Identification of an intracellular β-glucosidase in Aspergillus niger with transglycosylation activity
Aspergillus niger is featured with its copious amount of extracellular β-glucosidase which is generally used to balance the cellulolytic enzyme cocktails for lignocellulose saccharification. However, whether or not A. niger produces any intracellular β-glucosidase remains obscure. In this study, we...
Gespeichert in:
| Veröffentlicht in: | Applied microbiology and biotechnology 2020-10, Vol.104 (19), p.8367-8380 |
|---|---|
| Hauptverfasser: | , , , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 8380 |
|---|---|
| container_issue | 19 |
| container_start_page | 8367 |
| container_title | Applied microbiology and biotechnology |
| container_volume | 104 |
| creator | Zhao, Jun Shi, Dingchen Yang, Sen Lin, Hui Chen, Hongge |
| description | Aspergillus niger
is featured with its copious amount of extracellular β-glucosidase which is generally used to balance the cellulolytic enzyme cocktails for lignocellulose saccharification. However, whether or not
A. niger
produces any intracellular β-glucosidase remains obscure. In this study, we analyzed a total of fifteen putative β-glucosidase genes (
bgl
s) in
A. niger
CBS 513.88 genome and the five of them were predicted as intracellular
bgl
s due to the lack of signal peptide of extracellular proteins. After further characterization of these five genes through a
Saccharomyces cerevisiae
in vivo system, only An03g03740 (designated
bgl1B
) was confirmed to be a β-glucosidase gene. Western blot and mass spectrometry analysis confirmed BGL1B protein localization inside the cell. BGL1B exhibited the maximal activity at 40 °C and pH 5.6. The
K
m
for
p
-nitrophenyl-β-
d
-glucopyranoside and
K
i
for glucose were 0.233 ± 0.058 mM and 119.8 ± 4.35 mM, respectively. BGL1B showed a strong transglycosylation activity while hydrolyzing cellodextrins with sophorose, laminaribiose, and cellotriose formed from cellobiose, and sophorose and laminaribiose formed from cellotriose. The confirmation of the intracellular β-glucosidase BGL1B in
A. niger
further extends our understanding of how
A. niger
utilizes lignocellulose.
Key points
•
Identification of putative genes revealed a novel β-glucosidase in Aspergillus niger.
•
Newly identified β-glucosidase BGL1B was an intracellular enzyme of A. niger.
•
BGL1B exhibited a strong transglycosylation activity. |
| doi_str_mv | 10.1007/s00253-020-10840-4 |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_2436395908</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>2439758914</sourcerecordid><originalsourceid>FETCH-LOGICAL-c375t-b988e7911e83024aed234ff317329a803a97b886a9c15919e23cbad9be55c4433</originalsourceid><addsrcrecordid>eNp9kc9O3DAYxK2qqCxLX6CHKhKXXlw-_4vtI0IUkJC4wNlyHCc1yjqLnbTa1-qD8Ez1EgoSh558mN-M7RmEvhD4TgDkaQaggmGggAkoDph_QCvCGcVQE_4RrYBIgaXQ6hAd5fwAQKiq60_okFFFgUm-Qv116-MUuuDsFMZYjV1lYxXilKzzwzAPNlVPf3A_zG7MobXZF7E6y1uf-lD0XMXQ-1T9DtPPqphi7oddQXfDkmfdFH6FaXeMDjo7ZP_55Vyj-x8Xd-dX-Ob28vr87AY7JsWEG62Ul5oQrxhQbn1LGe86RiSj2ipgVstGqdpqR4Qm2lPmGtvqxgvhOGdsjb4tuds0Ps4-T2YT8v4nNvpxzoZyVjMtNKiCnrxDH8Y5xfK6PaWlULqUuUZ0oVwac06-M9sUNjbtDAGzn8EsM5gyg3mewexNX1-i52bj21fLv94LwBYgFymWAt_u_k_sX644lD8</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>2439758914</pqid></control><display><type>article</type><title>Identification of an intracellular β-glucosidase in Aspergillus niger with transglycosylation activity</title><source>MEDLINE</source><source>SpringerLink Journals - AutoHoldings</source><creator>Zhao, Jun ; Shi, Dingchen ; Yang, Sen ; Lin, Hui ; Chen, Hongge</creator><creatorcontrib>Zhao, Jun ; Shi, Dingchen ; Yang, Sen ; Lin, Hui ; Chen, Hongge</creatorcontrib><description>Aspergillus niger
is featured with its copious amount of extracellular β-glucosidase which is generally used to balance the cellulolytic enzyme cocktails for lignocellulose saccharification. However, whether or not
A. niger
produces any intracellular β-glucosidase remains obscure. In this study, we analyzed a total of fifteen putative β-glucosidase genes (
bgl
s) in
A. niger
CBS 513.88 genome and the five of them were predicted as intracellular
bgl
s due to the lack of signal peptide of extracellular proteins. After further characterization of these five genes through a
Saccharomyces cerevisiae
in vivo system, only An03g03740 (designated
bgl1B
) was confirmed to be a β-glucosidase gene. Western blot and mass spectrometry analysis confirmed BGL1B protein localization inside the cell. BGL1B exhibited the maximal activity at 40 °C and pH 5.6. The
K
m
for
p
-nitrophenyl-β-
d
-glucopyranoside and
K
i
for glucose were 0.233 ± 0.058 mM and 119.8 ± 4.35 mM, respectively. BGL1B showed a strong transglycosylation activity while hydrolyzing cellodextrins with sophorose, laminaribiose, and cellotriose formed from cellobiose, and sophorose and laminaribiose formed from cellotriose. The confirmation of the intracellular β-glucosidase BGL1B in
A. niger
further extends our understanding of how
A. niger
utilizes lignocellulose.
Key points
•
Identification of putative genes revealed a novel β-glucosidase in Aspergillus niger.
•
Newly identified β-glucosidase BGL1B was an intracellular enzyme of A. niger.
•
BGL1B exhibited a strong transglycosylation activity.</description><identifier>ISSN: 0175-7598</identifier><identifier>EISSN: 1432-0614</identifier><identifier>DOI: 10.1007/s00253-020-10840-4</identifier><identifier>PMID: 32820374</identifier><language>eng</language><publisher>Berlin/Heidelberg: Springer Berlin Heidelberg</publisher><subject>Antigens, Fungal ; Applied Genetics and Molecular Biotechnology ; Aspergillus niger ; Aspergillus niger - genetics ; Aspergillus niger - metabolism ; beta-Glucosidase - genetics ; beta-Glucosidase - metabolism ; Biomedical and Life Sciences ; Biotechnology ; Cellobiase ; Cellobiose ; Enzymes ; Genes ; Genomes ; Glucose ; Glucosidase ; Intracellular ; Kinetics ; Life Sciences ; Lignocellulose ; Localization ; Mass spectrometry ; Mass spectroscopy ; Microbial Genetics and Genomics ; Microbiology ; p-Nitrophenyl-b-D-glucopyranoside ; Proteins ; Saccharification ; Sophorose ; VOCs ; Volatile organic compounds ; β-Glucosidase</subject><ispartof>Applied microbiology and biotechnology, 2020-10, Vol.104 (19), p.8367-8380</ispartof><rights>Springer-Verlag GmbH Germany, part of Springer Nature 2020</rights><rights>Springer-Verlag GmbH Germany, part of Springer Nature 2020.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c375t-b988e7911e83024aed234ff317329a803a97b886a9c15919e23cbad9be55c4433</citedby><cites>FETCH-LOGICAL-c375t-b988e7911e83024aed234ff317329a803a97b886a9c15919e23cbad9be55c4433</cites><orcidid>0000-0002-7519-7341</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1007/s00253-020-10840-4$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1007/s00253-020-10840-4$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>314,780,784,27924,27925,41488,42557,51319</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/32820374$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Zhao, Jun</creatorcontrib><creatorcontrib>Shi, Dingchen</creatorcontrib><creatorcontrib>Yang, Sen</creatorcontrib><creatorcontrib>Lin, Hui</creatorcontrib><creatorcontrib>Chen, Hongge</creatorcontrib><title>Identification of an intracellular β-glucosidase in Aspergillus niger with transglycosylation activity</title><title>Applied microbiology and biotechnology</title><addtitle>Appl Microbiol Biotechnol</addtitle><addtitle>Appl Microbiol Biotechnol</addtitle><description>Aspergillus niger
is featured with its copious amount of extracellular β-glucosidase which is generally used to balance the cellulolytic enzyme cocktails for lignocellulose saccharification. However, whether or not
A. niger
produces any intracellular β-glucosidase remains obscure. In this study, we analyzed a total of fifteen putative β-glucosidase genes (
bgl
s) in
A. niger
CBS 513.88 genome and the five of them were predicted as intracellular
bgl
s due to the lack of signal peptide of extracellular proteins. After further characterization of these five genes through a
Saccharomyces cerevisiae
in vivo system, only An03g03740 (designated
bgl1B
) was confirmed to be a β-glucosidase gene. Western blot and mass spectrometry analysis confirmed BGL1B protein localization inside the cell. BGL1B exhibited the maximal activity at 40 °C and pH 5.6. The
K
m
for
p
-nitrophenyl-β-
d
-glucopyranoside and
K
i
for glucose were 0.233 ± 0.058 mM and 119.8 ± 4.35 mM, respectively. BGL1B showed a strong transglycosylation activity while hydrolyzing cellodextrins with sophorose, laminaribiose, and cellotriose formed from cellobiose, and sophorose and laminaribiose formed from cellotriose. The confirmation of the intracellular β-glucosidase BGL1B in
A. niger
further extends our understanding of how
A. niger
utilizes lignocellulose.
Key points
•
Identification of putative genes revealed a novel β-glucosidase in Aspergillus niger.
•
Newly identified β-glucosidase BGL1B was an intracellular enzyme of A. niger.
•
BGL1B exhibited a strong transglycosylation activity.</description><subject>Antigens, Fungal</subject><subject>Applied Genetics and Molecular Biotechnology</subject><subject>Aspergillus niger</subject><subject>Aspergillus niger - genetics</subject><subject>Aspergillus niger - metabolism</subject><subject>beta-Glucosidase - genetics</subject><subject>beta-Glucosidase - metabolism</subject><subject>Biomedical and Life Sciences</subject><subject>Biotechnology</subject><subject>Cellobiase</subject><subject>Cellobiose</subject><subject>Enzymes</subject><subject>Genes</subject><subject>Genomes</subject><subject>Glucose</subject><subject>Glucosidase</subject><subject>Intracellular</subject><subject>Kinetics</subject><subject>Life Sciences</subject><subject>Lignocellulose</subject><subject>Localization</subject><subject>Mass spectrometry</subject><subject>Mass spectroscopy</subject><subject>Microbial Genetics and Genomics</subject><subject>Microbiology</subject><subject>p-Nitrophenyl-b-D-glucopyranoside</subject><subject>Proteins</subject><subject>Saccharification</subject><subject>Sophorose</subject><subject>VOCs</subject><subject>Volatile organic compounds</subject><subject>β-Glucosidase</subject><issn>0175-7598</issn><issn>1432-0614</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2020</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><recordid>eNp9kc9O3DAYxK2qqCxLX6CHKhKXXlw-_4vtI0IUkJC4wNlyHCc1yjqLnbTa1-qD8Ez1EgoSh558mN-M7RmEvhD4TgDkaQaggmGggAkoDph_QCvCGcVQE_4RrYBIgaXQ6hAd5fwAQKiq60_okFFFgUm-Qv116-MUuuDsFMZYjV1lYxXilKzzwzAPNlVPf3A_zG7MobXZF7E6y1uf-lD0XMXQ-1T9DtPPqphi7oddQXfDkmfdFH6FaXeMDjo7ZP_55Vyj-x8Xd-dX-Ob28vr87AY7JsWEG62Ul5oQrxhQbn1LGe86RiSj2ipgVstGqdpqR4Qm2lPmGtvqxgvhOGdsjb4tuds0Ps4-T2YT8v4nNvpxzoZyVjMtNKiCnrxDH8Y5xfK6PaWlULqUuUZ0oVwac06-M9sUNjbtDAGzn8EsM5gyg3mewexNX1-i52bj21fLv94LwBYgFymWAt_u_k_sX644lD8</recordid><startdate>20201001</startdate><enddate>20201001</enddate><creator>Zhao, Jun</creator><creator>Shi, Dingchen</creator><creator>Yang, Sen</creator><creator>Lin, Hui</creator><creator>Chen, Hongge</creator><general>Springer Berlin Heidelberg</general><general>Springer Nature B.V</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>3V.</scope><scope>7QL</scope><scope>7T7</scope><scope>7WY</scope><scope>7WZ</scope><scope>7X7</scope><scope>7XB</scope><scope>87Z</scope><scope>88A</scope><scope>88E</scope><scope>88I</scope><scope>8AO</scope><scope>8FD</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>8FL</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BEZIV</scope><scope>BHPHI</scope><scope>C1K</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FRNLG</scope><scope>FYUFA</scope><scope>F~G</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>HCIFZ</scope><scope>K60</scope><scope>K6~</scope><scope>K9.</scope><scope>L.-</scope><scope>LK8</scope><scope>M0C</scope><scope>M0S</scope><scope>M1P</scope><scope>M2P</scope><scope>M7N</scope><scope>M7P</scope><scope>P64</scope><scope>PQBIZ</scope><scope>PQBZA</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>Q9U</scope><scope>7X8</scope><orcidid>https://orcid.org/0000-0002-7519-7341</orcidid></search><sort><creationdate>20201001</creationdate><title>Identification of an intracellular β-glucosidase in Aspergillus niger with transglycosylation activity</title><author>Zhao, Jun ; Shi, Dingchen ; Yang, Sen ; Lin, Hui ; Chen, Hongge</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c375t-b988e7911e83024aed234ff317329a803a97b886a9c15919e23cbad9be55c4433</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2020</creationdate><topic>Antigens, Fungal</topic><topic>Applied Genetics and Molecular Biotechnology</topic><topic>Aspergillus niger</topic><topic>Aspergillus niger - genetics</topic><topic>Aspergillus niger - metabolism</topic><topic>beta-Glucosidase - genetics</topic><topic>beta-Glucosidase - metabolism</topic><topic>Biomedical and Life Sciences</topic><topic>Biotechnology</topic><topic>Cellobiase</topic><topic>Cellobiose</topic><topic>Enzymes</topic><topic>Genes</topic><topic>Genomes</topic><topic>Glucose</topic><topic>Glucosidase</topic><topic>Intracellular</topic><topic>Kinetics</topic><topic>Life Sciences</topic><topic>Lignocellulose</topic><topic>Localization</topic><topic>Mass spectrometry</topic><topic>Mass spectroscopy</topic><topic>Microbial Genetics and Genomics</topic><topic>Microbiology</topic><topic>p-Nitrophenyl-b-D-glucopyranoside</topic><topic>Proteins</topic><topic>Saccharification</topic><topic>Sophorose</topic><topic>VOCs</topic><topic>Volatile organic compounds</topic><topic>β-Glucosidase</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Zhao, Jun</creatorcontrib><creatorcontrib>Shi, Dingchen</creatorcontrib><creatorcontrib>Yang, Sen</creatorcontrib><creatorcontrib>Lin, Hui</creatorcontrib><creatorcontrib>Chen, Hongge</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Industrial and Applied Microbiology Abstracts (Microbiology A)</collection><collection>ABI/INFORM Collection</collection><collection>ABI/INFORM Global (PDF only)</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>ABI/INFORM Global (Alumni Edition)</collection><collection>Biology Database (Alumni Edition)</collection><collection>Medical Database (Alumni Edition)</collection><collection>Science Database (Alumni Edition)</collection><collection>ProQuest Pharma Collection</collection><collection>Technology Research Database</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>ABI/INFORM Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest Central UK/Ireland</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Business Premium Collection</collection><collection>Natural Science Collection</collection><collection>Environmental Sciences and Pollution Management</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</collection><collection>Engineering Research Database</collection><collection>Business Premium Collection (Alumni)</collection><collection>Health Research Premium Collection</collection><collection>ABI/INFORM Global (Corporate)</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Business Collection (Alumni Edition)</collection><collection>ProQuest Business Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>ABI/INFORM Professional Advanced</collection><collection>ProQuest Biological Science Collection</collection><collection>ABI/INFORM Global</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Science Database</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biological Science Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>ProQuest One Business</collection><collection>ProQuest One Business (Alumni)</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central Basic</collection><collection>MEDLINE - Academic</collection><jtitle>Applied microbiology and biotechnology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Zhao, Jun</au><au>Shi, Dingchen</au><au>Yang, Sen</au><au>Lin, Hui</au><au>Chen, Hongge</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Identification of an intracellular β-glucosidase in Aspergillus niger with transglycosylation activity</atitle><jtitle>Applied microbiology and biotechnology</jtitle><stitle>Appl Microbiol Biotechnol</stitle><addtitle>Appl Microbiol Biotechnol</addtitle><date>2020-10-01</date><risdate>2020</risdate><volume>104</volume><issue>19</issue><spage>8367</spage><epage>8380</epage><pages>8367-8380</pages><issn>0175-7598</issn><eissn>1432-0614</eissn><abstract>Aspergillus niger
is featured with its copious amount of extracellular β-glucosidase which is generally used to balance the cellulolytic enzyme cocktails for lignocellulose saccharification. However, whether or not
A. niger
produces any intracellular β-glucosidase remains obscure. In this study, we analyzed a total of fifteen putative β-glucosidase genes (
bgl
s) in
A. niger
CBS 513.88 genome and the five of them were predicted as intracellular
bgl
s due to the lack of signal peptide of extracellular proteins. After further characterization of these five genes through a
Saccharomyces cerevisiae
in vivo system, only An03g03740 (designated
bgl1B
) was confirmed to be a β-glucosidase gene. Western blot and mass spectrometry analysis confirmed BGL1B protein localization inside the cell. BGL1B exhibited the maximal activity at 40 °C and pH 5.6. The
K
m
for
p
-nitrophenyl-β-
d
-glucopyranoside and
K
i
for glucose were 0.233 ± 0.058 mM and 119.8 ± 4.35 mM, respectively. BGL1B showed a strong transglycosylation activity while hydrolyzing cellodextrins with sophorose, laminaribiose, and cellotriose formed from cellobiose, and sophorose and laminaribiose formed from cellotriose. The confirmation of the intracellular β-glucosidase BGL1B in
A. niger
further extends our understanding of how
A. niger
utilizes lignocellulose.
Key points
•
Identification of putative genes revealed a novel β-glucosidase in Aspergillus niger.
•
Newly identified β-glucosidase BGL1B was an intracellular enzyme of A. niger.
•
BGL1B exhibited a strong transglycosylation activity.</abstract><cop>Berlin/Heidelberg</cop><pub>Springer Berlin Heidelberg</pub><pmid>32820374</pmid><doi>10.1007/s00253-020-10840-4</doi><tpages>14</tpages><orcidid>https://orcid.org/0000-0002-7519-7341</orcidid></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0175-7598 |
| ispartof | Applied microbiology and biotechnology, 2020-10, Vol.104 (19), p.8367-8380 |
| issn | 0175-7598 1432-0614 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_2436395908 |
| source | MEDLINE; SpringerLink Journals - AutoHoldings |
| subjects | Antigens, Fungal Applied Genetics and Molecular Biotechnology Aspergillus niger Aspergillus niger - genetics Aspergillus niger - metabolism beta-Glucosidase - genetics beta-Glucosidase - metabolism Biomedical and Life Sciences Biotechnology Cellobiase Cellobiose Enzymes Genes Genomes Glucose Glucosidase Intracellular Kinetics Life Sciences Lignocellulose Localization Mass spectrometry Mass spectroscopy Microbial Genetics and Genomics Microbiology p-Nitrophenyl-b-D-glucopyranoside Proteins Saccharification Sophorose VOCs Volatile organic compounds β-Glucosidase |
| title | Identification of an intracellular β-glucosidase in Aspergillus niger with transglycosylation activity |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-05T14%3A49%3A44IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Identification%20of%20an%20intracellular%20%CE%B2-glucosidase%20in%20Aspergillus%20niger%20with%20transglycosylation%20activity&rft.jtitle=Applied%20microbiology%20and%20biotechnology&rft.au=Zhao,%20Jun&rft.date=2020-10-01&rft.volume=104&rft.issue=19&rft.spage=8367&rft.epage=8380&rft.pages=8367-8380&rft.issn=0175-7598&rft.eissn=1432-0614&rft_id=info:doi/10.1007/s00253-020-10840-4&rft_dat=%3Cproquest_cross%3E2439758914%3C/proquest_cross%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=2439758914&rft_id=info:pmid/32820374&rfr_iscdi=true |