cellulase/atrofija

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Degeneration of beta-glucosidase activity in a foam fractionation process.

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Prijava / prijava

Foam fractionation is a promising technique for concentrating proteins because of its simplicity and low operating cost. One such protein that can be foamed is the enzyme cellulase. The use of inexpensively purified cellulase may be a key step in the economical production of ethanol from biomass. We

Cloning and DNA sequence of the gene coding for Clostridium thermocellum cellulase Ss (CelS), a major cellulosome component.

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Clostridium thermocellum ATCC 27405 produces an extracellular cellulase system capable of hydrolyzing crystalline cellulose. The enzyme system involves a multicomponent protein aggregate (the cellulosome) with a total molecular weight in the millions, impeding mechanistic studies. However, two major

Cloning and characterization of two cellulase genes from Lentinula edodes.

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Lentinula edodes has traditionally been grown on fallen logs. It produces a wide array of enzymes to digest the lignocellulolytic substrate for nutrients. Thus, this organism represents a rich source of potentially potent lignocellulolytic enzymes that can be harnessed for conversion of biomass to

Pedicel breakstrength and cellulase gene expression during tomato flower abscission.

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Six cellulase genes were isolated from total RNA of the ethylene-treated tomato (Lycopersicon esculentum Mill.) flower abscission zone by reverse-transcription polymerase chain reaction using degenerate primers to conserved amino acid sequences from known plant cellulases. Four of the gene fragments

Preventing fungal growth on heritage paper with antifungal and cellulase inhibiting magnesium oxide nanoparticles.

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Microorganisms such as bacteria, fungi, algae and moulds are highly proficient at colonizing artistic and architectural heritage. The irreparable damage they cause to unique artefacts results in immeasurable cultural and societal losses to our shared cultural heritage, which represent an important

Effect of Cellulases and Xylanases on Refining Process and Kraft Pulp Properties.

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Samples of bleached kraft pine cellulosic pulp, either treated with an enzyme preparation (a Thermomyces lanuginosus xylanase, an Aspergillus sp. cellulase, and a multienzyme preparation NS-22086 containing both these activities) or untreated, were refined in a laboratory PFI mill. The treatment

Endogenous cellulase production in the leaf litter foraging mangrove crab Parasesarma erythodactyla.

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The sesarmid crab Parasesarma erythodactyla consumes large amounts of mangrove leaf litter but its biochemical capacity for cellulose digestion is poorly known. We demonstrate the presence of endo-β-1,4-glucanase, β-glucosidase and total cellulase activities in the digestive juice of this crab. The

The use of conserved cellulase family-specific sequences to clone cellulase homologue cDNAs from Fusarium oxysporum.

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Five cDNAs from the cellulolytic fungi Fusarium oxysporum that code for five distinct cellulase homologues have been cloned and sequenced. The cloning strategy exploited the hydrophobic cluster analysis-based cellulase family classification of Henrissat and Bairoch [Biochem. J. 293 (1993) 781-788]

Isolation of a cDNA encoding a putative cellulase in the red claw crayfish Cherax quadricarinatus.

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Amino acid sequences of cellulases have been determined in insects, nematodes, plants, slime moulds and bacteria but not in crustaceans. However, cellulase activity has been demonstrated in the hepatopancreas of the red claw crayfish, Cherax quadricarinatus. In order to obtain information on the

Purification, characterization, cDNA cloning and nucleotide sequencing of a cellulase from the yellow-spotted longicorn beetle, Psacothea hilaris.

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A cellulase (endo-beta-1,4-glucanase, EC 3.2.1.4) was purified from the gut of larvae of the yellow-spotted longicorn beetle Psacothea hilaris by acetone precipitation and elution from gels after native PAGE and SDS/PAGE with activity staining. The purified protein formed a single band, and the

Retrieval of glycoside hydrolase family 9 cellulase genes from environmental DNA by metagenomic gene specific multi-primer PCR.

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A new method, termed metagenomic gene specific multi-primer PCR (MGSM-PCR), is presented that uses multiple gene specific primers derived from an isolated gene from a constructed metagenomic library rather than degenerate primers designed based on a known enzyme family. The utility of MGSM-PCR was

[Cloning and expressing of cellulase gene (cbh2) from thermophilic fungi Chaetomium thermophilum CT2].

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Chaetomium thermophilum CT2 can produce extracellular cellulase with industrial value. We designed two degenerate primers to amplify catalytic domain sequence of cellobiohydrolase II ( CBH II). Full length of cDNA was obtained by rapid amplification of cDNA ends technologies. DNA sequencing revealed

Molecular cloning and characterization of two novel cellulase genes from the mollusc Ampullaria crossean.

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Cellulase genes have been reported not only from fungi, bacteria and plant, but also from some invertebrate animals. Here, two cellulase (endo-beta-1,4-glucanase, EC 3.2.1.4) genes, eg27I and eg27II, were cloned from the freshwater snail Ampullaria crossean cDNA using degenerate primers. The

Degree of Polymerization of Cellulose from Acetobacter xylinum BPR2001 Decreased by Cellulase Produced by the Strain.

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Acetobacter xylinum produces both cellulase and bacterial cellulose, but some report believed that this cellulase activity does not decrease the degree of polymerization (DP) of bacterial cellulose during cultivation. A. xylinum subsp. sucrofermentans BPR2001 produces two enzymes that hydrolyze

Differential involvement of β-glucosidases from Hypocrea jecorina in rapid induction of cellulase genes by cellulose and cellobiose.

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Appropriate perception of cellulose outside the cell by transforming it into an intracellular signal ensures the rapid production of cellulases by cellulolytic Hypocrea jecorina. The major extracellular β-glucosidase BglI (CEL3a) has been shown to contribute to the efficient induction of cellulase

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