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Functional characterization of a thermostable endoglucanase belonging to glycoside hydrolase family 45 from Fomitopsis palustris
A gene encoding an endoglucanase belonging to subfamily C of glycoside hydrolase family 45 (GH45) was identified in the brown rot fungus Fomitopsis palustris and functionally expressed in Pichia pastoris . The recombinant protein displayed hydrolytic activities toward various substrates such as carb...
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| Published in: | Applied microbiology and biotechnology 2018-08, Vol.102 (15), p.6515-6523 |
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| container_title | Applied microbiology and biotechnology |
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| creator | Cha, Ju-Hee Yoon, Jeong-Jun Cha, Chang-Jun |
| description | A gene encoding an endoglucanase belonging to subfamily C of glycoside hydrolase family 45 (GH45) was identified in the brown rot fungus
Fomitopsis palustris
and functionally expressed in
Pichia pastoris
. The recombinant protein displayed hydrolytic activities toward various substrates such as carboxymethyl cellulose, phosphoric acid swollen cellulose, glucomannan, lichenan, and β-glucan. In particular, the enzyme had a unique catalytic efficiency on β-1,4-glucans rather than mixed β-1,3/1,4-glucans as compared to other GH45 endoglucanases. The fungal enzyme was relatively thermostable, retaining more than 91.4% activity at 80 °C for 1 h. Site-directed mutagenesis studies revealed that the mutants N95D and D117N had significantly reduced enzymatic activities, indicating that both residues are essential for the catalytic reaction. Our study expands knowledge and understanding of the catalytic mechanism of GH45 subfamily C enzymes and also suggests that this thermostable endoglucanase from
F. palustris
has great potential in industrial applications. |
| doi_str_mv | 10.1007/s00253-018-9075-5 |
| format | article |
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Fomitopsis palustris
and functionally expressed in
Pichia pastoris
. The recombinant protein displayed hydrolytic activities toward various substrates such as carboxymethyl cellulose, phosphoric acid swollen cellulose, glucomannan, lichenan, and β-glucan. In particular, the enzyme had a unique catalytic efficiency on β-1,4-glucans rather than mixed β-1,3/1,4-glucans as compared to other GH45 endoglucanases. The fungal enzyme was relatively thermostable, retaining more than 91.4% activity at 80 °C for 1 h. Site-directed mutagenesis studies revealed that the mutants N95D and D117N had significantly reduced enzymatic activities, indicating that both residues are essential for the catalytic reaction. Our study expands knowledge and understanding of the catalytic mechanism of GH45 subfamily C enzymes and also suggests that this thermostable endoglucanase from
F. palustris
has great potential in industrial applications.</description><identifier>ISSN: 0175-7598</identifier><identifier>EISSN: 1432-0614</identifier><identifier>DOI: 10.1007/s00253-018-9075-5</identifier><identifier>PMID: 29789883</identifier><language>eng</language><publisher>Berlin/Heidelberg: Springer Berlin Heidelberg</publisher><subject>Amino Acid Sequence ; Basidiomycota ; Biomedical and Life Sciences ; Biotechnologically Relevant Enzymes and Proteins ; Biotechnology ; Brown rot ; Carboxymethyl cellulose ; Carboxymethylcellulose ; Catalysis ; Cellulase - genetics ; Cellulase - metabolism ; Cellulose ; Cellulose - chemistry ; Cellulose - metabolism ; Cloning, Molecular ; Coriolaceae - enzymology ; Endoglucanase ; Enzymatic activity ; Enzymes ; Fungi ; Glucan ; Glucans ; Glycoside hydrolase ; Hydrolase ; Industrial applications ; Industrial Microbiology ; Life Sciences ; Microbial Genetics and Genomics ; Microbiology ; Mutagenesis, Site-Directed ; Phosphoric acid ; Physiological aspects ; Pichia - genetics ; Pichia pastoris ; Proteins ; Recombinant Proteins - genetics ; Recombinant Proteins - metabolism ; Site-directed mutagenesis ; Substrate Specificity ; Substrates ; Yeast ; β-Glucan</subject><ispartof>Applied microbiology and biotechnology, 2018-08, Vol.102 (15), p.6515-6523</ispartof><rights>Springer-Verlag GmbH Germany, part of Springer Nature 2018</rights><rights>COPYRIGHT 2018 Springer</rights><rights>Applied Microbiology and Biotechnology is a copyright of Springer, (2018). All Rights Reserved.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c576t-3d6e4a06c98876e8829cd72871e30ae06ae2ba833df412fa73fe4991820cbdf83</citedby><cites>FETCH-LOGICAL-c576t-3d6e4a06c98876e8829cd72871e30ae06ae2ba833df412fa73fe4991820cbdf83</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.proquest.com/docview/2042475138/fulltextPDF?pq-origsite=primo$$EPDF$$P50$$Gproquest$$H</linktopdf><linktohtml>$$Uhttps://www.proquest.com/docview/2042475138?pq-origsite=primo$$EHTML$$P50$$Gproquest$$H</linktohtml><link.rule.ids>314,780,784,11688,27924,27925,36060,44363,74895</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/29789883$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Cha, Ju-Hee</creatorcontrib><creatorcontrib>Yoon, Jeong-Jun</creatorcontrib><creatorcontrib>Cha, Chang-Jun</creatorcontrib><title>Functional characterization of a thermostable endoglucanase belonging to glycoside hydrolase family 45 from Fomitopsis palustris</title><title>Applied microbiology and biotechnology</title><addtitle>Appl Microbiol Biotechnol</addtitle><addtitle>Appl Microbiol Biotechnol</addtitle><description>A gene encoding an endoglucanase belonging to subfamily C of glycoside hydrolase family 45 (GH45) was identified in the brown rot fungus
Fomitopsis palustris
and functionally expressed in
Pichia pastoris
. The recombinant protein displayed hydrolytic activities toward various substrates such as carboxymethyl cellulose, phosphoric acid swollen cellulose, glucomannan, lichenan, and β-glucan. In particular, the enzyme had a unique catalytic efficiency on β-1,4-glucans rather than mixed β-1,3/1,4-glucans as compared to other GH45 endoglucanases. The fungal enzyme was relatively thermostable, retaining more than 91.4% activity at 80 °C for 1 h. Site-directed mutagenesis studies revealed that the mutants N95D and D117N had significantly reduced enzymatic activities, indicating that both residues are essential for the catalytic reaction. Our study expands knowledge and understanding of the catalytic mechanism of GH45 subfamily C enzymes and also suggests that this thermostable endoglucanase from
F. palustris
has great potential in industrial applications.</description><subject>Amino Acid Sequence</subject><subject>Basidiomycota</subject><subject>Biomedical and Life Sciences</subject><subject>Biotechnologically Relevant Enzymes and Proteins</subject><subject>Biotechnology</subject><subject>Brown rot</subject><subject>Carboxymethyl cellulose</subject><subject>Carboxymethylcellulose</subject><subject>Catalysis</subject><subject>Cellulase - genetics</subject><subject>Cellulase - metabolism</subject><subject>Cellulose</subject><subject>Cellulose - chemistry</subject><subject>Cellulose - metabolism</subject><subject>Cloning, Molecular</subject><subject>Coriolaceae - enzymology</subject><subject>Endoglucanase</subject><subject>Enzymatic activity</subject><subject>Enzymes</subject><subject>Fungi</subject><subject>Glucan</subject><subject>Glucans</subject><subject>Glycoside hydrolase</subject><subject>Hydrolase</subject><subject>Industrial applications</subject><subject>Industrial Microbiology</subject><subject>Life Sciences</subject><subject>Microbial Genetics and Genomics</subject><subject>Microbiology</subject><subject>Mutagenesis, Site-Directed</subject><subject>Phosphoric acid</subject><subject>Physiological aspects</subject><subject>Pichia - genetics</subject><subject>Pichia pastoris</subject><subject>Proteins</subject><subject>Recombinant Proteins - genetics</subject><subject>Recombinant Proteins - metabolism</subject><subject>Site-directed mutagenesis</subject><subject>Substrate Specificity</subject><subject>Substrates</subject><subject>Yeast</subject><subject>β-Glucan</subject><issn>0175-7598</issn><issn>1432-0614</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2018</creationdate><recordtype>article</recordtype><sourceid>M0C</sourceid><recordid>eNp1kUuLFDEUhYMoTjv6A9xIwJWLGvOoVFLLYbDHgQHBxzqkUzfVGVKVNknBtCt_-qTp8dGgZBE4-c4l5x6EXlNyQQmR7zMhTPCGUNX0RIpGPEEr2nLWkI62T9GK0CpK0asz9CLnO0IoU133HJ2xXqpeKb5CP9fLbIuPswnYbk0ytkDyP8xBwtFhg8sW0hRzMZsAGOYhjmGxZjYZ8AZCnEc_j7hEPIa9jdkPgLf7IcVwAJyZfNjjVmCX4oTXcfIl7rLPeGfCkkvy-SV65kzI8OrxPkff1h--Xn1sbj9d31xd3jZWyK40fOigNaSz9duyA6VYbwfJlKTAiQHSGWAbozgfXEuZM5I7aPueKkbsZnCKn6O3x7m7FL8vkIu-i0uqsbNmpGWtFJT_RY0mgPazi6WuZPLZ6kvRdqIulNJKXfyDqmeAyds4g_NVPzG8OzFUpsB9Gc2Ss7758vmUpUfWpphzAqd3yU8m7TUl-lC7Ptaua-36ULsW1fPmMdyymWD47fjVcwXYEcj1aR4h_Un__6kPYM64Jg</recordid><startdate>20180801</startdate><enddate>20180801</enddate><creator>Cha, Ju-Hee</creator><creator>Yoon, Jeong-Jun</creator><creator>Cha, 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biotechnology</jtitle><stitle>Appl Microbiol Biotechnol</stitle><addtitle>Appl Microbiol Biotechnol</addtitle><date>2018-08-01</date><risdate>2018</risdate><volume>102</volume><issue>15</issue><spage>6515</spage><epage>6523</epage><pages>6515-6523</pages><issn>0175-7598</issn><eissn>1432-0614</eissn><abstract>A gene encoding an endoglucanase belonging to subfamily C of glycoside hydrolase family 45 (GH45) was identified in the brown rot fungus
Fomitopsis palustris
and functionally expressed in
Pichia pastoris
. The recombinant protein displayed hydrolytic activities toward various substrates such as carboxymethyl cellulose, phosphoric acid swollen cellulose, glucomannan, lichenan, and β-glucan. In particular, the enzyme had a unique catalytic efficiency on β-1,4-glucans rather than mixed β-1,3/1,4-glucans as compared to other GH45 endoglucanases. The fungal enzyme was relatively thermostable, retaining more than 91.4% activity at 80 °C for 1 h. Site-directed mutagenesis studies revealed that the mutants N95D and D117N had significantly reduced enzymatic activities, indicating that both residues are essential for the catalytic reaction. Our study expands knowledge and understanding of the catalytic mechanism of GH45 subfamily C enzymes and also suggests that this thermostable endoglucanase from
F. palustris
has great potential in industrial applications.</abstract><cop>Berlin/Heidelberg</cop><pub>Springer Berlin Heidelberg</pub><pmid>29789883</pmid><doi>10.1007/s00253-018-9075-5</doi><tpages>9</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0175-7598 |
| ispartof | Applied microbiology and biotechnology, 2018-08, Vol.102 (15), p.6515-6523 |
| issn | 0175-7598 1432-0614 |
| language | eng |
| recordid | cdi_proquest_journals_2042475138 |
| source | ABI/INFORM Collection; Springer Link |
| subjects | Amino Acid Sequence Basidiomycota Biomedical and Life Sciences Biotechnologically Relevant Enzymes and Proteins Biotechnology Brown rot Carboxymethyl cellulose Carboxymethylcellulose Catalysis Cellulase - genetics Cellulase - metabolism Cellulose Cellulose - chemistry Cellulose - metabolism Cloning, Molecular Coriolaceae - enzymology Endoglucanase Enzymatic activity Enzymes Fungi Glucan Glucans Glycoside hydrolase Hydrolase Industrial applications Industrial Microbiology Life Sciences Microbial Genetics and Genomics Microbiology Mutagenesis, Site-Directed Phosphoric acid Physiological aspects Pichia - genetics Pichia pastoris Proteins Recombinant Proteins - genetics Recombinant Proteins - metabolism Site-directed mutagenesis Substrate Specificity Substrates Yeast β-Glucan |
| title | Functional characterization of a thermostable endoglucanase belonging to glycoside hydrolase family 45 from Fomitopsis palustris |
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