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Purification and enzymatic properties of a new thermostable endoglucanase from Aspergillus oryzae HML366
Aspergillus oryzae HML366 is a newly screened cellulase-producing strain. The endoglucanase HML ED1 from A. oryzae HML366 was quickly purified by a two-step method that combines ammonium sulfate precipitation and strong anion exchange column. SDS-PAGE electrophoresis indicated that the molecular wei...
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| Published in: | International microbiology 2023-08, Vol.26 (3), p.579-589 |
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| container_title | International microbiology |
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| creator | Qin, Yongling Qin, Baoshan Zhang, Jian Fu, Yue Li, Qiqian Luo, Fengfeng Luo, Yanmei He, Haiyan |
| description | Aspergillus oryzae
HML366 is a newly screened cellulase-producing strain. The endoglucanase HML ED1 from
A. oryzae
HML366 was quickly purified by a two-step method that combines ammonium sulfate precipitation and strong anion exchange column. SDS-PAGE electrophoresis indicated that the molecular weight of the enzyme was 68 kDa. The optimum temperature of the purified endoglucanase was 60 ℃ and the enzyme activity was stable below 70 ℃. The optimum pH was 6.5, and the enzyme activity was stable at pH between 4.5 and 9.0. The analysis indicated that additional Na
+
, K
+
, Ca
2+
, and Zn
2+
reduced the catalytic ability of enzyme to the substrate, but Mn
2+
enhanced its catalytic ability to the substrate.The
Km
and
Vmax
of the purified endoglucanase were 8.75 mg/mL and 60.24 μmol/min·mg, respectively. In this study, we report for the first time that
A. oryzae
HML366 can produce a heat-resistant and wide pH tolerant endoglucanase HML ED1, which has potential industrial application value in bioethanol, paper, food, textile, detergent, and pharmaceutical industries. |
| doi_str_mv | 10.1007/s10123-023-00322-8 |
| format | article |
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HML366 is a newly screened cellulase-producing strain. The endoglucanase HML ED1 from
A. oryzae
HML366 was quickly purified by a two-step method that combines ammonium sulfate precipitation and strong anion exchange column. SDS-PAGE electrophoresis indicated that the molecular weight of the enzyme was 68 kDa. The optimum temperature of the purified endoglucanase was 60 ℃ and the enzyme activity was stable below 70 ℃. The optimum pH was 6.5, and the enzyme activity was stable at pH between 4.5 and 9.0. The analysis indicated that additional Na
+
, K
+
, Ca
2+
, and Zn
2+
reduced the catalytic ability of enzyme to the substrate, but Mn
2+
enhanced its catalytic ability to the substrate.The
Km
and
Vmax
of the purified endoglucanase were 8.75 mg/mL and 60.24 μmol/min·mg, respectively. In this study, we report for the first time that
A. oryzae
HML366 can produce a heat-resistant and wide pH tolerant endoglucanase HML ED1, which has potential industrial application value in bioethanol, paper, food, textile, detergent, and pharmaceutical industries.</description><identifier>ISSN: 1618-1905</identifier><identifier>ISSN: 1139-6709</identifier><identifier>EISSN: 1618-1905</identifier><identifier>DOI: 10.1007/s10123-023-00322-8</identifier><identifier>PMID: 36705789</identifier><language>eng</language><publisher>Cham: Springer International Publishing</publisher><subject>Ammonium ; Ammonium sulfate ; Anion exchange ; Anion exchanging ; Applied Microbiology ; Aspergillus oryzae ; Aspergillus oryzae - metabolism ; Biofuels ; Biomedical and Life Sciences ; Calcium ions ; Cellulase ; Cellulase - metabolism ; Electrophoresis ; Endoglucanase ; Enzymatic activity ; Enzyme activity ; Enzyme Stability ; Enzymes ; Eukaryotic Microbiology ; Hot Temperature ; Hydrogen-Ion Concentration ; Industrial applications ; Life Sciences ; Medical Microbiology ; Microbial Ecology ; Microbiology ; Molecular weight ; pH effects ; Pharmaceutical industry ; Substrate Specificity ; Substrates ; Temperature ; Zinc</subject><ispartof>International microbiology, 2023-08, Vol.26 (3), p.579-589</ispartof><rights>The Author(s), under exclusive licence to Springer Nature Switzerland AG 2023. Springer Nature or its licensor (e.g. a society or other partner) holds exclusive rights to this article under a publishing agreement with the author(s) or other rightsholder(s); author self-archiving of the accepted manuscript version of this article is solely governed by the terms of such publishing agreement and applicable law.</rights><rights>2023. The Author(s), under exclusive licence to Springer Nature Switzerland AG.</rights><rights>Copyright Spanish Society for Microbiology Aug 2023</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c375t-32e19781d89bf933efdcd7d242c818d2d7692ce5d059ef5dc73678efc8bb3c0d3</citedby><cites>FETCH-LOGICAL-c375t-32e19781d89bf933efdcd7d242c818d2d7692ce5d059ef5dc73678efc8bb3c0d3</cites><orcidid>0000-0001-8921-5742</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,27901,27902</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/36705789$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Qin, Yongling</creatorcontrib><creatorcontrib>Qin, Baoshan</creatorcontrib><creatorcontrib>Zhang, Jian</creatorcontrib><creatorcontrib>Fu, Yue</creatorcontrib><creatorcontrib>Li, Qiqian</creatorcontrib><creatorcontrib>Luo, Fengfeng</creatorcontrib><creatorcontrib>Luo, Yanmei</creatorcontrib><creatorcontrib>He, Haiyan</creatorcontrib><title>Purification and enzymatic properties of a new thermostable endoglucanase from Aspergillus oryzae HML366</title><title>International microbiology</title><addtitle>Int Microbiol</addtitle><addtitle>Int Microbiol</addtitle><description>Aspergillus oryzae
HML366 is a newly screened cellulase-producing strain. The endoglucanase HML ED1 from
A. oryzae
HML366 was quickly purified by a two-step method that combines ammonium sulfate precipitation and strong anion exchange column. SDS-PAGE electrophoresis indicated that the molecular weight of the enzyme was 68 kDa. The optimum temperature of the purified endoglucanase was 60 ℃ and the enzyme activity was stable below 70 ℃. The optimum pH was 6.5, and the enzyme activity was stable at pH between 4.5 and 9.0. The analysis indicated that additional Na
+
, K
+
, Ca
2+
, and Zn
2+
reduced the catalytic ability of enzyme to the substrate, but Mn
2+
enhanced its catalytic ability to the substrate.The
Km
and
Vmax
of the purified endoglucanase were 8.75 mg/mL and 60.24 μmol/min·mg, respectively. In this study, we report for the first time that
A. oryzae
HML366 can produce a heat-resistant and wide pH tolerant endoglucanase HML ED1, which has potential industrial application value in bioethanol, paper, food, textile, detergent, and pharmaceutical industries.</description><subject>Ammonium</subject><subject>Ammonium sulfate</subject><subject>Anion exchange</subject><subject>Anion exchanging</subject><subject>Applied Microbiology</subject><subject>Aspergillus oryzae</subject><subject>Aspergillus oryzae - metabolism</subject><subject>Biofuels</subject><subject>Biomedical and Life Sciences</subject><subject>Calcium ions</subject><subject>Cellulase</subject><subject>Cellulase - metabolism</subject><subject>Electrophoresis</subject><subject>Endoglucanase</subject><subject>Enzymatic activity</subject><subject>Enzyme activity</subject><subject>Enzyme Stability</subject><subject>Enzymes</subject><subject>Eukaryotic Microbiology</subject><subject>Hot Temperature</subject><subject>Hydrogen-Ion Concentration</subject><subject>Industrial applications</subject><subject>Life Sciences</subject><subject>Medical Microbiology</subject><subject>Microbial Ecology</subject><subject>Microbiology</subject><subject>Molecular weight</subject><subject>pH effects</subject><subject>Pharmaceutical industry</subject><subject>Substrate Specificity</subject><subject>Substrates</subject><subject>Temperature</subject><subject>Zinc</subject><issn>1618-1905</issn><issn>1139-6709</issn><issn>1618-1905</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2023</creationdate><recordtype>article</recordtype><recordid>eNp9kUtPxCAUhYnR-P4DLgyJGzdVHtMCS2PUMRmjC10TCpexpi0jtDHjr5fJ-IoLFzdA-M65Fw5CR5ScUULEeaKEMl6QVRHOWCE30C6tqCyoIuXmr_0O2kvphRAqKkm20Q6vBCmFVLvo-WGMjW-sGZrQY9M7DP37sstHixcxLCAODSQcPDa4hzc8PEPsQhpM3UJGXZi3ozW9SYB9DB2-SFkyb9p2zKK4fDeAp3czXlUHaMubNsHh57qPnq6vHi-nxez-5vbyYlZYLsqh4AyoEpI6qWqvOAfvrBOOTZiVVDrmRKWYhdKRUoEvnRX5LRK8lXXNLXF8H52uffP0ryOkQXdNstC2pocwJs2EIJRKRVVGT_6gL2GMfZ5OMzkRildSTDLF1pSNIaUIXi9i05m41JToVQ56nYMmq1rloGUWHX9aj3UH7lvy9fEZ4Gsg5at-DvGn9z-2H_YBk-8</recordid><startdate>20230801</startdate><enddate>20230801</enddate><creator>Qin, Yongling</creator><creator>Qin, Baoshan</creator><creator>Zhang, Jian</creator><creator>Fu, Yue</creator><creator>Li, Qiqian</creator><creator>Luo, Fengfeng</creator><creator>Luo, Yanmei</creator><creator>He, Haiyan</creator><general>Springer International Publishing</general><general>Spanish Society for Microbiology</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>7QL</scope><scope>7U9</scope><scope>C1K</scope><scope>H94</scope><scope>M7N</scope><scope>7X8</scope><orcidid>https://orcid.org/0000-0001-8921-5742</orcidid></search><sort><creationdate>20230801</creationdate><title>Purification and enzymatic properties of a new thermostable endoglucanase from Aspergillus oryzae HML366</title><author>Qin, Yongling ; Qin, Baoshan ; Zhang, Jian ; Fu, Yue ; Li, Qiqian ; Luo, Fengfeng ; Luo, Yanmei ; He, Haiyan</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c375t-32e19781d89bf933efdcd7d242c818d2d7692ce5d059ef5dc73678efc8bb3c0d3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2023</creationdate><topic>Ammonium</topic><topic>Ammonium sulfate</topic><topic>Anion exchange</topic><topic>Anion exchanging</topic><topic>Applied Microbiology</topic><topic>Aspergillus oryzae</topic><topic>Aspergillus oryzae - metabolism</topic><topic>Biofuels</topic><topic>Biomedical and Life Sciences</topic><topic>Calcium ions</topic><topic>Cellulase</topic><topic>Cellulase - metabolism</topic><topic>Electrophoresis</topic><topic>Endoglucanase</topic><topic>Enzymatic activity</topic><topic>Enzyme activity</topic><topic>Enzyme Stability</topic><topic>Enzymes</topic><topic>Eukaryotic Microbiology</topic><topic>Hot Temperature</topic><topic>Hydrogen-Ion Concentration</topic><topic>Industrial applications</topic><topic>Life Sciences</topic><topic>Medical Microbiology</topic><topic>Microbial Ecology</topic><topic>Microbiology</topic><topic>Molecular weight</topic><topic>pH effects</topic><topic>Pharmaceutical industry</topic><topic>Substrate Specificity</topic><topic>Substrates</topic><topic>Temperature</topic><topic>Zinc</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Qin, Yongling</creatorcontrib><creatorcontrib>Qin, Baoshan</creatorcontrib><creatorcontrib>Zhang, Jian</creatorcontrib><creatorcontrib>Fu, Yue</creatorcontrib><creatorcontrib>Li, Qiqian</creatorcontrib><creatorcontrib>Luo, Fengfeng</creatorcontrib><creatorcontrib>Luo, Yanmei</creatorcontrib><creatorcontrib>He, Haiyan</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Virology and AIDS Abstracts</collection><collection>Environmental Sciences and Pollution Management</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>MEDLINE - Academic</collection><jtitle>International microbiology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Qin, Yongling</au><au>Qin, Baoshan</au><au>Zhang, Jian</au><au>Fu, Yue</au><au>Li, Qiqian</au><au>Luo, Fengfeng</au><au>Luo, Yanmei</au><au>He, Haiyan</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Purification and enzymatic properties of a new thermostable endoglucanase from Aspergillus oryzae HML366</atitle><jtitle>International microbiology</jtitle><stitle>Int Microbiol</stitle><addtitle>Int Microbiol</addtitle><date>2023-08-01</date><risdate>2023</risdate><volume>26</volume><issue>3</issue><spage>579</spage><epage>589</epage><pages>579-589</pages><issn>1618-1905</issn><issn>1139-6709</issn><eissn>1618-1905</eissn><abstract>Aspergillus oryzae
HML366 is a newly screened cellulase-producing strain. The endoglucanase HML ED1 from
A. oryzae
HML366 was quickly purified by a two-step method that combines ammonium sulfate precipitation and strong anion exchange column. SDS-PAGE electrophoresis indicated that the molecular weight of the enzyme was 68 kDa. The optimum temperature of the purified endoglucanase was 60 ℃ and the enzyme activity was stable below 70 ℃. The optimum pH was 6.5, and the enzyme activity was stable at pH between 4.5 and 9.0. The analysis indicated that additional Na
+
, K
+
, Ca
2+
, and Zn
2+
reduced the catalytic ability of enzyme to the substrate, but Mn
2+
enhanced its catalytic ability to the substrate.The
Km
and
Vmax
of the purified endoglucanase were 8.75 mg/mL and 60.24 μmol/min·mg, respectively. In this study, we report for the first time that
A. oryzae
HML366 can produce a heat-resistant and wide pH tolerant endoglucanase HML ED1, which has potential industrial application value in bioethanol, paper, food, textile, detergent, and pharmaceutical industries.</abstract><cop>Cham</cop><pub>Springer International Publishing</pub><pmid>36705789</pmid><doi>10.1007/s10123-023-00322-8</doi><tpages>11</tpages><orcidid>https://orcid.org/0000-0001-8921-5742</orcidid></addata></record> |
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| ispartof | International microbiology, 2023-08, Vol.26 (3), p.579-589 |
| issn | 1618-1905 1139-6709 1618-1905 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_2770118919 |
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| subjects | Ammonium Ammonium sulfate Anion exchange Anion exchanging Applied Microbiology Aspergillus oryzae Aspergillus oryzae - metabolism Biofuels Biomedical and Life Sciences Calcium ions Cellulase Cellulase - metabolism Electrophoresis Endoglucanase Enzymatic activity Enzyme activity Enzyme Stability Enzymes Eukaryotic Microbiology Hot Temperature Hydrogen-Ion Concentration Industrial applications Life Sciences Medical Microbiology Microbial Ecology Microbiology Molecular weight pH effects Pharmaceutical industry Substrate Specificity Substrates Temperature Zinc |
| title | Purification and enzymatic properties of a new thermostable endoglucanase from Aspergillus oryzae HML366 |
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