2018 |
Gil-Durán, C; Ravanal, M C; Ubilla, P; Vaca, I; Chávez, R Heterologous Expression, Purification and Characterization of a Highly Thermolabile Endoxylanase from the Antarctic Fungus Cladosporium Sp Artículo de revista Fungal Biology, 122 (9), pp. 875-882, 2018, ISSN: 1878-6146. Resumen | Enlaces | BibTeX | Etiquetas: Antarctica, Cold-active Cold-adapted Low Xylan enzyme, fungus, thermostability @article{RN383, title = {Heterologous Expression, Purification and Characterization of a Highly Thermolabile Endoxylanase from the Antarctic Fungus Cladosporium Sp}, author = { C. Gil-Dur\'{a}n and M.C. Ravanal and P. Ubilla and I. Vaca and R. Ch\'{a}vez}, url = {http://www.sciencedirect.com/science/article/pii/S187861461830093X}, doi = {10.1016/j.funbio.2018.05.002}, issn = {1878-6146}, year = {2018}, date = {2018-01-01}, journal = {Fungal Biology}, volume = {122}, number = {9}, pages = {875-882}, abstract = {Numerous endoxylanases from mesophilic fungi have been purified and characterized. However, endoxylanases from cold-adapted fungi, especially those from Antarctica, have been less studied. In this work, a cDNA from the Antarctic fungus Cladosporium sp. with similarity to endoxylanases from glycosyl hydrolase family 10, was cloned and expressed in Pichia pastoris. The pure recombinant enzyme (named XynA) showed optimal activity on xylan at 50 °C and pH 6\textendash7. The enzyme releases xylooligosaccharides but not xylose, indicating that XynA is a classical endoxylanase. The enzyme was most active on xylans with high content of arabinose (rye arabinoylan and wheat arabinoxylan) than on xylans with low content of arabinose (oat spelts xylan, birchwood xylan and beechwood xylan). Finally, XynA showed a very low thermostability. After 20\textendash30 min of incubation at 40 °C, the enzyme was completely inactivated, suggesting that XynA would be the most thermolabile endoxylanase described so far in filamentous fungi. This is one of the few reports describing the heterologous expression and characterization of a xylanase from a fungus isolated from Antarctica.}, keywords = {Antarctica, Cold-active Cold-adapted Low Xylan enzyme, fungus, thermostability}, pubstate = {published}, tppubtype = {article} } Numerous endoxylanases from mesophilic fungi have been purified and characterized. However, endoxylanases from cold-adapted fungi, especially those from Antarctica, have been less studied. In this work, a cDNA from the Antarctic fungus Cladosporium sp. with similarity to endoxylanases from glycosyl hydrolase family 10, was cloned and expressed in Pichia pastoris. The pure recombinant enzyme (named XynA) showed optimal activity on xylan at 50 °C and pH 6–7. The enzyme releases xylooligosaccharides but not xylose, indicating that XynA is a classical endoxylanase. The enzyme was most active on xylans with high content of arabinose (rye arabinoylan and wheat arabinoxylan) than on xylans with low content of arabinose (oat spelts xylan, birchwood xylan and beechwood xylan). Finally, XynA showed a very low thermostability. After 20–30 min of incubation at 40 °C, the enzyme was completely inactivated, suggesting that XynA would be the most thermolabile endoxylanase described so far in filamentous fungi. This is one of the few reports describing the heterologous expression and characterization of a xylanase from a fungus isolated from Antarctica. |
2011 |
San-Martin, A; Rovirosa, J; Vaca, I; Vergara, K; Acevedo, L; Vina, D; Orallo, F; Chamy, M C New Butyrolactone from a Marine-Derived Fungus Aspergillus Sp Artículo de revista Journal of the Chilean Chemical Society, 56 (1), pp. 625-627, 2011, ISSN: 0717-9707. Resumen | Enlaces | BibTeX | Etiquetas: aspergillus dibenzylbutyrolactone, fungus, marine-derived sesterterpenoids, sp strain @article{RN33e, title = {New Butyrolactone from a Marine-Derived Fungus Aspergillus Sp}, author = { A. San-Martin and J. Rovirosa and I. Vaca and K. Vergara and L. Acevedo and D. Vina and F. Orallo and M.C. Chamy}, url = {/brokenurl#<Go to ISI>://WOS:000290700500023}, doi = {10.4067/S0717-97072011000100023}, issn = {0717-9707}, year = {2011}, date = {2011-01-01}, journal = {Journal of the Chilean Chemical Society}, volume = {56}, number = {1}, pages = {625-627}, abstract = {Four compounds that belong to two structure types, namely dibenzylbutyrolactone and sesterterpenoids, were obtained from the extract of the strain Aspergillus sp. (2P-22), isolated from a marine sponge, Cliona chilensis. Among them, compound I was identified as new, namely butylrolactone-VI. The structures of these compounds were characterized on the basis of spectroscopic data. Biological activities of these fungal metabolites, are described.}, keywords = {aspergillus dibenzylbutyrolactone, fungus, marine-derived sesterterpenoids, sp strain}, pubstate = {published}, tppubtype = {article} } Four compounds that belong to two structure types, namely dibenzylbutyrolactone and sesterterpenoids, were obtained from the extract of the strain Aspergillus sp. (2P-22), isolated from a marine sponge, Cliona chilensis. Among them, compound I was identified as new, namely butylrolactone-VI. The structures of these compounds were characterized on the basis of spectroscopic data. Biological activities of these fungal metabolites, are described. |
2018 |
Heterologous Expression, Purification and Characterization of a Highly Thermolabile Endoxylanase from the Antarctic Fungus Cladosporium Sp Artículo de revista Fungal Biology, 122 (9), pp. 875-882, 2018, ISSN: 1878-6146. |
2011 |
New Butyrolactone from a Marine-Derived Fungus Aspergillus Sp Artículo de revista Journal of the Chilean Chemical Society, 56 (1), pp. 625-627, 2011, ISSN: 0717-9707. |