Purification, Identification, and Characterization of a Glycoside Hydrolase Family 11-Xylanase with High Activity from Aspergillus niger VTCC 017
Xylanases (EC 3.2.1.8) have been considered as a potential green solution for the sustainable development of a wide range of industries including pulp and paper, food and beverages, animal feed, pharmaceuticals, and biofuels because they are the key enzymes that degrade the xylosidic linkages of xyl...
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| Veröffentlicht in: | Molecular biotechnology 2022-02, Vol.64 (2), p.187-198 |
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| description | Xylanases (EC 3.2.1.8) have been considered as a potential green solution for the sustainable development of a wide range of industries including pulp and paper, food and beverages, animal feed, pharmaceuticals, and biofuels because they are the key enzymes that degrade the xylosidic linkages of xylan, the major component of the second most abundant raw material worldwide. Therefore, there is a critical need for the industrialized xylanases which must have high specific activity, be tolerant to organic solvent or detergent and be active during a wide range of conditions, such as high temperature and pH. In this study, an extracellular xylanase was purified from the culture broth of
Aspergillus niger
VTCC 017 for primary structure determination and properties characterization. The successive steps of purification comprised centrifugation, Sephadex G-100 filtration, and DEAE-Sephadex chromatography. The purified xylanase (specific activity reached 6596.79 UI/mg protein) was a monomer with a molecular weight of 37 kDa estimating from SDS electrophoresis. The results of LC/MS suggested that the purified protein is indeed an endo-1,4-β-
d
-xylanase. The purified xylanase showed the optimal temperature of 55 °C, and pH 6.5 with a stable xylanolytic activity within the temperature range of 45–50 °C, and within the pH range of 5.0–8.0. Most divalent metal cations including Zn
2+
, Fe
2+
, Mg
2+
, Cu
2+
, Mn
2+
showed some inhibition of xylanase activity while the monovalent metal cations such as K
+
and Ag
+
exhibited slight stimulating effects on the enzyme activity. The introduction of 10–30% different organic solvents (n-butanol, acetone, isopropanol) and several detergents (Triton X-100, Tween 20, and SDS) slightly reduced the enzyme activity. Moreover, the purified xylanase seemed to be tolerant to methanol and ethanol and was even stimulated by Tween 80. Overall, with these distinctive properties, the putative xylanase could be a successful candidate for numerous industrial uses.
Graphic Abstract |
| doi_str_mv | 10.1007/s12033-021-00395-8 |
| format | Article |
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Aspergillus niger
VTCC 017 for primary structure determination and properties characterization. The successive steps of purification comprised centrifugation, Sephadex G-100 filtration, and DEAE-Sephadex chromatography. The purified xylanase (specific activity reached 6596.79 UI/mg protein) was a monomer with a molecular weight of 37 kDa estimating from SDS electrophoresis. The results of LC/MS suggested that the purified protein is indeed an endo-1,4-β-
d
-xylanase. The purified xylanase showed the optimal temperature of 55 °C, and pH 6.5 with a stable xylanolytic activity within the temperature range of 45–50 °C, and within the pH range of 5.0–8.0. Most divalent metal cations including Zn
2+
, Fe
2+
, Mg
2+
, Cu
2+
, Mn
2+
showed some inhibition of xylanase activity while the monovalent metal cations such as K
+
and Ag
+
exhibited slight stimulating effects on the enzyme activity. The introduction of 10–30% different organic solvents (n-butanol, acetone, isopropanol) and several detergents (Triton X-100, Tween 20, and SDS) slightly reduced the enzyme activity. Moreover, the purified xylanase seemed to be tolerant to methanol and ethanol and was even stimulated by Tween 80. Overall, with these distinctive properties, the putative xylanase could be a successful candidate for numerous industrial uses.
Graphic Abstract</description><identifier>ISSN: 1073-6085</identifier><identifier>EISSN: 1559-0305</identifier><identifier>DOI: 10.1007/s12033-021-00395-8</identifier><identifier>PMID: 34580814</identifier><language>eng</language><publisher>New York: Springer US</publisher><subject>Amino acid sequence ; Animal feed ; Aspergillus niger ; Aspergillus niger - enzymology ; Beverages ; Biochemistry ; Biofuels ; Biological Techniques ; Biotechnology ; Butanol ; Cations ; Cell Biology ; Centrifugation ; Chemistry ; Chemistry and Materials Science ; Copper ; Detergents ; Detergents - chemistry ; Dextrans ; Electrophoresis ; Electrophoresis, Polyacrylamide Gel ; Enzymatic activity ; Enzyme activity ; Enzyme Stability ; Enzymes ; Ethanol ; Feeds ; Filtration - methods ; Fungal Proteins - chemistry ; Fungal Proteins - isolation & purification ; Fungal Proteins - metabolism ; Glycosidases ; Glycoside hydrolase ; High temperature ; Human Genetics ; Hydrogen-Ion Concentration ; Hydrolase ; Industrial applications ; Iron ; Kinetics ; Magnesium ; Metal ions ; Metals - chemistry ; Molecular weight ; Organic solvents ; Original Paper ; pH effects ; Protein Science ; Proteins ; Purification ; Silver ; Solvents ; Solvents - chemistry ; Structural analysis ; Sustainable development ; Temperature ; Xylan ; Xylanase ; Xylosidases - chemistry ; Xylosidases - isolation & purification ; Xylosidases - metabolism ; Zinc</subject><ispartof>Molecular biotechnology, 2022-02, Vol.64 (2), p.187-198</ispartof><rights>The Author(s), under exclusive licence to Springer Science+Business Media, LLC, part of Springer Nature 2021</rights><rights>2021. The Author(s), under exclusive licence to Springer Science+Business Media, LLC, part of Springer Nature.</rights><rights>The Author(s), under exclusive licence to Springer Science+Business Media, LLC, part of Springer Nature 2021.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c375t-57e154ee6a266ecbdf07f8816ef5f9c1f5b8da06cad40204344bb35b5f30e3c13</citedby><cites>FETCH-LOGICAL-c375t-57e154ee6a266ecbdf07f8816ef5f9c1f5b8da06cad40204344bb35b5f30e3c13</cites><orcidid>0000-0002-8048-5794</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/s12033-021-00395-8$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1007/s12033-021-00395-8$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>314,776,780,27901,27902,41464,42533,51294</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/34580814$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Dao, Thi Mai Anh</creatorcontrib><creatorcontrib>Cuong, Nguyen Tien</creatorcontrib><creatorcontrib>Nguyen, Thi Trung</creatorcontrib><creatorcontrib>Nguyen, Nguyen Phuong Dai</creatorcontrib><creatorcontrib>Tuyen, Do Thi</creatorcontrib><title>Purification, Identification, and Characterization of a Glycoside Hydrolase Family 11-Xylanase with High Activity from Aspergillus niger VTCC 017</title><title>Molecular biotechnology</title><addtitle>Mol Biotechnol</addtitle><addtitle>Mol Biotechnol</addtitle><description>Xylanases (EC 3.2.1.8) have been considered as a potential green solution for the sustainable development of a wide range of industries including pulp and paper, food and beverages, animal feed, pharmaceuticals, and biofuels because they are the key enzymes that degrade the xylosidic linkages of xylan, the major component of the second most abundant raw material worldwide. Therefore, there is a critical need for the industrialized xylanases which must have high specific activity, be tolerant to organic solvent or detergent and be active during a wide range of conditions, such as high temperature and pH. In this study, an extracellular xylanase was purified from the culture broth of
Aspergillus niger
VTCC 017 for primary structure determination and properties characterization. The successive steps of purification comprised centrifugation, Sephadex G-100 filtration, and DEAE-Sephadex chromatography. The purified xylanase (specific activity reached 6596.79 UI/mg protein) was a monomer with a molecular weight of 37 kDa estimating from SDS electrophoresis. The results of LC/MS suggested that the purified protein is indeed an endo-1,4-β-
d
-xylanase. The purified xylanase showed the optimal temperature of 55 °C, and pH 6.5 with a stable xylanolytic activity within the temperature range of 45–50 °C, and within the pH range of 5.0–8.0. Most divalent metal cations including Zn
2+
, Fe
2+
, Mg
2+
, Cu
2+
, Mn
2+
showed some inhibition of xylanase activity while the monovalent metal cations such as K
+
and Ag
+
exhibited slight stimulating effects on the enzyme activity. The introduction of 10–30% different organic solvents (n-butanol, acetone, isopropanol) and several detergents (Triton X-100, Tween 20, and SDS) slightly reduced the enzyme activity. Moreover, the purified xylanase seemed to be tolerant to methanol and ethanol and was even stimulated by Tween 80. Overall, with these distinctive properties, the putative xylanase could be a successful candidate for numerous industrial uses.
Graphic Abstract</description><subject>Amino acid sequence</subject><subject>Animal feed</subject><subject>Aspergillus niger</subject><subject>Aspergillus niger - enzymology</subject><subject>Beverages</subject><subject>Biochemistry</subject><subject>Biofuels</subject><subject>Biological Techniques</subject><subject>Biotechnology</subject><subject>Butanol</subject><subject>Cations</subject><subject>Cell Biology</subject><subject>Centrifugation</subject><subject>Chemistry</subject><subject>Chemistry and Materials Science</subject><subject>Copper</subject><subject>Detergents</subject><subject>Detergents - chemistry</subject><subject>Dextrans</subject><subject>Electrophoresis</subject><subject>Electrophoresis, Polyacrylamide Gel</subject><subject>Enzymatic activity</subject><subject>Enzyme activity</subject><subject>Enzyme Stability</subject><subject>Enzymes</subject><subject>Ethanol</subject><subject>Feeds</subject><subject>Filtration - methods</subject><subject>Fungal Proteins - chemistry</subject><subject>Fungal Proteins - isolation & purification</subject><subject>Fungal Proteins - metabolism</subject><subject>Glycosidases</subject><subject>Glycoside hydrolase</subject><subject>High temperature</subject><subject>Human Genetics</subject><subject>Hydrogen-Ion Concentration</subject><subject>Hydrolase</subject><subject>Industrial applications</subject><subject>Iron</subject><subject>Kinetics</subject><subject>Magnesium</subject><subject>Metal ions</subject><subject>Metals - chemistry</subject><subject>Molecular weight</subject><subject>Organic solvents</subject><subject>Original Paper</subject><subject>pH effects</subject><subject>Protein Science</subject><subject>Proteins</subject><subject>Purification</subject><subject>Silver</subject><subject>Solvents</subject><subject>Solvents - chemistry</subject><subject>Structural analysis</subject><subject>Sustainable development</subject><subject>Temperature</subject><subject>Xylan</subject><subject>Xylanase</subject><subject>Xylosidases - chemistry</subject><subject>Xylosidases - isolation & purification</subject><subject>Xylosidases - metabolism</subject><subject>Zinc</subject><issn>1073-6085</issn><issn>1559-0305</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2022</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>BENPR</sourceid><recordid>eNp9kc9u1DAQxi0EoqXwAhyQJS4cMIxjO3aOq4h2K1WCQ0HcLMexd10l8WInoPAWvDFut_wRB062Z37zzYw_hJ5TeEMB5NtMK2CMQEUJAGsEUQ_QKRWiIcBAPCx3kIzUoMQJepLzDRRScPYYnTAuFCjKT9GPD0sKPlgzhzi9xpe9m-a_3mbqcbs3ydjZpfD9LoqjxwZfDKuNOfQOb9c-xcFkh8_NGIYVU0o-r4OZbkPfwrzH27Db442dw9cwr9inOOJNPri0C8OwZDyFnUv403XbYqDyKXrkzZDds_vzDH08f3fdbsnV-4vLdnNFLJNiJkK6soxztanq2tmu9yC9UrR2XvjGUi861Ruorek5VMAZ513HRCc8A8csZWfo1VH3kOKXxeVZjyFbN5TBXVyyroSUXHBQTUFf_oPexCVNZTpd1RUoJhspClUdKZtizsl5fUhhNGnVFPStYfpomC426DvDtCpFL-6ll250_e-SXw4VgB2BXFJT-ag_vf8j-xMcWKER</recordid><startdate>20220201</startdate><enddate>20220201</enddate><creator>Dao, Thi Mai Anh</creator><creator>Cuong, Nguyen Tien</creator><creator>Nguyen, Thi Trung</creator><creator>Nguyen, Nguyen Phuong Dai</creator><creator>Tuyen, Do Thi</creator><general>Springer US</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>7QO</scope><scope>7T7</scope><scope>7U9</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88E</scope><scope>88I</scope><scope>8AO</scope><scope>8FD</scope><scope>8FE</scope><scope>8FG</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABJCF</scope><scope>ABUWG</scope><scope>AEUYN</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BGLVJ</scope><scope>BHPHI</scope><scope>C1K</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>H94</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>L6V</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M2P</scope><scope>M7N</scope><scope>M7P</scope><scope>M7S</scope><scope>P64</scope><scope>PHGZM</scope><scope>PHGZT</scope><scope>PJZUB</scope><scope>PKEHL</scope><scope>PPXIY</scope><scope>PQEST</scope><scope>PQGLB</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PTHSS</scope><scope>Q9U</scope><scope>7X8</scope><orcidid>https://orcid.org/0000-0002-8048-5794</orcidid></search><sort><creationdate>20220201</creationdate><title>Purification, Identification, and Characterization of a Glycoside Hydrolase Family 11-Xylanase with High Activity from Aspergillus niger VTCC 017</title><author>Dao, Thi Mai Anh ; Cuong, Nguyen Tien ; Nguyen, Thi Trung ; Nguyen, Nguyen Phuong Dai ; Tuyen, Do Thi</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c375t-57e154ee6a266ecbdf07f8816ef5f9c1f5b8da06cad40204344bb35b5f30e3c13</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2022</creationdate><topic>Amino acid sequence</topic><topic>Animal feed</topic><topic>Aspergillus niger</topic><topic>Aspergillus niger - enzymology</topic><topic>Beverages</topic><topic>Biochemistry</topic><topic>Biofuels</topic><topic>Biological Techniques</topic><topic>Biotechnology</topic><topic>Butanol</topic><topic>Cations</topic><topic>Cell Biology</topic><topic>Centrifugation</topic><topic>Chemistry</topic><topic>Chemistry and Materials Science</topic><topic>Copper</topic><topic>Detergents</topic><topic>Detergents - chemistry</topic><topic>Dextrans</topic><topic>Electrophoresis</topic><topic>Electrophoresis, Polyacrylamide Gel</topic><topic>Enzymatic activity</topic><topic>Enzyme activity</topic><topic>Enzyme Stability</topic><topic>Enzymes</topic><topic>Ethanol</topic><topic>Feeds</topic><topic>Filtration - methods</topic><topic>Fungal Proteins - chemistry</topic><topic>Fungal Proteins - isolation & purification</topic><topic>Fungal Proteins - metabolism</topic><topic>Glycosidases</topic><topic>Glycoside hydrolase</topic><topic>High temperature</topic><topic>Human Genetics</topic><topic>Hydrogen-Ion Concentration</topic><topic>Hydrolase</topic><topic>Industrial applications</topic><topic>Iron</topic><topic>Kinetics</topic><topic>Magnesium</topic><topic>Metal ions</topic><topic>Metals - chemistry</topic><topic>Molecular weight</topic><topic>Organic solvents</topic><topic>Original Paper</topic><topic>pH effects</topic><topic>Protein Science</topic><topic>Proteins</topic><topic>Purification</topic><topic>Silver</topic><topic>Solvents</topic><topic>Solvents - chemistry</topic><topic>Structural analysis</topic><topic>Sustainable development</topic><topic>Temperature</topic><topic>Xylan</topic><topic>Xylanase</topic><topic>Xylosidases - chemistry</topic><topic>Xylosidases - isolation & purification</topic><topic>Xylosidases - metabolism</topic><topic>Zinc</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Dao, Thi Mai Anh</creatorcontrib><creatorcontrib>Cuong, Nguyen Tien</creatorcontrib><creatorcontrib>Nguyen, Thi Trung</creatorcontrib><creatorcontrib>Nguyen, Nguyen Phuong Dai</creatorcontrib><creatorcontrib>Tuyen, Do Thi</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>Biotechnology Research Abstracts</collection><collection>Industrial and Applied Microbiology Abstracts (Microbiology A)</collection><collection>Virology and AIDS Abstracts</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</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 Technology 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>Materials Science & Engineering Collection</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest One Sustainability</collection><collection>ProQuest Central UK/Ireland</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Technology 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>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>ProQuest Engineering Collection</collection><collection>ProQuest Biological Science Collection</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>Engineering Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>ProQuest Central (New)</collection><collection>ProQuest One Academic (New)</collection><collection>ProQuest Health & Medical Research Collection</collection><collection>ProQuest One Academic Middle East (New)</collection><collection>ProQuest One Health & Nursing</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Applied & Life Sciences</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>Engineering Collection</collection><collection>ProQuest Central Basic</collection><collection>MEDLINE - Academic</collection><jtitle>Molecular biotechnology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Dao, Thi Mai Anh</au><au>Cuong, Nguyen Tien</au><au>Nguyen, Thi Trung</au><au>Nguyen, Nguyen Phuong Dai</au><au>Tuyen, Do Thi</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Purification, Identification, and Characterization of a Glycoside Hydrolase Family 11-Xylanase with High Activity from Aspergillus niger VTCC 017</atitle><jtitle>Molecular biotechnology</jtitle><stitle>Mol Biotechnol</stitle><addtitle>Mol Biotechnol</addtitle><date>2022-02-01</date><risdate>2022</risdate><volume>64</volume><issue>2</issue><spage>187</spage><epage>198</epage><pages>187-198</pages><issn>1073-6085</issn><eissn>1559-0305</eissn><abstract>Xylanases (EC 3.2.1.8) have been considered as a potential green solution for the sustainable development of a wide range of industries including pulp and paper, food and beverages, animal feed, pharmaceuticals, and biofuels because they are the key enzymes that degrade the xylosidic linkages of xylan, the major component of the second most abundant raw material worldwide. Therefore, there is a critical need for the industrialized xylanases which must have high specific activity, be tolerant to organic solvent or detergent and be active during a wide range of conditions, such as high temperature and pH. In this study, an extracellular xylanase was purified from the culture broth of
Aspergillus niger
VTCC 017 for primary structure determination and properties characterization. The successive steps of purification comprised centrifugation, Sephadex G-100 filtration, and DEAE-Sephadex chromatography. The purified xylanase (specific activity reached 6596.79 UI/mg protein) was a monomer with a molecular weight of 37 kDa estimating from SDS electrophoresis. The results of LC/MS suggested that the purified protein is indeed an endo-1,4-β-
d
-xylanase. The purified xylanase showed the optimal temperature of 55 °C, and pH 6.5 with a stable xylanolytic activity within the temperature range of 45–50 °C, and within the pH range of 5.0–8.0. Most divalent metal cations including Zn
2+
, Fe
2+
, Mg
2+
, Cu
2+
, Mn
2+
showed some inhibition of xylanase activity while the monovalent metal cations such as K
+
and Ag
+
exhibited slight stimulating effects on the enzyme activity. The introduction of 10–30% different organic solvents (n-butanol, acetone, isopropanol) and several detergents (Triton X-100, Tween 20, and SDS) slightly reduced the enzyme activity. Moreover, the purified xylanase seemed to be tolerant to methanol and ethanol and was even stimulated by Tween 80. Overall, with these distinctive properties, the putative xylanase could be a successful candidate for numerous industrial uses.
Graphic Abstract</abstract><cop>New York</cop><pub>Springer US</pub><pmid>34580814</pmid><doi>10.1007/s12033-021-00395-8</doi><tpages>12</tpages><orcidid>https://orcid.org/0000-0002-8048-5794</orcidid></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 1073-6085 |
| ispartof | Molecular biotechnology, 2022-02, Vol.64 (2), p.187-198 |
| issn | 1073-6085 1559-0305 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_2577454089 |
| source | MEDLINE; Springer Nature - Complete Springer Journals |
| subjects | Amino acid sequence Animal feed Aspergillus niger Aspergillus niger - enzymology Beverages Biochemistry Biofuels Biological Techniques Biotechnology Butanol Cations Cell Biology Centrifugation Chemistry Chemistry and Materials Science Copper Detergents Detergents - chemistry Dextrans Electrophoresis Electrophoresis, Polyacrylamide Gel Enzymatic activity Enzyme activity Enzyme Stability Enzymes Ethanol Feeds Filtration - methods Fungal Proteins - chemistry Fungal Proteins - isolation & purification Fungal Proteins - metabolism Glycosidases Glycoside hydrolase High temperature Human Genetics Hydrogen-Ion Concentration Hydrolase Industrial applications Iron Kinetics Magnesium Metal ions Metals - chemistry Molecular weight Organic solvents Original Paper pH effects Protein Science Proteins Purification Silver Solvents Solvents - chemistry Structural analysis Sustainable development Temperature Xylan Xylanase Xylosidases - chemistry Xylosidases - isolation & purification Xylosidases - metabolism Zinc |
| title | Purification, Identification, and Characterization of a Glycoside Hydrolase Family 11-Xylanase with High Activity from Aspergillus niger VTCC 017 |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-02-20T20%3A12%3A53IST&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=Purification,%20Identification,%20and%20Characterization%20of%20a%20Glycoside%20Hydrolase%20Family%2011-Xylanase%20with%20High%20Activity%20from%20Aspergillus%20niger%20VTCC%20017&rft.jtitle=Molecular%20biotechnology&rft.au=Dao,%20Thi%20Mai%20Anh&rft.date=2022-02-01&rft.volume=64&rft.issue=2&rft.spage=187&rft.epage=198&rft.pages=187-198&rft.issn=1073-6085&rft.eissn=1559-0305&rft_id=info:doi/10.1007/s12033-021-00395-8&rft_dat=%3Cproquest_cross%3E2620837975%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=2620837975&rft_id=info:pmid/34580814&rfr_iscdi=true |