• Journal of Plant Biology
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• v.32 no.4
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• pp.275-283
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• 1989

$\beta$-1, 4-endoglucanase (EC 3, 2, 1, 4) was isolated and purified from Nicotiana tabaccum L. Var. Virginia 115 suspensin cultured cells. The molecular weight as estimated by Sephadex G-100 was about 14, 000. The optimum pH for activity was 5.4. The Km value for carboxymethyl cellulose was 0.18 mg/unit and the enzyme was quite resistant to heating. Polyamine did not affect the activity of $\beta$-1, 4-endoglucanase in vitro but the activity increased drastically when polyamines were added in the suspension culture medium. It is suggested that increase in $\beta$-1, 4-endoglucenase activity due to polyamine might be related to growth of the plant.

• Microbiology and Biotechnology Letters
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• v.41 no.2
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• pp.145-152
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• 2013

The culture conditions to maximize the production of endoglucanase (EC 3.2.1.4) from the brown rot fungus Fomitopsis pinicola MKACC 54347 mycelia were investigated. Among the tested media for endoglucanase production, Mandel's mineral salts medium (MSM; 1% cellulose, 0.1% peptone, 0.14% $(NH_4)_2SO_4$, 0.03% urea, 0.2% $KH_2PO_4$, 0.03% $MgSO_4{\cdot}7H_2O$, 0.03% $CaCl_2$, and 0.1% trace metal solution (19.8 mM $FeSO_4$, 13.0 mM $MnSO_4$, 12.2 mM $ZnSO_4$, and 15.4 mM $CoCl_2$)) produced the highest activity of the enzyme. To optimize the medium composition for enzyme activity, the effects of various carbon, nitrogen, phosphorus, and inorganic sources were investigated in MSM. Maximal enzyme production was accomplished using a medium containing 2% carboxymethyl cellulose (CMC), 2% yeast extract, 0.2% $KH_2PO_4$, 0.03% $MnSO_4$, and 0.3% trace metal solution. Different physiological conditions, like incubation period and temperature, were also examined to assess their influence on enzyme production. Enzyme production from F. pinicola reached its highest level after cultivation for 8 days at $25^{\circ}C$. Nondenaturing polyacrylamide gel electrophoresis (PAGE), followed by the endoglucanase activity staining using CMC as the substrate, was performed to identify the endoglucanase under the culture conditions studied. Zymogram analysis of the culture supernatant revealed an endoglucanase band with a molecular mass of 52 kDa. The optimum pH and temperature for enzyme activity were $55^{\circ}C$ and pH 5.0, respectively.

• The Korean Journal of Soil Zoology
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• v.8 no.1_2
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• pp.7-12
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• 2003

Endogeneous endoglucanase (EC 3.2.1.4) cDNA was cloned from a representative species (Eisenia anderi) of the earthworm family Lumbricidae. Endoglucanase from the midgut of the earthworm is composed of 456 amino acids and belongs to glycosyl hydrolase family 9 (GHF9), sharing high homologies (50-51 %) with those of selected termite and crayfish. This endoglucanase consists of three consensus catalytic domains found in most microbial cellulases. A phylogenetic tree was constructed using the amino acid squence data matched through the BLASTX program and showed that GHF9 families could be divided into four groups of arthropoda, bacteria, plant and annelida.

• Korean Journal of Microbiology
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• v.36 no.1
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• pp.20-25
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• 2000

One of endoglucanases(F-II-II) was purified from the culture filtrate of Trichoderma sp. C-4 through two step procedures including chromatography on Sephacryl S-200 and Sephacryl S-100. The molecular weight of the enzyme was determined to be about 26,000 by SDS-PAGE and the isoelectric point as 8.0 by analytical isoelectric focusing. The optimum temperature of the enzyme was $50^{\circ}C$ and the optimum pH was 5.0. No loss of activity was observed when the enzyme was preincubated at $50^{\circ}C$ for 24 hours. The specific activity of the enzyme toward carboxymethylcellulose (CMC) was estimated to be 776.2 U/mg. The internal amino acid sequence was analysed.

• Proceedings of the Korean Society of Sericultural Science Conference
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• 2003.04a
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• pp.77-78
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• 2003

A novel -1, 4-endoglucanase (EGase, EC 3.2.1.4) cDNA belonging to glycoside hydrolase family (GHF) 45 was cloned from the mulberry longicorn beetle, Apriona germari. The cDNA encoding EGase of A. germari (Ag-EGase) is 711 base pairs long with an open reading frame of 237 amino acid residues. The deduced protein sequence of Ag-EGase showed 54% and 48% identity to phytophagous beetle Phaedon cochleariae and termite Reticulitermes speratus hindgut symbiont, respectively. (omitted)

• Journal of the Korea Organic Resources Recycling Association
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• v.15 no.3
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• pp.80-89
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• 2007

Two endogenous endo-${\beta}$-1,4-D-glucanase (EGase, EC 3.2.1.4) cDNAs were cloned from the midgut of the earthworm Eisenia anderi, and named EaEG2 and EaEG3, respectively. A sequence of 1,368 bp was determined and the coding region is composed of 456 amino acid residues including the initiation methionine. The N-terminal region of 20 residues in the deduced sequence was regarded as the signal peptide. These EGases belong to glycosyl hydrolase family 9 (GHF9) and showed high levels of identity(51-55%) with selected termite, cockroache, crayfish and mollusc EGases. The EGases of earthworm consist of three consensus catalytic domains found in most microbial cellulases. A phylogenetic tree was constructed using the deduced amino acid sequence data matched through the BLASTX program and showed that GHF9 families could be divided into five groups of arthropoda, bacteria, plant, annelida and mollusc.