• Proceedings of the Zoological Society Korea Conference
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• 1994.10a
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• pp.208.2-208
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• 1994

No Abstract, See Full Text

• The Plant Pathology Journal
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• v.21 no.3
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• pp.195-206
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• 2005

Spatial and temporal expression of pathogenesis-related (PR) gene and proteins has been recognized as inducible defense response in pepper plants. Gene expression and/or protein accumulation of PR-1, $\beta-1,3-glucanase$ and chitinase was predominantly found in pepper plants during the inoculations by Xanthomonas campestris pv. vesicatoria, Phytophthora capsici and Colletotrichum coccodes. PR-1 and chitinase genes were also induced in pepper plants in response to environmental stresses, such as high salinity and drought. PR-1 and chitinase gene expressions by biotic and abiotic stresses were regulated by their own promoter regions containing several stress-related cis-acting elements. Overexpression of pepper PR-1 or chitinase genes in heterogeneous transgenic plants showed enhanced disease resistance as well as environmental stress tolerances. In this review, we focused on the putative function of pepper PR-1, $\beta-1,3-glucanase$ and chitinase proteins and/or genes at the biochemical, molecular and cytological aspects.

• Journal of Microbiology and Biotechnology
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• v.27 no.2
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• pp.271-276
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• 2017

A highly thermostable ${\beta}-(1-4)-glucanase$ (NA23_08975) gene (fig) from Fervidobacterium islandicum AW-1, a native-feather degrading thermophilic eubacterium, was cloned and expressed in Escherichia coli. The recombinant FiG (rFiG) protein showed strong activity toward ${\beta}-{\small{D}}-glucan$ from barley (367.0 IU/mg), galactomannan (174.0 IU/mg), and 4-nitrophenyl-cellobioside (66.1 IU/mg), but relatively weak activity was observed with hydroxyethyl cellulose (5.3 IU/mg), carboxymethyl cellulose (2.4 IU/mg), and xylan from oat spelt (1.4 IU/mg). rFiG exhibited optimal activity at $90^{\circ}C$ and pH 5.0. In addition, this enzyme was extremely thermostable, showing a half-life of 113 h at $85^{\circ}C$. These results indicate that rFiG could be used for hydrolysis of cellulosic and hemicellulosic biomass substrates for biofuel production.

• 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

• Proceedings of the Zoological Society Korea Conference
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• 1995.10b
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• pp.96-98
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• 1995

No Abstract, See Full Text

• Asian-Australasian Journal of Animal Sciences
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• v.26 no.2
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• pp.253-259
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• 2013

Paddy rice is rarely used as a feed because of its high fiber content. In this study, two experiments were conducted to study the effects of supplementing an enzyme complex consisting of xylanase, beta-glucanase and cellulase, to paddy-based diets on the performance and nutrient digestibility in meat-type ducks. In the both experiments, meat-type ducks (Cherry Valley) were randomly assigned to four treatments. Treatment 1 was a basal diet of corn-soybean; treatment 2 was a basal diet of corn-paddy-soybean; treatment 3, had enzyme complex added to the corn-paddy-soybean basal diet at levels of 0.5 g/kg diet; and treatment 4, had enzyme complex added to the corn-paddy-soybean diet at levels of 1.0 g/kg diet. The results showed that the enzyme complex increased the ADG, and decreased the ADFI and F/G significantly (p<0.05) in the ducks, and the ADFI for the ducks fed the corn-paddy-soybean diet showed no difference compared to the ducks fed corn-soybean diets at all stages of the experiment (p<0.05). When corn was partially replaced by paddy, the digestibility of CP and NDF was decreased and increased, respectively (p<0.05), and the level of enzyme complex had a significant effect on both CP and NDF digestibility (p<0.05). As for the AME, addition of enzyme complex increased it significantly (p<0.05), but both diet types and levels of enzyme complex had no effect (p>0.05). The outcome of this research indicates that the application of enzyme complex made up of xylanase, beta-glucanase, and cellulase, in the corn-paddy-soybean diet, can improve performance and nutrition digestibility in meat-type ducks.

• Journal of Life Science
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• v.11 no.5
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• pp.423-431
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• 2001

Genomic and cDNA clones containing the RAT3 gene involving in Agobacterium-mediated plant transformation were identified using plant DNA flanking the righ border of a T-DNA rescued from the rat3 mutant as hy-bridization probe. Two highly homologous cDNA clones were identified; one (RAT3-1) weakly hybridized with the probe whereas another (RAT3-2) strongly hybridized with the probe. Both Rat3-1 and Rat3-2 proteins contain a putative signal peptide for secretion. The deduced molecular weights of encoded proteins are 15 kDa. The results of genomic DNA blot analysis and DNA sequencing indicated that RAT3-1 and RAT3-2 exist as single copy genes and they were arranged side by side with just 600 bp distance between them. RAT3-1 was disrupted by the integration of T-DNA into the 3 untranslated region in rat3 mutant. A BLAST search showed that both RAT3-1 and RAT3-2 proteins have homology with only the C-terminal region of $\beta$-1,3-glucanase homologues from Triticum aestivum and Arabidopsis thaliana. Thses $\beta$-1,3-glucanase homologues contain an unusually long C-terminal region with no sig-nificant homology to other $\beta$-1,3-glucanase.

• Korean Journal of Microbiology
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• v.30 no.5
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• pp.403-409
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• 1992

For the development of a glucanolytic yeast strain. the seceretion of endo-1.4-$\beta$-D-glucanase (CMCase) of Bacillus subtilis was performed in yeast using glucoamylase gene (STA1) of Saccharomyces diastaticus. A 1.7 kb-DNA fragment of STA1 gene containing authentic promoter, signal sequence, threonine serine-rich (TS) region and N-terminal region (98 amino acids) of mature glucoamylase was ligated to YEp 24. E. coli-yeast shuttle vector. And then. CMCase structural gene of B. subtilis was fused in frame with the 1.7 kb-DNA fragment of STA1 gene, resulting in recombinant plasmid pYES('24. Yeast transformant harboring pYESC24 had no CMCase activity. So. we deleted TS region and N-terminal region of mature glucoamylase existing between signal sequence and CMCase structural gene in pYESC24. consequently constructed recombinant plasmid pYESC11. The yeast transformed with the newly constructed recombinant plasmid pYESC11 efficiently secreted CMCase to extracellular medium. After 4 days culture. total CMCase activity of this transformant was 44.7 units/ml and over 93% of total CMCase activity was detected in culture supernatant.

• Journal of Microbiology and Biotechnology
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• v.22 no.10
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• pp.1359-1366
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• 2012

A strain of Streptomyces cavourensis subsp. cavourensis (coded as SY224) antagonistic to Colletotrichum gloeosporioides infecting pepper plants was isolated. SY224 produced lytic enzymes such as chitinase, ${\beta}$-1,3-glucanase, lipase, and protease in respective assays. To examine for antifungal activity, the treatments amended with the nonsterilized supernatant resulted in the highest growth inhibition rate of about 92.9% and 87.4% at concentrations of 30% and 10%, respectively. However, the sterilized treatments (autoclaved or chloroform treated) gave a lowered but significant inhibitory effect of about 63.4% and 62.6% for the 10% supernatant concentration, and 75.2% and 74.8% for the of 30% supernatant concentration in the PDA agar medium, respectively, indicative of the role of a non-protein, heat stable compound on the overall effect. This antifungal compound, which inhibited spore germination and altered hyphal morphology, was extracted by EtOAc and purified by ODS, silica gel, Sephadex LH-20 column, and HPLC, where an active fraction was confirmed to be 2-furancarboxaldehyde by GS-CI MS techniques. These results suggested that SY224 had a high potential in the biocontrol of anthracnose in pepper, mainly due to a combined effect of lytic enzymes and a non-protein, heat-stable antifungal compound, 2-furancarboxaldehyde.

• Journal of Microbiology and Biotechnology
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• v.28 no.12
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• pp.2036-2045
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• 2018

An endo-${\beta}$-1,4-glucanase gene, cel5L, was cloned using the shot-gun method from Bacillus sp.. The gene, which contained a predicted signal peptide, encoded a protein of 496 amino acid residues, and the molecular mass of the mature Cel5L was estimated to be 51.8 kDa. Cel5L contained a catalytic domain of glycoside hydrolase (GH) family 5 and a carbohydrate-binding module family 3 (CBM_3). Chromatography using HiTrap Q and CHT-II resulted in the isolation of two truncated forms corresponding to 50 (Cel5L-p50) and 35 kDa (Cel5L-p35, CBM_3-deleted form). Both enzymes were optimally active at pH 4.5 and $55^{\circ}C$, but had different half-lives of 4.0 and 22.8 min, respectively, at $70^{\circ}C$. The relative activities of Cel5L-p50 and Cel5L-p35 for barley ${\beta}$-glucan were 377.0 and 246.7%, respectively, compared to those for carboxymethyl-cellulose. The affinity and hydrolysis rate of pNPC by Cel5L-p35 were 1.7 and 3.3 times higher, respectively, than those by Cel5L-p50. Additions of each to a commercial enzyme set increased saccharification of pretreated rice straw powder by 17.5 and 21.0%, respectively. These results suggest CBM_3 is significantly contributing to thermostability, and to affinity and substrate specificity for small substrates, and that these two enzymes could be used as additives to enhance enzymatic saccharification.