Publicaciones 2011-2020

@article{RN384,
title = {Cold-Active Pectinolytic Activity Produced by Filamentous Fungi Associated with Antarctic Marine Sponges},
author = { G. Poveda and C. Gil-Duran and I. Vaca and G. Levican and R. Chavez},
url = {/brokenurl#<Go to ISI>://WOS:000442838400001},
doi = {10.1186/s40659-018-0177-4},
issn = {0716-9760},
year = {2018},
date = {2018-01-01},
journal = {Biological Research},
volume = {51},
abstract = {Background: Pectinase enzymes catalyze the breakdown of pectin, a keywords component of the plant cell wall. At industrial level, pectinases are used in diverse applications, especially in food-processing industry. Currently, most of the industrial pectinases have optimal activity at mesophilic temperatures. On the contrary, very little is known about the pectinolytic activities from organisms from cold climates such as Antarctica. In this work, 27 filamentous fungi isolated from marine sponges collected in King George Island, Antarctica, were screened as new source of cold-active pectinases., Results: In semi-quantitative plate assays, 8 out 27 of these isolates showed pectinolytic activities at 15 degrees C and one of them, Geomyces sp. strain F09-T3-2, showed the highest production of pectinases in liquid medium containing pectin as sole carbon source. More interesting, Geomyces sp. F09-T3-2 showed optimal pectinolytic activity at 30 degrees C, 10 degrees C under the temperature of currently available commercial mesophilic pectinases., Conclusion: Filamentous fungi associated with Antarctic marine sponges are a promising source of pectinolytic activity. In particular, pectinases from Geomyces sp. F09-T3-2 may be potentially suitable for biotechnological applications needing cold-active pectinases. To the best of our knowledge, this is the first report describing the production of pectinolytic activity from filamentous fungi from any environment in Antarctica.},
keywords = {antarctic cold-active diversity, enzymes, filamentous fungi, geomyces geomyces, marine pectinases, polygalacturonase, purification, sp., sponges, strains yeasts},
pubstate = {published},
tppubtype = {article}
}

@article{RN36h,
title = {A Preparative Method for the Purification of Isopenicillin N from Genetically Blocked Acremonium Chrysogenum Strain Td189: Studies on the Degradation Kinetics and Storage Conditions},
author = { I. Vaca and J. Casqueiro and R.V. Ullan and A. Rumbero and R. Chavez and J.F. Martin},
url = {/brokenurl#<Go to ISI>://WOS:000292090800006},
doi = {10.1038/ja.2011.30},
issn = {0021-8820},
year = {2011},
date = {2011-01-01},
journal = {Journal of Antibiotics},
volume = {64},
number = {6},
pages = {447-451},
abstract = {A protocol for preparative isopenicillin N (IPN) purification, a highly interesting and hitherto unavailable intermediate of the penicillin and cephalosporin biosynthetic pathway due to its high unstability, is described. Culture broths of Acremonium chrysogenum TD189, a strain blocked in cephalosporin biosynthesis that accumulates this metabolite, were treated with acetone and filtered though charcoal and a hydrophobic resin in a single step as tandem columns. The cleared broth was then lyophilized and passed though a Sephadex G-25 column. The last step was the purification to homogeneity of IPN in a semipreparative HPLC equipment and, optionally, a desalting step by Sephadex G-10 column. Once purified, a complete analysis of the stability of the compound and the conditions for its long-term storage was carried out. Our results suggest a first-order model for IPN decomposition for all the pH and temperature analyzed. IPN is more stable at neutral pH, and once lyophilized, can be stored under vacuum and -75 degrees C with a half-life of 770 days. The Journal of Antibiotics (2011); published online 27 April 2011},
keywords = {biosynthesis, cephalosporin-c, chrysogenum, conversion, hplc, isopenicillin liquid-chromatography n, natural-products, penicillium-chrysogenum, purification, stability, storage, system temperature},
pubstate = {published},
tppubtype = {article}
}