Purification and Characterization of [alpha]-D-Mannosidase from the Seeds of Kaya, Torreya nucifera
Alpha-D-mannosidase was purified from the extract of seeds of Kaya, Torreya nucifera. The purified enzyme had a molecular mass of ∼3.6 x 105 daltons. This enzyme had an optimum pH at 4.5, and was stable at pH between 5.5 and 6.5. This enzyme appeared to be a metal enzyme containing Zn2+. The enzyme...
Gespeichert in:
| Veröffentlicht in: | Bioscience, biotechnology, and biochemistry biotechnology, and biochemistry, 1996-04, Vol.60 (4), p.687 |
|---|---|
| Hauptverfasser: | , , , , , |
| Format: | Artikel |
| Sprache: | eng |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | |
|---|---|
| container_issue | 4 |
| container_start_page | 687 |
| container_title | Bioscience, biotechnology, and biochemistry |
| container_volume | 60 |
| creator | SHIROO, Tomomi OHTANI, Kimiko HUCHIGAMI, Kyoko NAKATANI, Masato YUASA, Isao MISAKI, Akira |
| description | Alpha-D-mannosidase was purified from the extract of seeds of Kaya, Torreya nucifera. The purified enzyme had a molecular mass of ∼3.6 x 105 daltons. This enzyme had an optimum pH at 4.5, and was stable at pH between 5.5 and 6.5. This enzyme appeared to be a metal enzyme containing Zn2+. The enzyme hydrolyzed p-nitrophenyl-α-D-mannoside, methyl-α-D-mannoside, α-1->3-man-nobiose, and α-1->6-mannobiose, with Km of 0.785 mM, 0.236 M, 2.505 mM, and 0.268 mM, fespectively. The hydrolysis of various α-linked mannobioses indicated that the enzyme hydrolyzes the α-mannobioses in the order of α-(1->2)> -(1->6)> -(1->3). |
| format | Article |
| fullrecord | <record><control><sourceid>proquest</sourceid><recordid>TN_cdi_proquest_journals_1449409144</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>3121699101</sourcerecordid><originalsourceid>FETCH-proquest_journals_14494091443</originalsourceid><addsrcrecordid>eNqNjssKwjAQRYMoWB__EHBroKFpa9c-EEQQ7E6kDO2ERjTRSbvQr7eiH-DqwrlncXoskJFKRZKptM-CMJOJWKhYDtnI-0sYdiCWASsPLRltSmiMsxxsxZc1EJQNknl9odP8BNd7DWexEnuw1nlTgUeuyd14UyM_Ilb-4-3gCXOeOyJ8ArdtaTQSTNhAw9Xj9LdjNtus8-VW3Mk9WvRNcXEt2e4qpFKZ6tKUiv6z3s3XRtQ</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>1449409144</pqid></control><display><type>article</type><title>Purification and Characterization of [alpha]-D-Mannosidase from the Seeds of Kaya, Torreya nucifera</title><source>Freely Accessible Japanese Titles (ERDB Project)</source><source>J-STAGE (Free - Japanese)</source><source>Free Full-Text Journals in Chemistry</source><source>EZB Electronic Journals Library</source><source>Oxford Journals</source><creator>SHIROO, Tomomi ; OHTANI, Kimiko ; HUCHIGAMI, Kyoko ; NAKATANI, Masato ; YUASA, Isao ; MISAKI, Akira</creator><creatorcontrib>SHIROO, Tomomi ; OHTANI, Kimiko ; HUCHIGAMI, Kyoko ; NAKATANI, Masato ; YUASA, Isao ; MISAKI, Akira</creatorcontrib><description>Alpha-D-mannosidase was purified from the extract of seeds of Kaya, Torreya nucifera. The purified enzyme had a molecular mass of ∼3.6 x 105 daltons. This enzyme had an optimum pH at 4.5, and was stable at pH between 5.5 and 6.5. This enzyme appeared to be a metal enzyme containing Zn2+. The enzyme hydrolyzed p-nitrophenyl-α-D-mannoside, methyl-α-D-mannoside, α-1->3-man-nobiose, and α-1->6-mannobiose, with Km of 0.785 mM, 0.236 M, 2.505 mM, and 0.268 mM, fespectively. The hydrolysis of various α-linked mannobioses indicated that the enzyme hydrolyzes the α-mannobioses in the order of α-(1->2)> -(1->6)> -(1->3).</description><identifier>ISSN: 0916-8451</identifier><identifier>EISSN: 1347-6947</identifier><language>eng</language><publisher>Tokyo: Oxford University Press</publisher><ispartof>Bioscience, biotechnology, and biochemistry, 1996-04, Vol.60 (4), p.687</ispartof><rights>Copyright Japan Science and Technology Agency 1996</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784</link.rule.ids></links><search><creatorcontrib>SHIROO, Tomomi</creatorcontrib><creatorcontrib>OHTANI, Kimiko</creatorcontrib><creatorcontrib>HUCHIGAMI, Kyoko</creatorcontrib><creatorcontrib>NAKATANI, Masato</creatorcontrib><creatorcontrib>YUASA, Isao</creatorcontrib><creatorcontrib>MISAKI, Akira</creatorcontrib><title>Purification and Characterization of [alpha]-D-Mannosidase from the Seeds of Kaya, Torreya nucifera</title><title>Bioscience, biotechnology, and biochemistry</title><description>Alpha-D-mannosidase was purified from the extract of seeds of Kaya, Torreya nucifera. The purified enzyme had a molecular mass of ∼3.6 x 105 daltons. This enzyme had an optimum pH at 4.5, and was stable at pH between 5.5 and 6.5. This enzyme appeared to be a metal enzyme containing Zn2+. The enzyme hydrolyzed p-nitrophenyl-α-D-mannoside, methyl-α-D-mannoside, α-1->3-man-nobiose, and α-1->6-mannobiose, with Km of 0.785 mM, 0.236 M, 2.505 mM, and 0.268 mM, fespectively. The hydrolysis of various α-linked mannobioses indicated that the enzyme hydrolyzes the α-mannobioses in the order of α-(1->2)> -(1->6)> -(1->3).</description><issn>0916-8451</issn><issn>1347-6947</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1996</creationdate><recordtype>article</recordtype><sourceid/><recordid>eNqNjssKwjAQRYMoWB__EHBroKFpa9c-EEQQ7E6kDO2ERjTRSbvQr7eiH-DqwrlncXoskJFKRZKptM-CMJOJWKhYDtnI-0sYdiCWASsPLRltSmiMsxxsxZc1EJQNknl9odP8BNd7DWexEnuw1nlTgUeuyd14UyM_Ilb-4-3gCXOeOyJ8ArdtaTQSTNhAw9Xj9LdjNtus8-VW3Mk9WvRNcXEt2e4qpFKZ6tKUiv6z3s3XRtQ</recordid><startdate>19960401</startdate><enddate>19960401</enddate><creator>SHIROO, Tomomi</creator><creator>OHTANI, Kimiko</creator><creator>HUCHIGAMI, Kyoko</creator><creator>NAKATANI, Masato</creator><creator>YUASA, Isao</creator><creator>MISAKI, Akira</creator><general>Oxford University Press</general><scope/></search><sort><creationdate>19960401</creationdate><title>Purification and Characterization of [alpha]-D-Mannosidase from the Seeds of Kaya, Torreya nucifera</title><author>SHIROO, Tomomi ; OHTANI, Kimiko ; HUCHIGAMI, Kyoko ; NAKATANI, Masato ; YUASA, Isao ; MISAKI, Akira</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-proquest_journals_14494091443</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1996</creationdate><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>SHIROO, Tomomi</creatorcontrib><creatorcontrib>OHTANI, Kimiko</creatorcontrib><creatorcontrib>HUCHIGAMI, Kyoko</creatorcontrib><creatorcontrib>NAKATANI, Masato</creatorcontrib><creatorcontrib>YUASA, Isao</creatorcontrib><creatorcontrib>MISAKI, Akira</creatorcontrib><jtitle>Bioscience, biotechnology, and biochemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>SHIROO, Tomomi</au><au>OHTANI, Kimiko</au><au>HUCHIGAMI, Kyoko</au><au>NAKATANI, Masato</au><au>YUASA, Isao</au><au>MISAKI, Akira</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Purification and Characterization of [alpha]-D-Mannosidase from the Seeds of Kaya, Torreya nucifera</atitle><jtitle>Bioscience, biotechnology, and biochemistry</jtitle><date>1996-04-01</date><risdate>1996</risdate><volume>60</volume><issue>4</issue><spage>687</spage><pages>687-</pages><issn>0916-8451</issn><eissn>1347-6947</eissn><abstract>Alpha-D-mannosidase was purified from the extract of seeds of Kaya, Torreya nucifera. The purified enzyme had a molecular mass of ∼3.6 x 105 daltons. This enzyme had an optimum pH at 4.5, and was stable at pH between 5.5 and 6.5. This enzyme appeared to be a metal enzyme containing Zn2+. The enzyme hydrolyzed p-nitrophenyl-α-D-mannoside, methyl-α-D-mannoside, α-1->3-man-nobiose, and α-1->6-mannobiose, with Km of 0.785 mM, 0.236 M, 2.505 mM, and 0.268 mM, fespectively. The hydrolysis of various α-linked mannobioses indicated that the enzyme hydrolyzes the α-mannobioses in the order of α-(1->2)> -(1->6)> -(1->3).</abstract><cop>Tokyo</cop><pub>Oxford University Press</pub></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0916-8451 |
| ispartof | Bioscience, biotechnology, and biochemistry, 1996-04, Vol.60 (4), p.687 |
| issn | 0916-8451 1347-6947 |
| language | eng |
| recordid | cdi_proquest_journals_1449409144 |
| source | Freely Accessible Japanese Titles (ERDB Project); J-STAGE (Free - Japanese); Free Full-Text Journals in Chemistry; EZB Electronic Journals Library; Oxford Journals |
| title | Purification and Characterization of [alpha]-D-Mannosidase from the Seeds of Kaya, Torreya nucifera |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2024-12-28T12%3A06%3A14IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Purification%20and%20Characterization%20of%20%5Balpha%5D-D-Mannosidase%20from%20the%20Seeds%20of%20Kaya,%20Torreya%20nucifera&rft.jtitle=Bioscience,%20biotechnology,%20and%20biochemistry&rft.au=SHIROO,%20Tomomi&rft.date=1996-04-01&rft.volume=60&rft.issue=4&rft.spage=687&rft.pages=687-&rft.issn=0916-8451&rft.eissn=1347-6947&rft_id=info:doi/&rft_dat=%3Cproquest%3E3121699101%3C/proquest%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=1449409144&rft_id=info:pmid/&rfr_iscdi=true |