a chimeric xylanase/endoglucanase with an internal cellulase-binding domain by fusing the Bacillus subtilis xyn gene fragment to the 5'-end of the Cellulomonas fimi cenA, overexpression in Escherichia coli
by removing some of the C-terminal sequence of the ORF of the endoglucanase (PH1171), two types of recombinant proteins are expressed from one ORF, using Escherichia coli
Cel6A production in Escherichia coli and the DB-Cel6A fusions are inserted by particle bombardment method into the tobacco (Nicotiana tabacum cv. Samsun) chloroplast genome for protein expression
CenA, DNA and amino acid sequence determination and analysis, expression of wild-type and mutant enzymes in Escherichia coli strain BL21(DE3), subcloning in Escherichia coli strain DH5alpha
cloned from camel rumen metagenom, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3), subcloning in Escherichia coli strain DH5alpha
DNA and amino acid sequence determination and analysis, sequence comparison and phylogenetic analysis, recombinant expression in Escherichia coli BL21 (DE3) and Rosetta cells
endoglucanase IV is reconstructed by fusing EGIV with an additional catalytic module (EGIVCM). The genes eg4 and eg4-cm are expressed in recombinant Pichia strains (Pichia pastoris EGIV1 and Pichia pastoris EGIV-CM1)
expressed cytosolically under control of the cauliflower mosaic virus 35S promoter in transgenic duckweed, Lemna minor 8627 without any obvious observable phenotypic effects on morphology or rate of growth. The duckweed-expressed enzyme is biologically active and the expression level is up to 0.24% of total soluble protein
expression of chimeric enzymes in Escherichia coli. The proteins are produced in high yields in but aggregated in inclusion bodies.The fusion protein SSO1949-CelA-SSO1949, that consists of 193 amino acids SSO1949 followed by 76 amino acids CelA and 39 amino acids SSO1949, is inactive with the substrate N-[2-N-[(S-(4-deoxy-4-dimethylamino-phenylazophenylthioureido-beta-D-glucopyranosyl)-(1->4)-beta-D-glucopyranosyl-(1->4)-beta-D-glucopyranosyl-(1->4)-beta-D-glucopyranosyl-(1->4)-beta-D-glucopyranosyl-(1->4)-beta-D-glucopyranosyl)-2-thioacetyl]aminoethyl]-1-naphthylamine-5-sulfonate. The fusion protein CelA-SSO1949-CelA, that consists of 70 amino acids CelA followed by 163 amino acids SSO1949 and 29 amino acids CelA, shows activity with the substrate N-[2-N-[(S-(4-deoxy-4-dimethylamino-phenylazophenylthioureido-beta-D-glucopyranosyl)-(1->4)-beta-D-glucopyranosyl-(1->4)-beta-D-glucopyranosyl-(1->4)-beta-D-glucopyranosyl-(1->4)-beta-D-glucopyranosyl-(1->4)-beta-D-glucopyranosyl)-2-thioacetyl]aminoethyl]-1-naphthylamine-5-sulfonate that is comparable to the native enzyme from Sulfolobus and shows a temperature optimum of approximately 85°C and a pH optimum of approximately pH 3 thus retaining the advantageous properties of the Sulfolobus parent enzyme
expression of chimeric enzymes in Escherichia coli. The proteins are produced in high yields in but aggregated in inclusion bodies.The fusion protein SSO1949-CelA-SSO1949, that consists of 193 amino acids SSO1949 followed by 76 amino acids CelA and 39 amino acids SSO1949, is inactive with the substrate N-[2-N-[(S-(4-deoxy-4-dimethylamino-phenylazophenylthioureido-beta-D-glucopyranosyl)-(1->4)-beta-D-glucopyranosyl-(1->4)-beta-D-glucopyranosyl-(1->4)-beta-D-glucopyranosyl-(1->4)-beta-D-glucopyranosyl-(1->4)-beta-D-glucopyranosyl)-2-thioacetyl]aminoethyl]-1-naphthylamine-5-sulphonate. The fusion protein CelA-SSO1949-CelA, that consists of 70 amino acids CelA followed by 163 amino acids SSO1949 and 29 amino acids CelA, shows activity with the substrate N-[2-N-[(S-(4-deoxy-4-dimethylamino-phenylazophenylthioureido-beta-D-glucopyranosyl)-(1->4)-beta-D-glucopyranosyl-(1->4)-beta-D-glucopyranosyl-(1->4)-beta-D-glucopyranosyl-(1->4)-beta-D-glucopyranosyl-(1->4)-beta-D-glucopyranosyl)-2-thioacetyl]aminoethyl]-1-naphthylamine-5-sulphonate that is comparable to the native enzyme from Sulfolobus and shows a temperature optimum of approximately 85°C and a pH optimum of approximately pH 3 thus retaining the advantageous properties of the Sulfolobus parent enzyme
expression of the fusion enzyme (EG-M-Xyn) of endoglucanase (cellulase) from Teleogryllus emma and xylanase from Thermomyces lanuginosus in Yarrowialipolytica
gene 168cel5 or eglS, recombinant expression of the enzyme, in an expression construct comprising DNA sequences encoding P43 promoter, signal peptide of Bacillus subtilis nprB, and mature Bacillus subtilis strain 168 Cel5 residues 30-499, in Paenibacillus sp. strain CAA11
gene bp_cel9A, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21
gene cel9 or celA, DNA and amino acid sequence determination and analysis, phylogenetic analysis, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3)
gene Celf_1230, DNA and amino acid sequence determination and analysis, sequence comparisons, codon-optimized, recombinant expression of N-terminally His-tagged enzyme in Escherichia coli
gene celI15, DNA and amino acid sequence determination and analysis, functional expression in Escherichia coli strain BL21(DE3) as extracellular enzyme, subcloning in Escherichia coli strain JM109
gene ctendo7, DNA and amino acid sequence determination and analysis, sequence comparisons, recombinant expression of C-terminally His6-tagged enzyme in Pichia pastoris strain GS115
gene eg1, recombinant expression in Pichia pastoris strains GS115 and X33, enzyme EG1 folding and secretion efficiency from the endoplasmic reticulum is best enhanced by co-overexpression of chaperone HAC1 in the host strain GS115 harboring eight EG1 copies, subcloning in Escherichia coli strain TOP10, quantitative PCR expression analysis, method evaluation and optimization for high enzyme production
gene Fpcel45a, DNA and amino acid sequence determination and analysis, phylogenetic tree of fungal proteins belonging to GH family 45, recombinant expression of His-tagged enzyme in Pichia pastoris strain GS115
gene ge40, DNA and amino acid sequence determination and analysis, sequence comparisons, genetic structure of the cloning construct, cloning with a signal peptide sequence derived from the endoxylanse (EC 3.2.1.8) encoding gene GtxynA1 from Geobacillus thermodenitrificans strain T12, overview. Recombinant expression of the enzyme in Escherichia coli strain BL21(DE3) (under control of the lac operator) and in Geobacillus thermodenitrificans strain T12
gene nmGH45, cloned from saline-alkaline lake soil microbial metagenomic DNA, DNA and amino acid sequence determination and analysis, sequence comparisons, recombinant expression in Pichia pastoris strain GS115, co-expression of molecular chaperone BIP enhances enzyme protein secretion by 20%, but chaperones PDI and HAC1 have limited influences
gene vul_cel5A, DNA and amino acid sequence determination and analysis, sequence comparisons, recombinant expression of His-tagged enzyme in Escherichia coli strain C43
heterologous expression in Talaromyces cellulolyticus under the control of a glucoamylase promoter of Talaromyces cellulolyticus. The characteristics of the enzyme are almost same as those prepared by Escherichia coli
hybrid cellulase with the Thermomonospora fusca E2 cellulose-binding domain at its C terminus joined to the Prevotella ruminicola 40500 Da carboxymethylcellulase, expression in Escherichia coli
overexpressed in a tropical Leguminosae tree, sengon (Paraserianthes falcataria), by the Agrobacterium tumefaciens method, increases the length and width of stems with larger leaves, which shows a moderately higher density of green color than leaves of the wild type. The pairs of leaves on the transgenic plants close more slowly during sunset than those on the wild-type plants. When main veins from each genotype are excised and placed on a paper towel, however, the leaves of the transgenic plants close more rapidly than those of the wildtype plant. Based on carbohydrate analyses of cell walls, the leaves of the transgenic plants contain less wall-bound xyloglucan than those of the wild-type plants. In situ xyloglucan endotransglucosylase activity shows that the incorporation of whole xyloglucan, potentially for wall tightening, occurrs in the parenchyma cells (motor cells) of the petiolule pulvinus attached to the main vein, although the transgenic plant incorporates less whole xyloglucan than the wild type plant. These observations support the hypothesis that the paracrystalline sites of cellulose microfibrils are attacked by poplar cellulase, which loosens xyloglucan intercalation, resulting in an irreversible wall modification. This process could be the reason why the overexpression of poplar cellulase both promotes plant growth and disturbs the biological clock of the plant by altering the closing movements of the leaves of the plant
recombinant expression of FnCel5A in Escherichia coli strain BL21, method evaluation and optimization for overproduction and up-scaling to be used in production of bioethanol and biofuel
selenomethionine-substituted CMCax is overexpressed in Escherichia coli B834 Codon Plus (DE3)-IRL (Stratagene) with a (His)6-tag at the N-terminus in place of the signal peptide
sequence comparisons, design and production of a chimeric enzyme library, recombinant expression of wild-type and mutant enzymes in Pichia pastoris strain GS115
shorter version mutants exhibiting activity at 80°C are expressed in Escherichia coli with a C-terminal His6 tag to facilitate purification using immobilized-metal affinity chromatography. Both the wild type and the deletion mutants are highly expressed in Escherichia coli after IPTG induction
The gene encoding for the thermoactive endoglucanase is derived from a metagenomic gene library based on a mixed culture grown anaerobically on cellulose at 70 C and pH 7. The recombinant endoglucanase is actively expressed in Escherichia coli TunerTM(DE3)pLacI by induction with 1 mM IPTG.
truncated mutants are constructed by deleting five residues from C-termini of endoglucanase catalytic domain. The truncated gene is inserted into the expression vector pET11a (Novagen, Madison, WI). The constructed plasmids are introduced into Escherichia coli strain BL21(DE3)
heterologous expression in Talaromyces cellulolyticus under the control of a glucoamylase promoter of Talaromyces cellulolyticus. The characteristics of the enzyme are almost same as those prepared by Escherichia coli
heterologous expression in Talaromyces cellulolyticus under the control of a glucoamylase promoter of Talaromyces cellulolyticus. The characteristics of the enzyme are almost same as those prepared by Escherichia coli
sequence comparisons, design and production of a chimeric enzyme library, recombinant expression of wild-type and mutant enzymes in Pichia pastoris strain GS115
sequence comparisons, design and production of a chimeric enzyme library, recombinant expression of wild-type and mutant enzymes in Pichia pastoris strain GS115
3.2.1.4 cellulase
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