Characterization of a surface-active protein extracted from a marine strain of penicillium chrysogenum
Cicatiello, Paola ; Stanzione, Ilaria ; Dardano, Principia ; De Stefano, Luca ; Birolo, Leila ; De Chiaro, Addolorata ; Monti, Daria Maria ; Petruk, Ganna LU
; D’errico, Gerardino
and Giardina, Paola
(2019)
In International Journal of Molecular Sciences
20(13).
p.1-13
- Abstract
Marine microorganisms represent a reservoir of new promising secondary metabolites. Surface-active proteins with good emulsification activity can be isolated from fungal species that inhabit the marine environment and can be promising candidates for different biotechnological applications. In this study a novel surface-active protein, named Sap-Pc, was purified from a marine strain of Penicillium chrysogenum. The effect of salt concentration and temperature on protein production was analyzed, and a purification method was set up. The purified protein, identified as Pc13g06930, was annotated as a hypothetical protein. It was able to form emulsions, which were stable for at least one month, with an emulsification index comparable to that... (More)
Marine microorganisms represent a reservoir of new promising secondary metabolites. Surface-active proteins with good emulsification activity can be isolated from fungal species that inhabit the marine environment and can be promising candidates for different biotechnological applications. In this study a novel surface-active protein, named Sap-Pc, was purified from a marine strain of Penicillium chrysogenum. The effect of salt concentration and temperature on protein production was analyzed, and a purification method was set up. The purified protein, identified as Pc13g06930, was annotated as a hypothetical protein. It was able to form emulsions, which were stable for at least one month, with an emulsification index comparable to that of other known surface-active proteins. The surface tension reduction was analyzed as function of protein concentration and a critical micellar concentration of 2 µM was determined. At neutral or alkaline pH, secondary structure changes were monitored over time, concurrently with the appearance of protein precipitation. Formation of amyloid-like fibrils of SAP-Pc was demonstrated by spectroscopic and microscopic analyses. Moreover, the effect of protein concentration, a parameter affecting kinetics of fibril formation, was investigated and an on-pathway involvement of micellar aggregates during the fibril formation process was suggested.
(Less)
- author
- Cicatiello, Paola
; Stanzione, Ilaria
; Dardano, Principia
; De Stefano, Luca
; Birolo, Leila
; De Chiaro, Addolorata
; Monti, Daria Maria
; Petruk, Ganna
LU
; D’errico, Gerardino
and Giardina, Paola
- publishing date
- 2019-07-01
- type
- Contribution to journal
- publication status
- published
- keywords
- Amyloid fibrils, Biosurfactant proteins, Emulsions, Marine fungi
- in
- International Journal of Molecular Sciences
- volume
- 20
- issue
- 13
- article number
- 3242
- pages
- 1 - 13
- publisher
- MDPI AG
- external identifiers
-
- pmid:31269636
- scopus:85068693057
- ISSN
- 1661-6596
- DOI
- 10.3390/ijms20133242
- language
- English
- LU publication?
- no
- additional info
- Publisher Copyright: © 2019 by the authors. Licensee MDPI, Basel, Switzerland.
- id
- 5b8fb8fc-6d58-4984-aecb-a4f4cafce5ce
- date added to LUP
- 2025-01-21 15:46:32
- date last changed
- 2025-07-09 05:33:48
@article{5b8fb8fc-6d58-4984-aecb-a4f4cafce5ce,
abstract = {{<p>Marine microorganisms represent a reservoir of new promising secondary metabolites. Surface-active proteins with good emulsification activity can be isolated from fungal species that inhabit the marine environment and can be promising candidates for different biotechnological applications. In this study a novel surface-active protein, named Sap-Pc, was purified from a marine strain of Penicillium chrysogenum. The effect of salt concentration and temperature on protein production was analyzed, and a purification method was set up. The purified protein, identified as Pc13g06930, was annotated as a hypothetical protein. It was able to form emulsions, which were stable for at least one month, with an emulsification index comparable to that of other known surface-active proteins. The surface tension reduction was analyzed as function of protein concentration and a critical micellar concentration of 2 µM was determined. At neutral or alkaline pH, secondary structure changes were monitored over time, concurrently with the appearance of protein precipitation. Formation of amyloid-like fibrils of SAP-Pc was demonstrated by spectroscopic and microscopic analyses. Moreover, the effect of protein concentration, a parameter affecting kinetics of fibril formation, was investigated and an on-pathway involvement of micellar aggregates during the fibril formation process was suggested.</p>}},
author = {{Cicatiello, Paola and Stanzione, Ilaria and Dardano, Principia and De Stefano, Luca and Birolo, Leila and De Chiaro, Addolorata and Monti, Daria Maria and Petruk, Ganna and D’errico, Gerardino and Giardina, Paola}},
issn = {{1661-6596}},
keywords = {{Amyloid fibrils; Biosurfactant proteins; Emulsions; Marine fungi}},
language = {{eng}},
month = {{07}},
number = {{13}},
pages = {{1--13}},
publisher = {{MDPI AG}},
series = {{International Journal of Molecular Sciences}},
title = {{Characterization of a surface-active protein extracted from a marine strain of penicillium chrysogenum}},
url = {{http://dx.doi.org/10.3390/ijms20133242}},
doi = {{10.3390/ijms20133242}},
volume = {{20}},
year = {{2019}},
}