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A family 51 alpha-l-arabinofuranosidase from Penicillium purpurogenum: purification, properties and amino acid sequence.
The soft rot fungus Penicillium purpurogenum secretes a wide variety of xylanolytic enzymes to the medium, among them three alpha-l-arabinofuranosidases. This work refers to arabinofuranosidase 2Expand
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Comparison of different types of pretreatment and enzymatic saccharification of Macrocystis pyrifera for the production of biofuel
In this work, the brown algae Macrocystis pyrifera were pretreated with dilute sulfuric acid, water and three different types of ionic liquids (ILs): 1-ethyl-3-methylimidazolium acetate ([EMIM][OAcExpand
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Novel Bifunctional α-l-Arabinofuranosidase/Xylobiohydrolase (ABF3) from Penicillium purpurogenum
ABSTRACT The soft rot fungus Penicillium purpurogenum grows on a variety of natural substrates and secretes various isoforms of xylanolytic enzymes, including three arabinofuranosidases. This workExpand
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Penicillium purpurogenum produces a family 1 acetyl xylan esterase containing a carbohydrate-binding module: characterization of the protein and its gene.
At least three acetyl xylan esterases (AXE I, II and III) are secreted by Penicillium purpurogenum. This publication describes more detailed work on AXE I and its gene. AXE I binds cellulose but notExpand
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Thermal Stability of Phosphoenolpyruvate Carboxykinases from Escherichia coli, Trypanosoma brucei, and Saccharomyces cerevisiae
The quaternary structure of ATP-dependent phosphoenolpyruvate (PEP) carboxykinases is variable. Thus, the carboxykinases from Escherichia coli, Trypanosoma brucei, and Saccharomyces cerevisiae areExpand
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The role of alginate lyases in the enzymatic saccharification of brown macroalgae, Macrocystis pyrifera and Saccharina latissima
Abstract In this work, we have compared the carbohydrate content and the enzymatic saccharification of the brown algae Macrocystis pyrifera from Chile and Saccharina latissima from Norway. M .Expand
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Heterologous expression and biochemical characterization of a novel cold-active α-amylase from the Antarctic bacteria Pseudoalteromonas sp. 2-3.
α-Amylase is an endo-acting enzyme which catalyzes random hydrolysis of starch. These enzymes are used in various biotechnological processes including the textile, paper, food, biofuels, detergentsExpand
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Penicillium purpurogenum produces two GH family 43 enzymes with β-xylosidase activity, one monofunctional and the other bifunctional: Biochemical and structural analyses explain the difference.
β-Xylosidases participate in xylan biodegradation, liberating xylose from the non-reducing end of xylooligosaccharides. The fungus Penicillium purpurogenum secretes two enzymes with β-D-xylosidaseExpand
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Aqueous Extraction of the Sulfated Polysaccharide Ulvan from the Green Alga Ulva rigida—Kinetics and Modeling
The incentives for utilizing a versatile range of renewable feedstocks in novel ways are continuously increasing. Sulfated polysaccharides from green algae, such as ulvan, are interesting due to theExpand
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Α-L-arabinofuranosidase 3 from Penicillium purpurogenum (ABF3): potential application in the enhancement of wine flavour and heterologous expression of the enzyme.
An α-l-arabinofuranosidase (ABF3) from Penicillium purpurogenum was purified and its possible biotechnological application in the enhancement of wine flavour combined with P. purpurogenumExpand
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