Results 231 to 240 of about 54,625 (263)
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1988
Publisher Summary Streptomyces can produce inductively extracellular xylanase in the presence of xylan, but cannot secrete β-xylosidase into medium. When the xylanase acts on xylan, mainly xylose and xylobiose are accumulated in the hydrolyzate. Streptomyces can produce inductively the xylanase in response to nonmetabolizable β-xylosides.
Tuneo Yasui +3 more
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Publisher Summary Streptomyces can produce inductively extracellular xylanase in the presence of xylan, but cannot secrete β-xylosidase into medium. When the xylanase acts on xylan, mainly xylose and xylobiose are accumulated in the hydrolyzate. Streptomyces can produce inductively the xylanase in response to nonmetabolizable β-xylosides.
Tuneo Yasui +3 more
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Studies on xylanase fromBasidiomycetes
Folia Microbiologica, 1975Formation of extracellular xylanase was studied in 10 strains of wood-destroying fungi belonging to Basidiomycetes during their submerged cultivation with willow sawdust. The highest enzyme activity was found in the fungus Trametes hirsuta (Wulf.) Pilát.
M, Kubacková +2 more
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Biochemical Characterization of a GH11 Xylanase from Xylanase-Producing Trichoderma citrinoviride
Applied Biochemistry and BiotechnologyXylan, a prevalent component of lignocellulose, ranks as the second most abundant carbohydrate in nature. Endo-1,4-xylanase, pivotal for its ability to cleave β-1,4-glycosidic linkages within xylan, is crucial for various applications in the food/feed processing, biofuel production, and paper/pulp industries.
Beom Soo, Kim +4 more
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Protein Expression and Purification, 2019
The ricexip gene, which encodes the rice xylanase-inhibiting protein (riceXIP), was recombinantly expressed in Pichia pastoris GS115 under the control of AOX1 promoter. Recombinant riceXIP (rePriceXIP) was secreted into the supernatant and purified to homogeneity with the use of Ni-affinity resin. The molecular mass of rePriceXIP was approximately 44.0
Yahui, Dang, Mingqi, Liu, Xiaoqian, Wu
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The ricexip gene, which encodes the rice xylanase-inhibiting protein (riceXIP), was recombinantly expressed in Pichia pastoris GS115 under the control of AOX1 promoter. Recombinant riceXIP (rePriceXIP) was secreted into the supernatant and purified to homogeneity with the use of Ni-affinity resin. The molecular mass of rePriceXIP was approximately 44.0
Yahui, Dang, Mingqi, Liu, Xiaoqian, Wu
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Xylanases: Structure and Function
1981A number of papers in this seminar are devoted to the production and characterization of cellulases. This is proper, since the use of cellulases is perhaps the most feasible method of converting cellulose to products that may be used for fuels and chemicals.
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Thermostable Bacterial Xylanases
2013Hemicellulose is the second most abundant component in lignocellulosics available in nature. It is a storage polymer occurring in seeds and a prominent structural component of cell walls in plants. Hemicelluloses in agricultural residues constitute up to 40%.
Vikash Kumar +3 more
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Biochemical and Biophysical Research Communications, 1999
A 1.0 kilobase gene fragment from the genomic DNA of an alkaliphilic thermophilic Bacillus was found to code for a functional xylanase (XynII). The complete nucleotide sequence including the structural gene and the 5' and 3' flanking sequences of the xylanase gene have been determined.
N, Kulkarni, M, Lakshmikumaran, M, Rao
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A 1.0 kilobase gene fragment from the genomic DNA of an alkaliphilic thermophilic Bacillus was found to code for a functional xylanase (XynII). The complete nucleotide sequence including the structural gene and the 5' and 3' flanking sequences of the xylanase gene have been determined.
N, Kulkarni, M, Lakshmikumaran, M, Rao
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Use of Psychrophilic Xylanases Provides Insight into the Xylanase Functionality in Bread Making
Journal of Agricultural and Food Chemistry, 2011The bread-improving potential of three psychrophilic xylanases from Pseudoalteromonas haloplanktis TAH3A (XPH), Flavobacterium sp. MSY-2 (rXFH), and unknown bacterial origin (rXyn8) was compared to that of the mesophilic xylanases from Bacillus subtilis (XBS) and Aspergillus aculeatus (XAA).
Emmie, Dornez +4 more
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Proteinaceous inhibitors of microbial xylanases
Biochemistry (Moscow), 2010At the end of 1990s two structurally different proteinaceous inhibitors of xylanases were discovered in the grain of wheat (Triticum aestivum). They were named TAXI (T. aestivum xylanase inhibitor) and XIP (xylanase-inhibiting protein). Later it was shown that TAXI and XIP in wheat are present in several isoforms encoded by different genes.
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