An AA9-LPMO containing a CBM1 domain in Aspergillus nidulans is active on cellulose and cleaves cello-oligosaccharides
Abstract Lytic polysaccharide monooxygenases (LPMOs) are copper dependent enzymes that carry out oxidative cleavage of cellulose and other polysaccharides. Aspergillus nidulans, an ascomycete fungus that contains multiple AA9 LPMOs in the genome, offers an excellent model system to study their activ...
| Main Authors: | , , |
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| Format: | Article |
| Language: | English |
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SpringerOpen
2018-10-01
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| Series: | AMB Express |
| Subjects: | |
| Online Access: | http://link.springer.com/article/10.1186/s13568-018-0701-5 |
| _version_ | 1811290695413006336 |
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| author | Guru Jagadeeswaran Lawrie Gainey Andrew J. Mort |
| author_facet | Guru Jagadeeswaran Lawrie Gainey Andrew J. Mort |
| author_sort | Guru Jagadeeswaran |
| collection | DOAJ |
| description | Abstract Lytic polysaccharide monooxygenases (LPMOs) are copper dependent enzymes that carry out oxidative cleavage of cellulose and other polysaccharides. Aspergillus nidulans, an ascomycete fungus that contains multiple AA9 LPMOs in the genome, offers an excellent model system to study their activity during the oxidative degradation of biomass. AN1602, a dual domain AA9-LPMO in A. nidulans appended with a carbohydrate-binding module, CBM1, was expressed in Pichia pastoris for analyzing oxidative cleavage on cellulosic substrates. The mass spectral and HPAEC analyses showed that the enzyme cleaves phosphoric acid swollen cellulose (PASC) in the presence of a reducing agent, yielding a range of cello-oligosaccharides. In addition to the polymeric substrate cellulose, AN1602 is also active on soluble cellohexaose, a property that is restricted to only a few characterized LPMOs. Product analysis of AN1602 cleaved cellohexaose revealed that C4 was the sole site of oxidation. The sequence and predicted structure of the catalytic domain of AN1602 matched very closely to known C4 cellohexaose active enzymes. |
| first_indexed | 2024-04-13T04:17:15Z |
| format | Article |
| id | doaj.art-1fb132edd6f14e3384628f099415065f |
| institution | Directory Open Access Journal |
| issn | 2191-0855 |
| language | English |
| last_indexed | 2024-04-13T04:17:15Z |
| publishDate | 2018-10-01 |
| publisher | SpringerOpen |
| record_format | Article |
| series | AMB Express |
| spelling | doaj.art-1fb132edd6f14e3384628f099415065f2022-12-22T03:02:56ZengSpringerOpenAMB Express2191-08552018-10-018111310.1186/s13568-018-0701-5An AA9-LPMO containing a CBM1 domain in Aspergillus nidulans is active on cellulose and cleaves cello-oligosaccharidesGuru Jagadeeswaran0Lawrie Gainey1Andrew J. Mort2Department of Biochemistry and Molecular Biology, Oklahoma State UniversityDepartment of Biochemistry and Molecular Biology, Oklahoma State UniversityDepartment of Biochemistry and Molecular Biology, Oklahoma State UniversityAbstract Lytic polysaccharide monooxygenases (LPMOs) are copper dependent enzymes that carry out oxidative cleavage of cellulose and other polysaccharides. Aspergillus nidulans, an ascomycete fungus that contains multiple AA9 LPMOs in the genome, offers an excellent model system to study their activity during the oxidative degradation of biomass. AN1602, a dual domain AA9-LPMO in A. nidulans appended with a carbohydrate-binding module, CBM1, was expressed in Pichia pastoris for analyzing oxidative cleavage on cellulosic substrates. The mass spectral and HPAEC analyses showed that the enzyme cleaves phosphoric acid swollen cellulose (PASC) in the presence of a reducing agent, yielding a range of cello-oligosaccharides. In addition to the polymeric substrate cellulose, AN1602 is also active on soluble cellohexaose, a property that is restricted to only a few characterized LPMOs. Product analysis of AN1602 cleaved cellohexaose revealed that C4 was the sole site of oxidation. The sequence and predicted structure of the catalytic domain of AN1602 matched very closely to known C4 cellohexaose active enzymes.http://link.springer.com/article/10.1186/s13568-018-0701-5Lytic polysaccharide monooxygenasesAN1602AA9 LPMOAspergillus nidulansCelluloseCellohexaose |
| spellingShingle | Guru Jagadeeswaran Lawrie Gainey Andrew J. Mort An AA9-LPMO containing a CBM1 domain in Aspergillus nidulans is active on cellulose and cleaves cello-oligosaccharides AMB Express Lytic polysaccharide monooxygenases AN1602 AA9 LPMO Aspergillus nidulans Cellulose Cellohexaose |
| title | An AA9-LPMO containing a CBM1 domain in Aspergillus nidulans is active on cellulose and cleaves cello-oligosaccharides |
| title_full | An AA9-LPMO containing a CBM1 domain in Aspergillus nidulans is active on cellulose and cleaves cello-oligosaccharides |
| title_fullStr | An AA9-LPMO containing a CBM1 domain in Aspergillus nidulans is active on cellulose and cleaves cello-oligosaccharides |
| title_full_unstemmed | An AA9-LPMO containing a CBM1 domain in Aspergillus nidulans is active on cellulose and cleaves cello-oligosaccharides |
| title_short | An AA9-LPMO containing a CBM1 domain in Aspergillus nidulans is active on cellulose and cleaves cello-oligosaccharides |
| title_sort | aa9 lpmo containing a cbm1 domain in aspergillus nidulans is active on cellulose and cleaves cello oligosaccharides |
| topic | Lytic polysaccharide monooxygenases AN1602 AA9 LPMO Aspergillus nidulans Cellulose Cellohexaose |
| url | http://link.springer.com/article/10.1186/s13568-018-0701-5 |
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