bioresour Technol doi: 10.1016/j.biortech.2005.05.022 – ident: 10.1186/s43141-021-00145-y_bib2 – volume: 23 start-page: 155 year: 1992 ident: 10.1186/s43141-021-00145-y_bib1 article-title: Industrial enzymes from Aspergillus species publication-title: Biotechnol – volume: 21 start-page: 48 issue: 1 year: 1997 ident: 10.1186/s43141-021-00145-y_bib19 article-title: The use of yam peel for growth of locally isolated Aspergillus niger and amylase production publication-title: Enzym Microb Technol doi: 10.1016/S0141-0229(96)00225-6 – volume: 77 start-page: 2192 issue: 9 year: 2020 ident: 10.1186/s43141-021-00145-y_bib9 article-title: Optimized solid-state fermentation medium enhances the multienzymes production from Penicillium citrinum and Aspergillus clavatus publication-title: Curr Microbiol doi: 10.1007/s00284-020-02036-w – volume: 34 start-page: 1 issue: 1 year: 1977 ident: 10.1186/s43141-021-00145-y_bib13 article-title: Rapid induction of alpha-amylase by nongrowing mycelia of Aspergillus oryzae publication-title: Appl Environ Microbiol doi: 10.1128/aem.34.1.1-6.1977 – volume: 46 start-page: S161 issue: 1 year: 2009 ident: 10.1186/s43141-021-00145-y_bib3 article-title: Post-genomic insights into the plant polysaccharide degradation potential of Aspergillus nidulans and comparison to Aspergillus niger and Aspergillus oryzae publication-title: Fungal Genet Biol doi: 10.1016/j.fgb.2008.07.020 – volume: 73 start-page: 93 issue: 1 year: 2006 ident: 10.1186/s43141-021-00145-y_bib18 article-title: Amylase production by Aspergillus niger in submerged cultivation on two wastes from food industries publication-title: J Food Eng doi: 10.1016/j.jfoodeng.2005.01.009 – ident: 10.1186/s43141-021-00145-y_bib26 – volume: 7 start-page: 551 issue: 3 year: 2008 ident: 10.1186/s43141-021-00145-y_bib24 article-title: Production and characterization of α-amylase from Aspergillus niger publication-title: Biotechnol doi: 10.3923/biotech.2008.551.556 – volume: 2 start-page: 23 year: 2007 ident: 10.1186/s43141-021-00145-y_bib27 article-title: Cellulase production by Aspergillus niger isolated from coastal mangrove debris publication-title: Trends Appl Sci Res doi: 10.3923/tasr.2007.23.27 – volume: 3 start-page: 1405 year: 1949 ident: 10.1186/s43141-021-00145-y_bib10 article-title: Investigations on dextranase. I. On the occurrence and the assay of dextranase publication-title: Aeta Chem Scand doi: 10.3891/acta.chem.scand.03-1405 – volume: 5 start-page: 2954 year: 2012 ident: 10.1186/s43141-021-00145-y_bib7 article-title: Physico-chemical characterization and associated antioxidant capacity of fiber concentrates from Moroccan date flesh publication-title: Indian J Sci Technol doi: 10.17485/ijst/2012/v5i7.4 – volume: 24 start-page: 963 year: 2017 ident: 10.1186/s43141-021-00145-y_bib5 article-title: Physico-chemical and microbial properties of undervalued dates and processed dates by-products in Morocco publication-title: Int Food Re J – volume: 6 start-page: 576 year: 2007 ident: 10.1186/s43141-021-00145-y_bib23 article-title: Production and characterization of fungal amylase enzyme isolated from Aspergillus sp. JGI 12 in solid state culture publication-title: Afr J Biotechnol – ident: 10.1186/s43141-021-00145-y_bib14 – volume: 2 start-page: 73 year: 2002 ident: 10.1186/s43141-021-00145-y_bib28 article-title: Biosynthesis of alpha amylase by chemically treated mutant of Bacillus subtilis GCBU-20 publication-title: Pak J Biol Sci doi: 10.3923/jbs.2002.73.75 – volume: 5 start-page: 116 year: 2016 ident: 10.1186/s43141-021-00145-y_bib8 article-title: Enzymatic, kinetic and anti-microbial studies on Aspergillus terreus culture filtrate and Allium cepa seeds extract and their potent applications publication-title: Biocatal Agric Biotechnol doi: 10.1016/j.bcab.2016.01.005 – volume: 1 start-page: 232 issue: 9 year: 1984 ident: 10.1186/s43141-021-00145-y_bib15 article-title: The API ZYM enzyme testing system as an aid to the rapid identification of Penicillium isolates publication-title: Microbiol Sci – volume: 58 start-page: 29 issue: 1 year: 2009 ident: 10.1186/s43141-021-00145-y_bib22 article-title: Production and characterization of a-amylase from Aspergillus niger JGI 24 isolated in Bangalore publication-title: Pol J Microbiol – volume: 119 start-page: 101 issue: 2 year: 1992 ident: 10.1186/s43141-021-00145-y_bib16 article-title: Biochemical and physiological tests as aids to identification of Verticillium section Nigrescentia publication-title: Mycopathologia doi: 10.1007/BF00443941 – volume: 31 start-page: 426 issue: 3 year: 1959 ident: 10.1186/s43141-021-00145-y_bib11 article-title: Use of dinitrosalicylic acid reagent for determination of reducing sugar publication-title: Anal Chem doi: 10.1021/ac60147a030 – volume: 12 start-page: 311 year: 2010 ident: 10.1186/s43141-021-00145-y_bib6 article-title: Chemical composition and microbial quality of dates grown in Figuig oasis of Morocco publication-title: Int J Agric Biol – volume: 44 start-page: 5 year: 2002 ident: 10.1186/s43141-021-00145-y_bib17 article-title: Control of amylase production and growth characteristics of Aspergillus ochraceus publication-title: Rev Latinoam Microbiol – volume: 65 start-page: 497 issue: 4 year: 2001 ident: 10.1186/s43141-021-00145-y_bib4 article-title: Aspergillus enzymes involved in degradation of plant cell wall polysaccharides publication-title: Microbiol Mol Biol Rev doi: 10.1128/MMBR.65.4.497-522.2001 – volume: 21 year: 2019 ident: 10.1186/s43141-021-00145-y_bib12 article-title: Degradation of complex casein polymer: production and optimization of a novel serine metalloprotease from Aspergillus niger KIBGE-IB36 publication-title: Biocatal Agric Biotechnol doi: 10.1016/j.bcab.2019.101256 – volume: 97 start-page: 1217 issue: 10 year: 2006 ident: 10.1186/s43141-021-00145-y_bib20 article-title: Enzymatic detergent formulation containing amylase from Aspergillus niger: a comparative study with commercial detergent formulations publication-title: Bioresour Technol doi: 10.1016/j.biortech.2005.05.022 – volume: 2 start-page: 108 year: 2013 ident: 10.1186/s43141-021-00145-y_bib21 article-title: Production of fungal amylase and cellulase enzymes via solid state fermentation using Aspergillus oryzae and Trichoderma reesei publication-title: Int J Adv Res Technol – volume: 12 year: 2020 ident: 10.1186/s43141-021-00145-y_bib25 article-title: Isolation, purification and characterization of cellulase produced by Aspergillus niger cultured on Arachis hypogaea shells publication-title: Heliyon |
SSID | ssj0000548151 |
Score | 2.33998 |
Snippet | Background
This work aims to study the optimal conditions of the fermentation culture medium used for the production of extracellular enzymes (amylase,... This work aims to study the optimal conditions of the fermentation culture medium used for the production of extracellular enzymes (amylase, cellulase, lipase,... Background This work aims to study the optimal conditions of the fermentation culture medium used for the production of extracellular enzymes (amylase,... BackgroundThis work aims to study the optimal conditions of the fermentation culture medium used for the production of extracellular enzymes (amylase,... Abstract Background This work aims to study the optimal conditions of the fermentation culture medium used for the production of extracellular enzymes... |
SourceID | doaj pubmedcentral proquest gale pubmed crossref springer |
SourceType | Open Website Open Access Repository Aggregation Database Index Database Enrichment Source Publisher |
StartPage | 50 |
SubjectTerms | Agricultural wastes Amylases Aspergillus niger Biomass Biomedical Engineering and Bioengineering biotechnology Byproducts Carbon carboxylic ester hydrolases Cell culture Cellulase culture media Date by-products endo-1,4-beta-glucanase Engineering Enzymes Extracellular Extracellular enzymes Fermentation Floods Hydrochloric acid Optimization pH effects Potassium Proteases proteinases quantitative analysis Substrates |
SummonAdditionalLinks | – databaseName: DOAJ Directory of Open Access Journals dbid: DOA link: http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwrV29b9UwELdQpy4IRAuBgoyExABR7fgj8fioqCqkMlGpmxXHNjzpNa9qXofHxn_OnZ2EviJgYcjinJWz7853F_t-JuQNRMnghYMreSt0KaOXZSN5KE3rjYqwKJsOE8Xzz_rsQn66VJd3rvrCM2EZHjhP3LGvZMdj3cQKwcE8N7WQzknhhDI6qIQEygzLydRUFdPo4wE8o4RMuYIHt87K7Y7nSQD9vy_Dd_zQ_TOS9zZKk_85fUQejoEjXWSGH5MHoX9CfpzMeMu5nJK2vadrWAaupoZ1pLD-AlFYrfDIKQ399-1VGOh1xnpFGrelC0QM_7oEmoH2S_g-HdLtEQNdgnZCQOopVqJQ_EEA9OXYezggF6cfv5ycleOlCmUHwcymVEG5rtGxMY6Dc4YAK8IYXTCRRcF5FyGD8oI72XjXmVYwp5hw0gRmonRtEIdkr1_34RmhXsS6clK3zCupHWti7Y2suqiFaw3zBeHThNtuRBxH1lc2ZR6NtllIFoRkk5DstiDv5j7XGW_jr9QfUI4zJWJlpwbQIDtqkP2XBhXkLWqBRYtGcbRjYQIMErGx7ELXRoka8tqCHE2KYkdTH2wF6YkS0nBVkNfzazBSlGvbh_XtYAX4FRgB57ogT7NezTwLRPRnEtiodzRuZ1C7b_rltwQEjtGFrKHn-0k3f7H150l7_j8m7QXZr5JtYXXmEdnb3NyGlxCebdyrZIk_AYV3OlQ priority: 102 providerName: Directory of Open Access Journals – databaseName: ProQuest Technology Collection dbid: 8FG link: http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwfV1Lb9QwELagCIkL4t1AQUZC4gBR4_iR-ISWiqVCghOV9mbFsV1W2iZLsz0st_7zzjiPskX0kIszlmzP04_5hpB3ECWDF_Y2ZRVXqQhOpKVgPtWV0zKAUdY1bhS__1DHJ-LbQi6GA7dueFY52sRoqF1b4xn5YQ5RoORCM_lp_TvFqlF4uzqU0LhL7jHwNCjn5fzrdMYC4UjJYgVGpkCXmCwWY95MqQ478J0C9tI5fHi5lm53fFOE8P_XUP_lqW6-orxxlRo91PwReTiElnTWy8Jjcsc3T8j9vtjk9im5PJqwmfvUS1o1jrZgMs7GhjZQsNVA5FcrfJ5KffNne-Y7uu5xYZHGbukM0cVPl0DT0WYJI6FdrDTR0SVIMgSvjmLWCsXDBKBPh97dM3Iy__Lz6DgdCjCkNQQ-m1R6aetShVJbXF4IxgLM1nodssAZqwPsthxnVpTO1rrimZUZt0L7TAdhK8-fk72mbfw-oY6HIrdCVZmTQtmsDIXTIq-D4rbSmUsIG5fe1AM6OQ59ZeIupVSmZ5cBdpnILrNNyIepz7rH5riV-jNydKJEXO3Y0J6fmkFNjctFzUJRhhyh6BzTBRfWCm651MpLkZD3KA8GtR_ZUQ1JDDBJxNEyM1WAlBawB07IwSgyZjALnbkW4oS8nX6DQiNfq8a3F53h4INgBoyphLzoJWwaM0f0_0zAMIod2duZ1O6fZvkrgoZjJCIK6PlxlNLrYf1_0V7ePotX5EEe9QdzNA_I3ub8wr-GIG1j30RNvAJ4bjsy priority: 102 providerName: ProQuest |
Title | Characterization and optimization of extracellular enzymes production by Aspergillus niger strains isolated from date by-products |
URI | https://link.springer.com/article/10.1186/s43141-021-00145-y https://www.ncbi.nlm.nih.gov/pubmed/33788044 https://www.proquest.com/docview/2729534915 https://www.proquest.com/docview/3153186116 https://pubmed.ncbi.nlm.nih.gov/PMC8012474 https://doaj.org/article/d24c1f78f22142d19734bb43b3596e54 |
Volume | 19 |
hasFullText | 1 |
inHoldings | 1 |
isFullTextHit | |
isPrint | |
link | http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwlV1Lb9QwELZoe4ED4k2grIyExAEi4viR-LhddamQuqoQlXqz4timK22zFdkelhv_nBknG3bLQ-KQHJyxNJOZ8czEmc-EvIEsGaKwtymruEpFcCItBfOprpyWARZlXWOheDpTJ-fi04W86GFysBdme_-elepDCwFOQMGbw4U7YOl6jxxIxlXcmFWTTR_MH0l3Yk2E5P994d2KPLf_iry1NRojzvQBud-ninTc6fYhueObR-TeFoDgY_JjMuAtd-2UtGocXcIycLUZWAYK6y8Q-cUCfzmlvvm-vvItve6wXpHGrukYEcO_zoGmpc0cuKFtPD2ipXOwTkhIHcVOFIofCIA-7We3T8j59PjL5CTtD1VIa0hmVqn00talCqW2DIIzJFgBJLZehyxwxuoAFZTjzIrS2VpXPLMy41Zon-kgbOX5U7LfLBv_nFDHQ5FboarMSaFsVobCaZHXQXFb6cwlhG1ev6l7xHFkfWFi5VEq06nMgMpMVJlZJ-TdMOe6w9v4J_URanWgRKzsOAAmZHrXMy4XNQtFGXKEl3NMF1xYK7jlUisvRULeok0Y9GhUR9U3JoCQiI1lxqrQkhdQ1ybkcGM2pnf11uRQnkguNJMJeT08BidFvVaNX960hkNcAQkYUwl51lnZwDNHRP9MABvFjv3tCLX7pJlfRiBwzC5EATPfbyz1F1t_f2kv_o_8JbmbR5_CPsxDsr_6duNfQSK2siOyV04_jsjB0fHs7PMo-uMoftSA--zs9CcE3zUs |
linkProvider | Springer Nature |
linkToHtml | http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwtR3LbtQw0CpbIbgg3iwUMBKIA0SNY8dJDghtS6stbVcItVJvbhzbZaVtsjRboXDjh_hGZvIqW0RvPewlGa9mMm_bM0PIa4iSwQtb7bGUS084I7xYMOslqUlCB0Y5yTBR3J_I8aH4fBQerZDfXS0MXqvsbGJtqE2R4R75egBRYMhFwsKP8-8eTo3C09VuhEYjFru2-gEpW_lh5xPw900QbG8dbI69dqqAl4E3X3ihDXUWSxcnmoF3ggjDmQxISZzvOGOZgxTCcKZFbHSWpNzXoc-1SKyfOKFTy-F_b5BVgRWtA7K6sTX58rXf1YEAKGb1zEcmQXtZGB11lTqxXC_BWwvI3gP44XGeVy15w3powL-u4S_fePne5qXD29onbt8ld9pglo4a6btHVmx-n9xsxltWD8ivzb4bdFPsSdPc0AKM1Gn3oHAUvAMA2dkML8RSm_-sTm1J500nWoTRFR1hP_OTKcCUNJ8CJrSsZ1uUdAq6A-GyoVgnQ3H7AuC9dnX5kBxeC3MekUFe5PYJoYa7KNBCpr4JhdR-7CKTiCBzkus08c2QsO7Tq6zth46oz1SdF8VSNexSwC5Vs0tVQ_KuXzNvuoFcCb2BHO0hsZN3_aA4O1GtYVAmEBlzUewCbH5nWBJxobXgGuRL2lAMyVuUB4X2BtmRtmUTQCR27lIjGYFeRJB1D8laJzKqNUSlulCbIXnVvwYTgnxNc1ucl4qD1wMKGJND8riRsB5njvMGfAFoREuyt0TU8pt8-q1uU46xj4hg5ftOSi_Q-v9He3o1FS_JrfHB_p7a25nsPiO3g1qXsEJ0jQwWZ-f2OYSIC_2i1UtKjq_bFPwBtl56zw |
linkToPdf | http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwtR3LbtQw0CpFIC6INwsFjATiANHGsePEB4SWlqWlUHGgUm8mju2y0jZZmq1QuPFbfB0zeZUtorcecknGkcfztj0zhDwDLxmssDMBy7gMhLciSAVzgcqsij0oZZVjoPhpT27viw8H8cEa-d3nwuC1yl4nNoraljnukY8j8AJjLhSLx767FvF5a_pm8T3ADlJ40tq302hZZNfVPyB8q17vbAGtn0fR9N2Xze2g6zAQ5GDZl0HsYpOn0qfKMLBU4G14mwNayoeeM5Z7CCcsZ0ak1uQq46GJQ26EcqHywmSOw38vkcsJTxQGfun0_bC_A65Qypruj0yCHLM4OehzdlI5rsBuC4jjI3jwYC-oV-xi0z7gXyPxl5U8e4PzzDFuYx2nN8j1zq2lk5YPb5I1V9wiV9pGl_Vt8mtzqAvdpn3SrLC0BHV11L8oPYXFBiA3n-PVWOqKn_WRq-iirUmLMKamE6xsfjgDmIoWM5gJrZouFxWdgRSB42wpZsxQ3MgA-KAbXd0h-xdCmrtkvSgLd59Qy30SGSGz0MZCmjD1iVUiyr3kJlOhHRHWL73Ou8roOPW5biKkVOqWXBrIpRty6XpEXg5jFm1dkHOh3yJFB0is6d28KI8PdacitI1EznyS-gjL4FmmEi6MEdzwWEkXixF5gfygUfMgObIugQKQxBpeeiITkJAE4u8R2ehZRncqqdKnAjQiT4fPoEyQrlnhypNKc7B_gAFjckTutRw2zJlj54FQwDSSFd5bQWr1SzH71hQsRy9IJDDyVc-lp9P6_6I9OB-LJ-QqKAD9cWdv9yG5FjWihKmiG2R9eXziHoGvuDSPG6Gk5OtFa4E_Ag59nw |
openUrl | ctx_ver=Z39.88-2004&ctx_enc=info%3Aofi%2Fenc%3AUTF-8&rfr_id=info%3Asid%2Fsummon.serialssolutions.com&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.atitle=Characterization+and+optimization+of+extracellular+enzymes+production+by+Aspergillus+niger+strains+isolated+from+date+by-products&rft.jtitle=Journal+of+Genetic+Engineering+and+Biotechnology&rft.au=Bellaouchi%2C+Reda&rft.au=Abouloifa%2C+Houssam&rft.au=Rokni%2C+Yahya&rft.au=Hasnaoui%2C+Amina&rft.date=2021-03-31&rft.pub=Springer+Berlin+Heidelberg&rft.eissn=2090-5920&rft.volume=19&rft.issue=1&rft_id=info:doi/10.1186%2Fs43141-021-00145-y&rft.externalDocID=10_1186_s43141_021_00145_y |
thumbnail_l | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/lc.gif&issn=1687-157X&client=summon |
thumbnail_m | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/mc.gif&issn=1687-157X&client=summon |
thumbnail_s | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/sc.gif&issn=1687-157X&client=summon |