Zobrazeno 1 - 10
of 109
pro vyhledávání: '"F.I.J. Pastor"'
Autor:
Susana V. Valenzuela, Elena Jiménez-Ortega, Julia Sanz-Aparicio, Mercedes Ramírez-Escudero, F.I.J. Pastor
Publikováno v:
Digital.CSIC. Repositorio Institucional del CSIC
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13 pags., 6 figs., 2 tabs.
Reducing-end xylose-releasing exo-oligoxylanases (Rex) are GH8 enzymes that depolymerize xylooligosaccharides complementing xylan degradation by endoxylanases in an exo manner. We have studied Paenibacillus barcinonens
Reducing-end xylose-releasing exo-oligoxylanases (Rex) are GH8 enzymes that depolymerize xylooligosaccharides complementing xylan degradation by endoxylanases in an exo manner. We have studied Paenibacillus barcinonens
Oxidized Product Profiles of AA9 Lytic Polysaccharide Monooxygenases Depend on the Type of Cellulose
Autor:
Pimvisuth Chunkrua, Peicheng Sun, Willem J. H. van Berkel, Susana V. Valenzuela, Christophe V. F. P. Laurent, Mirjam A. Kabel, Roland Ludwig, F.I.J. Pastor
Publikováno v:
ACS Sustainable Chemistry & Engineering
ACS Sustainable Chemistry and Engineering, 9(42), 14124-14133
ACS Sustainable Chemistry and Engineering 9 (2021) 42
ACS Sustainable Chemistry and Engineering, 9(42), 14124-14133
ACS Sustainable Chemistry and Engineering 9 (2021) 42
Lytic polysaccharide monooxygenases (LPMOs) are essential for enzymatic conversion of lignocellulose-rich biomass in the context of biofuels and platform chemicals production. Considerable insight into the mode of action of LPMOs has been obtained, b
Publikováno v:
Biotechnology and Applied Biochemistry. 63:51-56
The gene coding for a lichenase from Paenibacillus barcinonensis BP-23, a powerful carbohydrate-degrading strain, was obtained using a genome walking strategy and expressed in Escherichia coli for further characterization. The amino acid sequence ded
Publikováno v:
Cellulose. 21:203-219
A newly identified cellulase with a high polysaccharide degrading potential and a processive mode of action, has been evaluated on cellulose fibers. Cellulase Cel9B from Paenibacillus barcinonensis is a modular endoglucanase with the domain structure
Publikováno v:
Recercat. Dipósit de la Recerca de Catalunya
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UPCommons. Portal del coneixement obert de la UPC
Universitat Politècnica de Catalunya (UPC)
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UPCommons. Portal del coneixement obert de la UPC
Universitat Politècnica de Catalunya (UPC)
Four new bacterial xylanases from different glycosyl hydrolase families (11, 10 and 5) were evaluated for hexenuronic acid (HexA) removal capacity and bleach boosting ability of a eucalypt kraft pulp. The family 11 xylanase was the most effective in
Publikováno v:
Letters in Applied Microbiology. 45:108-113
Aims: To isolate new fungal strains from subtropical soils and to identify those that produce high cellulase activity. To select microbial strains producing thermostable cellulases with potential application in industry. Methods and Results: The new
Publikováno v:
Letters in Applied Microbiology. 40:218-227
C. RUIZ, F.I.J. PASTOR AND P. DIAZ.2005. Aims: To isolate the micro-organisms from three soil samples obtained from a subtropical forest of Puerto Iguazu ´ (Argentina), to analyse them for detection of the biotechnologically interesting enzymatic ac
Publikováno v:
Cellulose. 9:115-125
The effect of two different cellulases on the hornification phenomenon,in which drainability (Schopper–Riegler method) and mechanical propertiesdiminish when pulps are dried, was studied. The enzyme applications testedincluded a commercial enzyme n
Publikováno v:
Applied Microbiology and Biotechnology. 55:61-68
The gene celB encoding an endoglucanase from Paenibacillus sp. BP-23 was cloned and expressed in Escherichia coli. The nucleotide sequence of a 4161 bp DNA fragment containing the celB gene was determined, revealing an open reading frame of 2991 nucl
Publikováno v:
Bioresource Technology. 74:135-140
The use of a novel ‘‘xylanase A’’ enzyme was found beneficial in the elemental chlorine free (ECF) bleaching of oxygen delignified Eucalyptus kraft pulps. The application of the enzyme made possible production of fully bleached pulps with hig