• Korean Journal of Soil Science and Fertilizer
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• v.21 no.2
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• pp.129-134
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• 1988

Enzymatical properties of Streptomyces sp. S-45 producing chitinase and ${\beta}$-1.3-glucanase isolated from soil were investigated. Chitinase activity was 3.01(U/ml) and ${\beta}$-1.3-glucanase activity was 2.49(U/ml). The optimum medium for mycolytic enzyme production of strain was composed of 0.7% colloidal chitin, 0.3% glucose, 0.5% asparagine, 0.2% peptone, 0.01% NaCl, 0.01% $K_2HPO_4$ and 0.01% $MgSO_4{\cdot}7H_2O$ in intial pH 7.0. The optimal condition for mycolytic enzyme activities were: pH 6.5-7.0, $45-50^{\circ}C$. Enzyme activities were activated by metal ion as $10^{-2}M\;Co^{{+}{+}}$, $Cu^{{+}{+}}$, $Mn^{{+}{+}}$, $Al^{{+}{+}{+}}$ and $10^{-3}M\;Sn^{{+}{+}}$ but $Ag^{{+}{+}}$, $Hg^{{+}{+}}$ inhibited.

• 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.

• The Microorganisms and Industry
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• v.11 no.1
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• pp.21-33
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• 1985

이글은 다음과 같이 구성되어져 있다. preface 1) introduction 2) general information 3) folin protein determination 4) cellobiase assay 5) filter paper assay for saccharifying cellulase 6) carboxymethyl cellulase assay for endo-.betha.-1,4-glucanase 7) additional assay procedure for endoglucanase 8) evalutaiton of cellulase under process conditions 9) general remartks, references.

• Proceedings of the Korean Society of Life Science Conference
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• 2002.03a
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• pp.24-25
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• 2002

• Journal of Microbiology and Biotechnology
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• v.24 no.12
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• pp.1699-1706
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• 2014

A lichenase gene (mt-lic) was identified for the first time through function-based screening of a soil metagenomic library. Its deduced amino acid sequence exhibited a high degree of homology with endo-${\beta}$-1,3-1,4-glucanase (having both lichenase and chitosanase activities), encoded by the bgc gene of Bacillus circulans WL-12. The recombinant lichenase overexpressed and purified from Escherichia coli was able to efficiently hydrolyze both barley ${\beta}$-glucan and lichenan. The enzyme showed maximal activity at a pH of 6.0 at $50^{\circ}C$, with Azo-barley-glucan as the substrate. The metal ions $Mn^{2+}$, $Mg^{2+}$, $Ca^{2+}$, and $Fe^{2+}$ enhanced the enzymatic activity, whereas the $Cu^{2+}$ and $Zn^{2+}$ ions inhibited the enzymatic activity. The $K_m$ and $V_{max}$ values of the purified lichenase were determined to be 0.45 mg/ml and 24.83 U/min/mg of protein, respectively.

• Journal of Korea Technical Association of The Pulp and Paper Industry
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• v.47 no.6
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• pp.57-65
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• 2015

Microfibrillated cellulose (MFC) or Nanofibrillated cellulose (NFC) has been used to reduce the use of raw pulp and to improve paper strength. The problem of MFC preparation is high manufacturing cost. In this study, it was carried out to prepare MFC after enzyme beating and estimated properties of MFC. Endo-D was the best beating efficiency among three type of endo-glucanase. As the grinder pass number increased, the viscosity and the fines of MFC suspension increased while the crystallinity and the porosity of MFC sheet decreased. Also enzyme beating MFC was higher value in the crystallinity and lower value in the viscosity than non-enzyme MFC. In addition, the aspect ratio of MFC was the highest at 5 pass. MFC addition improved the handsheet strength and the air permeability but worsened the drainage.

• Microbiology and Biotechnology Letters
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• v.28 no.4
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• pp.195-201
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• 2000

Glucoamylase of Saccharomyces diastaticus is produced as a large precursor composed of signal peptide (21 amino acid residues), Thr and Ser-rich region and functional glucoamylase. To evaluate the utility of the glucoamylase signal peptide (GSP) for the secretion of foreign proteins, four types of GSP mutants (ml : Pro-18 longrightarrowLeu-18, m2 : Tyr-13 longrightarrowLeu, m3 : Ser-9longrightarrowLeu-9, m4 : Asn-5 longrightarrowPro-5) were constructed and secretion efficiency of each mutant was compared with that of native GSP by the expression and secretion of Bacillus subtilis CMCase under the control of GAP in N-terminal domain and hydrophobic domain. n mutant 4, a polar amino acid was replaced by a helix - breaking Pro residue. CMCase activity assay and Western blot analysis revealed that CMCase secretion by GSP mutants replaced by Leu were increased compared with native GSP. In the case of m2 and m3, the substitution of Leu for Tyr-13 and Ser-9 in the hydrophobic region resulted in a twofold increase in the extracellular CMCase activity.

• Korean Journal of Environmental Biology
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• v.35 no.4
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• pp.648-653
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• 2017

The aim of this study was to select various fungal strains indigenous to Korea that have the potential to produce cellulases, including filter paper activity (FPase), $endo-{\beta}$-1,4-glucanase (EG), and ${\beta}-glucosidase$ (BGL). Among the 25 species of Ascomycetes and the 32 species of Basidiomycetes tested in this study, the Bjerkandera adusta KUC10565, Heterobasidion orientale KUC10556, Hyphoderma praetermissum KUC10609, and Trichoderma harzianum KUC1716 all exhibited remarkably high FPase activity. In addition, the T. harzianum KUC1716 showed high levels of EG and BGL activity. This strain has been selected for further study because of their enzymatic potential.

• Journal of Applied Biological Chemistry
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• v.62 no.3
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• pp.293-297
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• 2019

Leaf rust is the most widespread and destructive fungal disease, and outbreaks have always caused considerable losses in wheat yields. Thus, worldwide increases in wheat production depend on the development of leaf rust-resistant wheat varieties. In this study, we evaluated the resistance of forty Korean wheat cultivars to leaf rust at the seedling stage. Only two Korean wheats, Ol and Jonong, were resistant to leaf rust, whereas the remaining thirty-eight Korean wheats were susceptible to leaf rust. The Ol and Jonong varieties presented larger dry seed weights and higher antioxidant activity in response to leaf rust than the susceptible wheat varieties. No differences in ${\beta}$-1,3-glucanase activity or chlorophyll content between resistant and susceptible wheat varieties were observed. Overall, these results are important for the development of wheat varieties that are highly resistant to leaf rust and to understand the underlying mechanisms that confer leaf rust resistance.

• Journal of Microbiology and Biotechnology
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• v.28 no.4
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• pp.588-596
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• 2018

An endo-${\beta}$-1,4-glucanase gene, cel9K, was cloned using the shot-gun method from Paenibacillus sp. X4, which was isolated from alpine soil. The gene was 2,994 bp in length, encoding a protein of 997 amino acid residues with a predicted signal peptide composed of 32 amino acid residues. Cel9K was a multimodular enzyme, and the molecular mass and theoretical pI of the mature Cel9K were 103.5 kDa and 4.81, respectively. Cel9K contains the GGxxDAGD, PHHR, GAxxGG, YxDDI, and EVxxDYN motifs found in most glycoside hydrolase family 9 (GH9) members. The protein sequence showed the highest similarity (88%) with the cellulase of Bacillus sp. BP23 in comparison with the enzymes with reported properties. The enzyme was purified by chromatography using HiTrap Q, CHT-II, and HiTrap Butyl HP. Using SDS-PAGE/activity staining, the molecular mass of Cel9K was estimated to be 93 kDa, which is a truncated form produced by the proteolytic cleavage of its C-terminus. Cel9K was optimally active at pH 5.5 and $50^{\circ}C$ and showed a half-life of 59.2 min at $50^{\circ}C$. The CMCase activity was increased to more than 150% in the presence of 2 mM $Na^+$, $K^+$, and $Ba^{2+}$, but decreased significantly to less than 50% by $Mn^{2+}$ and $Co^{2+}$. The addition of Cel9K to a commercial enzyme set (Celluclast 1.5L + Novozym 188) increased the saccharification of the pretreated reed and rice straw powders by 30.4% and 15.9%, respectively. The results suggest that Cel9K can be used to enhance the enzymatic conversion of lignocellulosic biomass to reducing sugars as an additive.