Purification and Biochemical Characterization of a Highly Thermostable Xylanase from Actinomadura sp. Strain Cpt20 Isolated from Poultry Compost
An extracellular thermostable xylanase from a newly isolated thermophilic Actinomadura sp. strain Cpt20 was purified and characterized. Based on matrix-assisted laser desorption–ionization time-of-flight mass spectrometry analysis, the purified enzyme is a monomer with a molecular mass of 20,110.13 ...
Gespeichert in:
| Veröffentlicht in: | Applied biochemistry and biotechnology 2012-02, Vol.166 (3), p.663-679 |
|---|---|
| Hauptverfasser: | , , , , , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 679 |
|---|---|
| container_issue | 3 |
| container_start_page | 663 |
| container_title | Applied biochemistry and biotechnology |
| container_volume | 166 |
| creator | Taibi, Zina Saoudi, Boudjemaa Boudelaa, Mokhtar Trigui, Héla Belghith, Hafedh Gargouri, Ali Ladjama, Ali |
| description | An extracellular thermostable xylanase from a newly isolated thermophilic
Actinomadura
sp. strain Cpt20 was purified and characterized. Based on matrix-assisted laser desorption–ionization time-of-flight mass spectrometry analysis, the purified enzyme is a monomer with a molecular mass of 20,110.13 Da. The 19 residue N-terminal sequence of the enzyme showed 84% homology with those of actinomycete endoxylanases. The optimum pH and temperature values for xylanase activity were pH 10 and 80 °C, respectively. This xylanase was stable within a pH range of 5–10 and up to a temperature of 90 °C. It showed high thermostability at 60 °C for 5 days and half-life times at 90 °C and 100 °C were 2 and 1 h, respectively. The xylanase was specific for xylans, showing higher specific activity on soluble oat-spelt xylan followed by beechwood xylan. This enzyme obeyed the Michaelis–Menten kinetics, with the
K
m
and
k
cat
values being 1.55 mg soluble oat-spelt xylan/ml and 388 min
−1
, respectively. While the xylanase from
Actinomadura
sp. Cpt20 was activated by Mn
2+
, Ca
2+
, and Cu
2+
, it was, strongly inhibited by Hg
2+
, Zn
2+
, and Ba
2+
. These properties make this enzyme a potential candidate for future use in biotechnological applications particularly in the pulp and paper industry. |
| doi_str_mv | 10.1007/s12010-011-9457-y |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_954651508</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>2577474621</sourcerecordid><originalsourceid>FETCH-LOGICAL-c498t-a026658a19b0f509c41825ea04897241b3689c02bbde6fbf0462a17849fc25403</originalsourceid><addsrcrecordid>eNqFkVFr1TAUx4Mo7jr9AL5IEMSnznPSpm0eZ5luMHDgBN9Kmia7GW1Tk_Shfgo_8nLp1YEgPh3I-Z3_yeFHyGuEMwSoPgRkgJABYiYKXmXrE7JDzkUGTOBTsgNW5RljtTghL0K4B0BW8-o5OWEMS8QCduTXzeKtsUpG6yYqp55-tE7t9ZieBtrspZcqam9_boAzVNJLe7cfVnq71350Icpu0PT7OshJBk2NdyM9V9FObpT94iUN8xn9Gr20E23myIBeBTfIqPuNvXHLEP1KGzfOKe0leWbkEPSrYz0l3z5d3DaX2fWXz1fN-XWmClHHTAIrS15LFB0YDkIVWDOuJRS1qFiBXV7WQgHrul6XpjNQlExiVRfCKMYLyE_J-y139u7HokNsRxuUHtIZ2i2hFbwoOXKo_0-iEDxnZZ7It3-R927xUzrjAJVpe3WIww1S3oXgtWlnb0fp1xahPWhtN61t0toetLZrmnlzDF66Ufd_Jn57TMC7IyBDEme8nJQNjxzntQDkiWMbF1JrutP-8Yf_3v4ANQm6xA</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>919678478</pqid></control><display><type>article</type><title>Purification and Biochemical Characterization of a Highly Thermostable Xylanase from Actinomadura sp. Strain Cpt20 Isolated from Poultry Compost</title><source>MEDLINE</source><source>SpringerLink Journals - AutoHoldings</source><creator>Taibi, Zina ; Saoudi, Boudjemaa ; Boudelaa, Mokhtar ; Trigui, Héla ; Belghith, Hafedh ; Gargouri, Ali ; Ladjama, Ali</creator><creatorcontrib>Taibi, Zina ; Saoudi, Boudjemaa ; Boudelaa, Mokhtar ; Trigui, Héla ; Belghith, Hafedh ; Gargouri, Ali ; Ladjama, Ali</creatorcontrib><description>An extracellular thermostable xylanase from a newly isolated thermophilic
Actinomadura
sp. strain Cpt20 was purified and characterized. Based on matrix-assisted laser desorption–ionization time-of-flight mass spectrometry analysis, the purified enzyme is a monomer with a molecular mass of 20,110.13 Da. The 19 residue N-terminal sequence of the enzyme showed 84% homology with those of actinomycete endoxylanases. The optimum pH and temperature values for xylanase activity were pH 10 and 80 °C, respectively. This xylanase was stable within a pH range of 5–10 and up to a temperature of 90 °C. It showed high thermostability at 60 °C for 5 days and half-life times at 90 °C and 100 °C were 2 and 1 h, respectively. The xylanase was specific for xylans, showing higher specific activity on soluble oat-spelt xylan followed by beechwood xylan. This enzyme obeyed the Michaelis–Menten kinetics, with the
K
m
and
k
cat
values being 1.55 mg soluble oat-spelt xylan/ml and 388 min
−1
, respectively. While the xylanase from
Actinomadura
sp. Cpt20 was activated by Mn
2+
, Ca
2+
, and Cu
2+
, it was, strongly inhibited by Hg
2+
, Zn
2+
, and Ba
2+
. These properties make this enzyme a potential candidate for future use in biotechnological applications particularly in the pulp and paper industry.</description><identifier>ISSN: 0273-2289</identifier><identifier>EISSN: 1559-0291</identifier><identifier>DOI: 10.1007/s12010-011-9457-y</identifier><identifier>PMID: 22161140</identifier><identifier>CODEN: ABIBDL</identifier><language>eng</language><publisher>New York: Humana Press Inc</publisher><subject>Actinomadura ; Actinomycetales - chemistry ; Actinomycetales - enzymology ; Amino Acid Sequence ; Animals ; Bacterial Proteins - genetics ; Bacterial Proteins - isolation & purification ; Bacterial Proteins - metabolism ; Biochemistry ; Biological and medical sciences ; Biotechnology ; Chemistry ; Chemistry and Materials Science ; Chickens ; Endo-1,4-beta Xylanases - genetics ; Endo-1,4-beta Xylanases - isolation & purification ; Endo-1,4-beta Xylanases - metabolism ; Enzyme Stability ; Enzymes ; Fundamental and applied biological sciences. Psychology ; Half-Life ; Hot Temperature ; Hydrogen-Ion Concentration ; Ionization ; Kinetics ; Mass spectrometry ; Molecular Sequence Data ; Molecular Weight ; Phylogeny ; Poultry ; Pulp & paper industry ; RNA, Ribosomal, 16S - biosynthesis ; Soil ; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization ; Substrate Specificity ; Xylans - metabolism</subject><ispartof>Applied biochemistry and biotechnology, 2012-02, Vol.166 (3), p.663-679</ispartof><rights>Springer Science+Business Media, LLC 2011</rights><rights>2015 INIST-CNRS</rights><rights>Springer Science+Business Media, LLC 2012</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c498t-a026658a19b0f509c41825ea04897241b3689c02bbde6fbf0462a17849fc25403</citedby><cites>FETCH-LOGICAL-c498t-a026658a19b0f509c41825ea04897241b3689c02bbde6fbf0462a17849fc25403</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1007/s12010-011-9457-y$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1007/s12010-011-9457-y$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>314,780,784,27924,27925,41488,42557,51319</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=25589015$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/22161140$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Taibi, Zina</creatorcontrib><creatorcontrib>Saoudi, Boudjemaa</creatorcontrib><creatorcontrib>Boudelaa, Mokhtar</creatorcontrib><creatorcontrib>Trigui, Héla</creatorcontrib><creatorcontrib>Belghith, Hafedh</creatorcontrib><creatorcontrib>Gargouri, Ali</creatorcontrib><creatorcontrib>Ladjama, Ali</creatorcontrib><title>Purification and Biochemical Characterization of a Highly Thermostable Xylanase from Actinomadura sp. Strain Cpt20 Isolated from Poultry Compost</title><title>Applied biochemistry and biotechnology</title><addtitle>Appl Biochem Biotechnol</addtitle><addtitle>Appl Biochem Biotechnol</addtitle><description>An extracellular thermostable xylanase from a newly isolated thermophilic
Actinomadura
sp. strain Cpt20 was purified and characterized. Based on matrix-assisted laser desorption–ionization time-of-flight mass spectrometry analysis, the purified enzyme is a monomer with a molecular mass of 20,110.13 Da. The 19 residue N-terminal sequence of the enzyme showed 84% homology with those of actinomycete endoxylanases. The optimum pH and temperature values for xylanase activity were pH 10 and 80 °C, respectively. This xylanase was stable within a pH range of 5–10 and up to a temperature of 90 °C. It showed high thermostability at 60 °C for 5 days and half-life times at 90 °C and 100 °C were 2 and 1 h, respectively. The xylanase was specific for xylans, showing higher specific activity on soluble oat-spelt xylan followed by beechwood xylan. This enzyme obeyed the Michaelis–Menten kinetics, with the
K
m
and
k
cat
values being 1.55 mg soluble oat-spelt xylan/ml and 388 min
−1
, respectively. While the xylanase from
Actinomadura
sp. Cpt20 was activated by Mn
2+
, Ca
2+
, and Cu
2+
, it was, strongly inhibited by Hg
2+
, Zn
2+
, and Ba
2+
. These properties make this enzyme a potential candidate for future use in biotechnological applications particularly in the pulp and paper industry.</description><subject>Actinomadura</subject><subject>Actinomycetales - chemistry</subject><subject>Actinomycetales - enzymology</subject><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Bacterial Proteins - genetics</subject><subject>Bacterial Proteins - isolation & purification</subject><subject>Bacterial Proteins - metabolism</subject><subject>Biochemistry</subject><subject>Biological and medical sciences</subject><subject>Biotechnology</subject><subject>Chemistry</subject><subject>Chemistry and Materials Science</subject><subject>Chickens</subject><subject>Endo-1,4-beta Xylanases - genetics</subject><subject>Endo-1,4-beta Xylanases - isolation & purification</subject><subject>Endo-1,4-beta Xylanases - metabolism</subject><subject>Enzyme Stability</subject><subject>Enzymes</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Half-Life</subject><subject>Hot Temperature</subject><subject>Hydrogen-Ion Concentration</subject><subject>Ionization</subject><subject>Kinetics</subject><subject>Mass spectrometry</subject><subject>Molecular Sequence Data</subject><subject>Molecular Weight</subject><subject>Phylogeny</subject><subject>Poultry</subject><subject>Pulp & paper industry</subject><subject>RNA, Ribosomal, 16S - biosynthesis</subject><subject>Soil</subject><subject>Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization</subject><subject>Substrate Specificity</subject><subject>Xylans - metabolism</subject><issn>0273-2289</issn><issn>1559-0291</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2012</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>eNqFkVFr1TAUx4Mo7jr9AL5IEMSnznPSpm0eZ5luMHDgBN9Kmia7GW1Tk_Shfgo_8nLp1YEgPh3I-Z3_yeFHyGuEMwSoPgRkgJABYiYKXmXrE7JDzkUGTOBTsgNW5RljtTghL0K4B0BW8-o5OWEMS8QCduTXzeKtsUpG6yYqp55-tE7t9ZieBtrspZcqam9_boAzVNJLe7cfVnq71350Icpu0PT7OshJBk2NdyM9V9FObpT94iUN8xn9Gr20E23myIBeBTfIqPuNvXHLEP1KGzfOKe0leWbkEPSrYz0l3z5d3DaX2fWXz1fN-XWmClHHTAIrS15LFB0YDkIVWDOuJRS1qFiBXV7WQgHrul6XpjNQlExiVRfCKMYLyE_J-y139u7HokNsRxuUHtIZ2i2hFbwoOXKo_0-iEDxnZZ7It3-R927xUzrjAJVpe3WIww1S3oXgtWlnb0fp1xahPWhtN61t0toetLZrmnlzDF66Ufd_Jn57TMC7IyBDEme8nJQNjxzntQDkiWMbF1JrutP-8Yf_3v4ANQm6xA</recordid><startdate>20120201</startdate><enddate>20120201</enddate><creator>Taibi, Zina</creator><creator>Saoudi, Boudjemaa</creator><creator>Boudelaa, Mokhtar</creator><creator>Trigui, Héla</creator><creator>Belghith, Hafedh</creator><creator>Gargouri, Ali</creator><creator>Ladjama, Ali</creator><general>Humana Press Inc</general><general>Springer</general><general>Springer Nature B.V</general><scope>IQODW</scope><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>7ST</scope><scope>7T7</scope><scope>7TM</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>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</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>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M2P</scope><scope>M7P</scope><scope>P64</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>Q9U</scope><scope>RC3</scope><scope>SOI</scope><scope>7X8</scope><scope>7QO</scope></search><sort><creationdate>20120201</creationdate><title>Purification and Biochemical Characterization of a Highly Thermostable Xylanase from Actinomadura sp. Strain Cpt20 Isolated from Poultry Compost</title><author>Taibi, Zina ; Saoudi, Boudjemaa ; Boudelaa, Mokhtar ; Trigui, Héla ; Belghith, Hafedh ; Gargouri, Ali ; Ladjama, Ali</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c498t-a026658a19b0f509c41825ea04897241b3689c02bbde6fbf0462a17849fc25403</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2012</creationdate><topic>Actinomadura</topic><topic>Actinomycetales - chemistry</topic><topic>Actinomycetales - enzymology</topic><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Bacterial Proteins - genetics</topic><topic>Bacterial Proteins - isolation & purification</topic><topic>Bacterial Proteins - metabolism</topic><topic>Biochemistry</topic><topic>Biological and medical sciences</topic><topic>Biotechnology</topic><topic>Chemistry</topic><topic>Chemistry and Materials Science</topic><topic>Chickens</topic><topic>Endo-1,4-beta Xylanases - genetics</topic><topic>Endo-1,4-beta Xylanases - isolation & purification</topic><topic>Endo-1,4-beta Xylanases - metabolism</topic><topic>Enzyme Stability</topic><topic>Enzymes</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Half-Life</topic><topic>Hot Temperature</topic><topic>Hydrogen-Ion Concentration</topic><topic>Ionization</topic><topic>Kinetics</topic><topic>Mass spectrometry</topic><topic>Molecular Sequence Data</topic><topic>Molecular Weight</topic><topic>Phylogeny</topic><topic>Poultry</topic><topic>Pulp & paper industry</topic><topic>RNA, Ribosomal, 16S - biosynthesis</topic><topic>Soil</topic><topic>Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization</topic><topic>Substrate Specificity</topic><topic>Xylans - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Taibi, Zina</creatorcontrib><creatorcontrib>Saoudi, Boudjemaa</creatorcontrib><creatorcontrib>Boudelaa, Mokhtar</creatorcontrib><creatorcontrib>Trigui, Héla</creatorcontrib><creatorcontrib>Belghith, Hafedh</creatorcontrib><creatorcontrib>Gargouri, Ali</creatorcontrib><creatorcontrib>Ladjama, Ali</creatorcontrib><collection>Pascal-Francis</collection><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>Environment Abstracts</collection><collection>Industrial and Applied Microbiology Abstracts (Microbiology A)</collection><collection>Nucleic Acids 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 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>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>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>SciTech Premium Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>ProQuest Biological Science Collection</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Science Database</collection><collection>Biological Science Database</collection><collection>Biotechnology and BioEngineering Abstracts</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>Genetics Abstracts</collection><collection>Environment Abstracts</collection><collection>MEDLINE - Academic</collection><collection>Biotechnology Research Abstracts</collection><jtitle>Applied biochemistry and biotechnology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Taibi, Zina</au><au>Saoudi, Boudjemaa</au><au>Boudelaa, Mokhtar</au><au>Trigui, Héla</au><au>Belghith, Hafedh</au><au>Gargouri, Ali</au><au>Ladjama, Ali</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Purification and Biochemical Characterization of a Highly Thermostable Xylanase from Actinomadura sp. Strain Cpt20 Isolated from Poultry Compost</atitle><jtitle>Applied biochemistry and biotechnology</jtitle><stitle>Appl Biochem Biotechnol</stitle><addtitle>Appl Biochem Biotechnol</addtitle><date>2012-02-01</date><risdate>2012</risdate><volume>166</volume><issue>3</issue><spage>663</spage><epage>679</epage><pages>663-679</pages><issn>0273-2289</issn><eissn>1559-0291</eissn><coden>ABIBDL</coden><abstract>An extracellular thermostable xylanase from a newly isolated thermophilic
Actinomadura
sp. strain Cpt20 was purified and characterized. Based on matrix-assisted laser desorption–ionization time-of-flight mass spectrometry analysis, the purified enzyme is a monomer with a molecular mass of 20,110.13 Da. The 19 residue N-terminal sequence of the enzyme showed 84% homology with those of actinomycete endoxylanases. The optimum pH and temperature values for xylanase activity were pH 10 and 80 °C, respectively. This xylanase was stable within a pH range of 5–10 and up to a temperature of 90 °C. It showed high thermostability at 60 °C for 5 days and half-life times at 90 °C and 100 °C were 2 and 1 h, respectively. The xylanase was specific for xylans, showing higher specific activity on soluble oat-spelt xylan followed by beechwood xylan. This enzyme obeyed the Michaelis–Menten kinetics, with the
K
m
and
k
cat
values being 1.55 mg soluble oat-spelt xylan/ml and 388 min
−1
, respectively. While the xylanase from
Actinomadura
sp. Cpt20 was activated by Mn
2+
, Ca
2+
, and Cu
2+
, it was, strongly inhibited by Hg
2+
, Zn
2+
, and Ba
2+
. These properties make this enzyme a potential candidate for future use in biotechnological applications particularly in the pulp and paper industry.</abstract><cop>New York</cop><pub>Humana Press Inc</pub><pmid>22161140</pmid><doi>10.1007/s12010-011-9457-y</doi><tpages>17</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0273-2289 |
| ispartof | Applied biochemistry and biotechnology, 2012-02, Vol.166 (3), p.663-679 |
| issn | 0273-2289 1559-0291 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_954651508 |
| source | MEDLINE; SpringerLink Journals - AutoHoldings |
| subjects | Actinomadura Actinomycetales - chemistry Actinomycetales - enzymology Amino Acid Sequence Animals Bacterial Proteins - genetics Bacterial Proteins - isolation & purification Bacterial Proteins - metabolism Biochemistry Biological and medical sciences Biotechnology Chemistry Chemistry and Materials Science Chickens Endo-1,4-beta Xylanases - genetics Endo-1,4-beta Xylanases - isolation & purification Endo-1,4-beta Xylanases - metabolism Enzyme Stability Enzymes Fundamental and applied biological sciences. Psychology Half-Life Hot Temperature Hydrogen-Ion Concentration Ionization Kinetics Mass spectrometry Molecular Sequence Data Molecular Weight Phylogeny Poultry Pulp & paper industry RNA, Ribosomal, 16S - biosynthesis Soil Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization Substrate Specificity Xylans - metabolism |
| title | Purification and Biochemical Characterization of a Highly Thermostable Xylanase from Actinomadura sp. Strain Cpt20 Isolated from Poultry Compost |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2024-12-23T01%3A38%3A26IST&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%20and%20Biochemical%20Characterization%20of%20a%20Highly%20Thermostable%20Xylanase%20from%20Actinomadura%20sp.%20Strain%20Cpt20%20Isolated%20from%20Poultry%20Compost&rft.jtitle=Applied%20biochemistry%20and%20biotechnology&rft.au=Taibi,%20Zina&rft.date=2012-02-01&rft.volume=166&rft.issue=3&rft.spage=663&rft.epage=679&rft.pages=663-679&rft.issn=0273-2289&rft.eissn=1559-0291&rft.coden=ABIBDL&rft_id=info:doi/10.1007/s12010-011-9457-y&rft_dat=%3Cproquest_cross%3E2577474621%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=919678478&rft_id=info:pmid/22161140&rfr_iscdi=true |