Zobrazeno 1 - 10
of 82
pro vyhledávání: '"Jaime Eyzaguirre"'
Publikováno v:
Mycology, Vol 10, Iss 2, Pp 118-125 (2019)
Penicillium purpurogenum is a filamentous fungus, which grows on a variety of natural carbon sources and secretes a large number of enzymes involved in cellulose, hemicelluloses and pectin biodegradation. The purpose of this work has been to identify
Externí odkaz:
https://doaj.org/article/2e2f57d5ea0f47a48d782b490be01baf
Autor:
Wladimir Mardones, Alex Di Genova, María Paz Cortés, Dante Travisany, Alejandro Maass, Jaime Eyzaguirre
Publikováno v:
Mycology, Vol 9, Iss 1, Pp 59-69 (2018)
The high lignocellulolytic activity displayed by the soft-rot fungus Penicillium purpurogenum has made it a target for the study of novel lignocellulolytic enzymes. We have obtained a reference genome of 36.2 Mb of non-redundant sequence (11,057 prot
Externí odkaz:
https://doaj.org/article/91880b91e8934fc68e708cfd8bc91b35
Autor:
RENATO CHÁVEZ, KAREN SCHACHTER, CLAUDIO NAVARRO, ALESSANDRA PEIRANO, PAULINA BULL, JAIME EYZAGUIRRE
Publikováno v:
Biological Research, Vol 37, Iss 1, Pp 107-113 (2004)
The expression of the acetyl xylan esterase II (axeII) gene from Penicillium purpurogenum is repressed by glucose and induced by xylan, as well as to a small degree by xylose and xylitol. This gene is expressed at neutral pH, but not under alkaline o
Externí odkaz:
https://doaj.org/article/c8ec626710db4fa3b4114abb01f85d41
Autor:
RENATO CHÁVEZ, CAROLINA ALMARZA, KAREN SCHACHTER, ALESSANDRA PEIRANO, PAULINA BULL, JAIME EYZAGUIRRE
Publikováno v:
Biological Research, Vol 34, Iss 3-4, Pp 217-226 (2001)
Penicillium purpurogenum produces several endoxylanases, two of which (XynA and XynB) have been purified and characterized. XynB has been sequenced, and it belongs to glycosyl hydrolase family 11. In this publication we report the structure of the xy
Externí odkaz:
https://doaj.org/article/74a7f738cd984b7982673c494915db34
Autor:
Jaime Eyzaguirre, Karina Espinoza
Publikováno v:
Carbohydrate Research. 468:45-50
Penicillium purpurogenum grows on a variety of natural carbon sources and secretes to the medium a large number of enzymes that degrade the polysaccharides present in lignocellulose. In this work, the gene coding for a novel xylanase (XynC) belonging
Publikováno v:
Mycology, Vol 10, Iss 2, Pp 118-125 (2019)
Penicillium purpurogenum is a filamentous fungus, which grows on a variety of natural carbon sources and secretes a large number of enzymes involved in cellulose, hemicelluloses and pectin biodegradation. The purpose of this work has been to identify
Autor:
Valentina Echeverría, Jaime Eyzaguirre
Publikováno v:
Applied Biochemistry and Biotechnology. 187:298-309
The fungus Penicillium purpurogenum grows on a variety of natural carbon sources and secretes a large number of enzymes which degrade the polysaccharides present in lignocellulose. In this work, the gene coding for a novel endoxylanase has been ident
Autor:
Jaime Eyzaguirre, Felipe Bravo-Moraga, Danilo Gonzalez-Nilo, María Cristina Ravanal, Felipe Vilches
Publikováno v:
Carbohydrate Research. 455:106-113
Penicillium purpurogenum secretes numerous lignocellulose-degrading enzymes, including four arabinofuranosidases and an exo-arabinanase. In this work, the biochemical properties of an endo-arabinanase (ABN1) are presented. A gene, coding for a potent
Autor:
María Cristina Ravanal, Luis Morales-Quintana, Vasni Zavaleta, Carolina Faúndez, Raúl Herrera, María Alejandra Moya-León, Jaime Eyzaguirre
Publikováno v:
Carbohydrate Research. 448:57-66
The fungus Penicillium purpurogenum degrades plant cell walls by the action of cellulolytic, xylanolytic and pectinolytic enzymes. The α-D-galactosidase is one of the enzymes which may act on pectin degradation. This enzyme has several biotechnologi
Publikováno v:
Applied Biochemistry and Biotechnology. 179:143-154
The genes of two α-L-arabinofuranosidases (AbfI and II) from family GH 62 have been identified in the genome of Aspergillus fumigatus wmo. Both genes have been expressed in Pichia pastoris and the enzymes have been purified and characterized. AbfI i