Hyaluronic acid degradation by Purpureocillium lilacinum: biochemical and transcriptomic insights.
Saved in:
| Title: | Hyaluronic acid degradation by Purpureocillium lilacinum: biochemical and transcriptomic insights. |
|---|---|
| Authors: | Minguet-Lobato, Marina1,2 (AUTHOR) m.minguet@csic.es, Fernández-Polo, David1 (AUTHOR), Cervantes, Fadia V.1 (AUTHOR), Plou, Francisco J.1 (AUTHOR), Fernández-Lobato, María2 (AUTHOR) maria.fernandezlobato@uam.es |
| Source: | Applied Microbiology & Biotechnology. 3/22/2026, Vol. 110 Issue 1, p1-12. 12p. |
| Subjects: | Hyaluronic acid, Depolymerization, Biotechnology, Glycosidases, Filamentous fungi, Transcriptomes, Oligosaccharides, Fungal enzymes |
| Abstract: | Enzymatic depolymerization of hyaluronic acid into well-defined oligosaccharides offers a sustainable alternative to chemical methods, providing precise control over product size and functionality. Yet, fungal enzymes capable of this transformation remain largely unexplored, despite fungi being prolific producers of carbohydrate-active enzymes through their complex secretomes. Here, we report the extracellular degradation of high molecular weight hyaluronic acid by the filamentous fungus Purpureocillium lilacinum. Hyaluronan depolymerization was monitored directly in culture supernatants, revealing the progressive accumulation of hyaluronan fragments and oligosaccharides with varying degrees of polymerization. Chromatographic time-resolved analyses showed the sequential appearance of long and short fragments, while mass spectrometric analysis demonstrated a complex product profile composed of even-numbered saturated and both even- and rare odd-numbered unsaturated species. This pattern differs from the uniform profiles typically generated by canonical hyaluronidases, suggesting a non-canonical degradation mechanism. Comparative cultivation of different Purpureocillium species showed that this activity is restricted to P.lilacinum among the species tested. To explore the genetic basis of this phenotype, a de novo transcriptome was assembled and functionally annotated. Although numerous carbohydrate-active enzymes were identified, none of the secreted candidates could be confidently assigned to known canonical hyaluronidase families. In particular, polysaccharide lyases associated with β-elimination mechanisms were not predicted to be secreted, and only a small fraction of glycoside hydrolases from families previously linked to hyaluronan degradation were extracellular. Together, our results establish P.lilacinum as a novel fungal system capable of extracellular hyaluronic acid degradation and support the existence of a non-canonical, potentially multienzymatic pathway. This work expands current knowledge of fungal glycosaminoglycan metabolism and highlights filamentous fungi as an underexplored source of hyaluronan-processing activities with biotechnological potential. Key points: • Purpureocillium lilacinum is a new hyaluronic acid degrader • Degradation yields diverse saturated and unsaturated hyaluronan oligosaccharides • Transcriptomics suggests a non-canonical, multienzymatic degradation system [ABSTRACT FROM AUTHOR] |
| Copyright of Applied Microbiology & Biotechnology is the property of Springer Nature and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.) | |
| Database: | Engineering Source |
|
Full text is not displayed to guests.
Login for full access.
|
|
| FullText | Links: – Type: pdflink Text: Availability: 1 |
|---|---|
| Header | DbId: egs DbLabel: Engineering Source An: 192461639 AccessLevel: 6 PubType: Academic Journal PubTypeId: academicJournal PreciseRelevancyScore: 0 |
| IllustrationInfo | |
| Items | – Name: Title Label: Title Group: Ti Data: Hyaluronic acid degradation by Purpureocillium lilacinum: biochemical and transcriptomic insights. – Name: Author Label: Authors Group: Au Data: <searchLink fieldCode="AR" term="%22Minguet-Lobato%2C+Marina%22">Minguet-Lobato, Marina</searchLink><relatesTo>1,2</relatesTo> (AUTHOR)<i> m.minguet@csic.es</i><br /><searchLink fieldCode="AR" term="%22Fernández-Polo%2C+David%22">Fernández-Polo, David</searchLink><relatesTo>1</relatesTo> (AUTHOR)<br /><searchLink fieldCode="AR" term="%22Cervantes%2C+Fadia+V%2E%22">Cervantes, Fadia V.</searchLink><relatesTo>1</relatesTo> (AUTHOR)<br /><searchLink fieldCode="AR" term="%22Plou%2C+Francisco+J%2E%22">Plou, Francisco J.</searchLink><relatesTo>1</relatesTo> (AUTHOR)<br /><searchLink fieldCode="AR" term="%22Fernández-Lobato%2C+María%22">Fernández-Lobato, María</searchLink><relatesTo>2</relatesTo> (AUTHOR)<i> maria.fernandezlobato@uam.es</i> – Name: TitleSource Label: Source Group: Src Data: <searchLink fieldCode="JN" term="%22Applied+Microbiology+%26+Biotechnology%22">Applied Microbiology & Biotechnology</searchLink>. 3/22/2026, Vol. 110 Issue 1, p1-12. 12p. – Name: Subject Label: Subjects Group: Su Data: <searchLink fieldCode="DE" term="%22Hyaluronic+acid%22">Hyaluronic acid</searchLink><br /><searchLink fieldCode="DE" term="%22Depolymerization%22">Depolymerization</searchLink><br /><searchLink fieldCode="DE" term="%22Biotechnology%22">Biotechnology</searchLink><br /><searchLink fieldCode="DE" term="%22Glycosidases%22">Glycosidases</searchLink><br /><searchLink fieldCode="DE" term="%22Filamentous+fungi%22">Filamentous fungi</searchLink><br /><searchLink fieldCode="DE" term="%22Transcriptomes%22">Transcriptomes</searchLink><br /><searchLink fieldCode="DE" term="%22Oligosaccharides%22">Oligosaccharides</searchLink><br /><searchLink fieldCode="DE" term="%22Fungal+enzymes%22">Fungal enzymes</searchLink> – Name: Abstract Label: Abstract Group: Ab Data: Enzymatic depolymerization of hyaluronic acid into well-defined oligosaccharides offers a sustainable alternative to chemical methods, providing precise control over product size and functionality. Yet, fungal enzymes capable of this transformation remain largely unexplored, despite fungi being prolific producers of carbohydrate-active enzymes through their complex secretomes. Here, we report the extracellular degradation of high molecular weight hyaluronic acid by the filamentous fungus Purpureocillium lilacinum. Hyaluronan depolymerization was monitored directly in culture supernatants, revealing the progressive accumulation of hyaluronan fragments and oligosaccharides with varying degrees of polymerization. Chromatographic time-resolved analyses showed the sequential appearance of long and short fragments, while mass spectrometric analysis demonstrated a complex product profile composed of even-numbered saturated and both even- and rare odd-numbered unsaturated species. This pattern differs from the uniform profiles typically generated by canonical hyaluronidases, suggesting a non-canonical degradation mechanism. Comparative cultivation of different Purpureocillium species showed that this activity is restricted to P.lilacinum among the species tested. To explore the genetic basis of this phenotype, a de novo transcriptome was assembled and functionally annotated. Although numerous carbohydrate-active enzymes were identified, none of the secreted candidates could be confidently assigned to known canonical hyaluronidase families. In particular, polysaccharide lyases associated with β-elimination mechanisms were not predicted to be secreted, and only a small fraction of glycoside hydrolases from families previously linked to hyaluronan degradation were extracellular. Together, our results establish P.lilacinum as a novel fungal system capable of extracellular hyaluronic acid degradation and support the existence of a non-canonical, potentially multienzymatic pathway. This work expands current knowledge of fungal glycosaminoglycan metabolism and highlights filamentous fungi as an underexplored source of hyaluronan-processing activities with biotechnological potential. Key points: • Purpureocillium lilacinum is a new hyaluronic acid degrader • Degradation yields diverse saturated and unsaturated hyaluronan oligosaccharides • Transcriptomics suggests a non-canonical, multienzymatic degradation system [ABSTRACT FROM AUTHOR] – Name: AbstractSuppliedCopyright Label: Group: Ab Data: <i>Copyright of Applied Microbiology & Biotechnology is the property of Springer Nature and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract.</i> (Copyright applies to all Abstracts.) |
| PLink | https://search.ebscohost.com/login.aspx?direct=true&site=eds-live&db=egs&AN=192461639 |
| RecordInfo | BibRecord: BibEntity: Identifiers: – Type: doi Value: 10.1007/s00253-026-13790-5 Languages: – Code: eng Text: English PhysicalDescription: Pagination: PageCount: 12 StartPage: 1 Subjects: – SubjectFull: Hyaluronic acid Type: general – SubjectFull: Depolymerization Type: general – SubjectFull: Biotechnology Type: general – SubjectFull: Glycosidases Type: general – SubjectFull: Filamentous fungi Type: general – SubjectFull: Transcriptomes Type: general – SubjectFull: Oligosaccharides Type: general – SubjectFull: Fungal enzymes Type: general Titles: – TitleFull: Hyaluronic acid degradation by Purpureocillium lilacinum: biochemical and transcriptomic insights. Type: main BibRelationships: HasContributorRelationships: – PersonEntity: Name: NameFull: Minguet-Lobato, Marina – PersonEntity: Name: NameFull: Fernández-Polo, David – PersonEntity: Name: NameFull: Cervantes, Fadia V. – PersonEntity: Name: NameFull: Plou, Francisco J. – PersonEntity: Name: NameFull: Fernández-Lobato, María IsPartOfRelationships: – BibEntity: Dates: – D: 22 M: 03 Text: 3/22/2026 Type: published Y: 2026 Identifiers: – Type: issn-print Value: 01757598 Numbering: – Type: volume Value: 110 – Type: issue Value: 1 Titles: – TitleFull: Applied Microbiology & Biotechnology Type: main |
| ResultId | 1 |
