• KSBB Journal
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• v.14 no.1
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• pp.24-30
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• 1999

The fed-bach simultaneous saccharification and fermentation (SSF) of newspaper to ethanol with Brettanomyces custersii was studied. The initial substrate concentration for the effective fed-batch SSF was 8% (w/v). The initial optimum enzyme concentration was 30 FPU/g cellulose for cellulase and the optimum volumetric ratio of $\beta$-glucosidase to cellulase was 0.1. When 4% (w/v) of ball-milled newspaper was supplemented intermittently at time intervals, considering the mixing of newspaper slurry, the fed-batch SSF showed higher ethanol concentration (26.80 g/L) and two times higher ethanol production yield based on enzyme than the batch SSF.

• Asian-Australasian Journal of Animal Sciences
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• v.15 no.10
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• pp.1398-1402
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• 2002

Hu sheep was sampled randomly from Huzhou city, Zhejiang province, China. Of the 11 genetic markers from the blood examined by starch-gel and cellulose acetate electrophoresis, polymorphisms in Hu sheep were found for 10 loci, i.e. post-albumin (Po), transferring (Tf), alkaline phosphatase (Alp), leucine aminopeptidase (Lap), arylesterase (Ary-Es), hemoglobin-$\beta$ (Hb-$\beta$)、Xprotein(X-p), carbonic anhydrase (CA), catalase (Cat) and lysine (Ly). The same data except for Po locus were collected from another 14 sheep breeds from China and other countries, in order to ascertain their genetic relationships with one another and with the Hu sheep. The sheep populations from the east and south of Central Asia can be classified into three genetic groups: 'Mongolian sheep', 'South Asian sheep' and 'European sheep'. The Hu sheep belong to the 'Mongolian sheep' group.

• Journal of Plant Biology
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• v.38 no.3
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• pp.251-258
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• 1995

The soluble acid invertase ($\beta$-D-fructofuranoside fructohydrolase, EC 3.2.1.26) was isolated and characterized from the hypocotyls of mung bean (Phaseolus radiatus L.). The enzyme was purified to apparent homogeneity by consecutive step using diethylaminoethyl (DEAE)-cellulose anion exchange, Concanavalin (Con) A affinity and Sephacryl S-300 chromatography. The overall purification was about 148-fold with a yield of about 15%. The finally purified enzyme exhibited a specific activity of about 139 $\mu$mol of glucose produced mg-1 protein min-1 at pH 5.0 and appeared to be a single protein by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and nondenaturing PAGE. The enzyme had the native molecular weight of 70 kD and subunit molecular weight of 70 kD as estimated by Sephadex G-200 chromatography and SDS-PAGE, respectively, suggesting that the enzyme was composed of a monomeric protein. On the other hand, the enzyme appeared to be a glycoprotein containing N-linked high mannose oligosaccharide chain on the basis of its ability to bind to the immobilized C on A. The enzyme had a Km for sucrose of 1.8 mM at pH 5.0 and maximum activity around pH 5.0. The enzyme showed highest enzyme activity with sucrose as substrate, but the activity was slightly measured with raffinose and cellobise. No activity was measured with maltose and lactose. These results indicate the soluble acid invertase is a $\beta$-fructofuranosidase.

• Journal of Plant Biology
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• v.38 no.4
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• pp.349-357
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• 1995

The alkaline invertase ($\beta$-D-fructofuranoside fructohydrolase, EC 3.2.1.26) was isolated and characterized from the hypocotyls of mung bean (Phaseolus radiatus L.). The enzyme was purified by consecutive step using diethylaminoethyl (DEAE)-cellulose anion exchange, 1st Sephadex G-200, DEAE-Sephadex A50 and 2nd Sephadex G-200 chromatography. The overall purification was about 77-fold with a yield of about 6%. The finally purified enzyme exhibited a specific activity of about 48 $\mu$mol of glucose produced mg-1 protein min-1 at pH 7.0 and appeared to be a single protein by nondenaturing polyacrylamide gel electrophoresis (PAGE). The enzyme had the native molecular weight of 450 kD and subunits molecular weight of 63 kD and 38 kD as estimated by Sephadex G-200 chromatography and SDS-PAGE, respectively, suggesting that the enzyme is a heteromultimeric protein composed of two types of subunits. On the other hand, the enzyme appeared to be not a glycoprotein according to the results of Con A chromatography and glycoprotein staining. The enzyme had a Km for sucrose of 19.7 mM at pH 7.0 and maximum activity around pH 7.5. The enzyme was most active with sucrose as substrate, compared to raffinose, cellobiose, maltose and lactose. These results indicate the alkaline invertase is a $\beta$-fructofuranosidase.

• Mycobiology
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• v.36 no.1
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• pp.50-54
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• 2008

This study examined the chemical composition of A. blasiliensis and the chemical structural properties of an immuno-stimulating polysaccharide. The amino acids, free sugars, and organic acids by HPLC and fatty acids by GC were analyzed. The immuno-stimulating substance from A. blasiliensis was extracted with hot water and purified by ethanol precipitation. It underwent ion exchange chromatography on DEAE-cellulose and gel filtration on Toyopearl HW 65F. Through GP-HPLC, the substance was found to be homogeneous. Its chemical structure was determined by $^{13}C-NMR$. Fatty acids, organic acids, and sugar alcohol composition consisted exclusively of linoleic acid, fumaric acid and mannitol, respectively. The amino acids were mainly glutamic acid, glycine, and arginine. By $^{13}C-NMR$ analysis, the immuno-stimulating substance was identified as ${\beta}-(1{\rightarrow}3)\;(1{\rightarrow}6)$-glucan, composed of a backbone with $(1{\rightarrow}3)$-linked D-glucopyranosyl residues branching a $(1{\rightarrow}6)$-linked D-glucopyranosyl residue. The ${\beta}$-glucan from A. blasiliensis showed pronounced immuno-stimulating activity on the antibody-production ability of B-lymphocytes by the hemolytic suspension assay. In these results, A. blasiliensis was estimated to have potent pharmacological properties and potential nutritional values.

• Journal of the Korean Society of Food Science and Nutrition
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• v.27 no.1
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• pp.29-34
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• 1998

This study was investigated to know changes of the cell wall components, cell wall degrading enzyme activities and contents of soluble protein of strawberry during ripening and softening. The contents of water soluble substances were slightly increased during ripening, but the contents of alcohol-insoluble substances were not changed. The contents of pectin were not changed at green mature and turning stage, while decreased after mature stage. The contents of alkali-soluble hemicellulose and cellulose were increased during ripening and softening. The contents of water-soluble and saltsoluble protein were not changed, but the content of cell wall protein was slightly decreased during ripening. The content of total protein was increased at turning stage, it is not changed after turning stage. $\beta$-Galactosidase activity was increased during ripening, and pectinmethylesterase activity was decreased at turning. Phenylalanine ammonia-lyase activity was changed up to mature stage, but decreased at overripening stage. Polygalacturonase and cellulase activities were not detected at all of ripening stages.

• Journal of the Korean Wood Science and Technology
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• v.47 no.3
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• pp.371-380
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• 2019

Termites are pests that cause serious economic and cultural damage by digesting wood cellulose. Termites are arthropods and have an epidermis surrounded by a chitin layer. To maintain a healthy epidermis, termites have chitinase (${\beta}$-1,4-poly-N-acetyl glucosamidinase, EC 3.2.1.14), an enzyme that hydrolyzes the ${\beta}$-1,4 bond of chitin. In this study, the amino acid sequence of the gene, which is presumed to be termite chitinolytic enzyme (NCBI accession no. KC477099), was obtained from a transcriptomic analysis of Reticulitermes speratus KMT001 in Bukhan Mountain, Korea. An NCBI protein BLAST search confirmed that the protein is a glycoside hydrolase family 18 (GH18). The highest homology value found was 47%, with a chitinase from Araneus ventricosus. Phylogenetic analysis indicated that the KC477099 protein has the same origins as those of arthropods but has a very low similarity with other arthropod chitinases, resulting in separation at an early stage of evolution. The KC477099 protein contains two conserved motifs, which encode the general enzymatic characteristics of the GH18 group. The amino acid sequences $Asp^{156}-Trp^{157}-Glu^{158}$, which play an important role in the enzymatic activity of the GH18 group, were also present. This study suggests that the termite KC477099 protein is a new type of chitinase, which is evolutionarily distant from other insect chitinases.

• Bulletin of the Korean Chemical Society
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• v.8 no.4
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• pp.332-335
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• 1987

This paper is a continuation of our previous $paper,^1$ and deals with Eq.(1) (see the text), which was theoretically derived in the $paper,^1$$ [{\eta}]^f\; and\; [{\eta}]^0$ is the intrinsic viscosity at stress f and f = O, respectively. Equation (1) predicts how $[{{\eta}}]^f / [{\eta}]^0$ changes with stress f, relaxation time ${\beta}_2$ of flow unit 2 and a constant $c_2$ related with the elasticity of molecular spring of flow unit 2. In this paper, Eq.(1) is applied to a biopolymer, e.g., poly (${\gamma}$-benzyl L-glutamate), and nonbiopolymers, e.g., polyisobutylene, polystyrene, polydimethylsiloxane and cellulose triacetate. It was found that the $c_2$ factor is zero for non-biopolymers while $c_2{\neq}0$ for biopolymers as found $previously.^1$ Because of the non-Newtonian nature of the solutions, the ratio $[{{\eta}}]^f / [{\eta}]^0$ drops from its unity with increasing f. We found that the smaller the ${\beta}_2,$ the larger the $f_c$ at which the viscosity ratio drops from the unity, vice versa.

• Journal of the Korean Wood Science and Technology
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• v.51 no.4
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• pp.270-282
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• 2023

Lower termites need symbiotic microbes for cellulose digestion. Elizabethkingia miricola strain BM10 has been proposed as a symbiotic microbe that assists in low-temperature digestion and metabolism of Reticulitermes speratus KMT1, a termite on Bukhan Mountain, Seoul, Korea. In E. miricola strain BM10, β-glucosidase genes expressed at 10℃ were identified, and the psychrophilic enzymatic characteristic was confirmed by heterogeneously expressed proteins. Crude β-glucosidase in the culture broth of E. miricola strain BM10 showed specific enzymatic properties, and its substrate affinity was 4.69 times higher than that of Cellic CTec2. Among the genes proposed as β-glucosidase, two genes, bglB_1 and bglA_2, whose gene expression was more than doubled at 10℃ than at 30℃, were identified. They were heterogeneously expressed in Escherichia coli and identified as psychrophilic enzymes with an optimal reaction temperature of about 20℃-25℃. In this study, E. miricola strain BM10, a symbiotic bacterium of lower termites, produced psychrophilic β-glucosidases that contribute to the spread of the low-temperature habitat of a lower termite, R. speratus KMT1.

• Clinical and Experimental Reproductive Medicine
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• v.10 no.2
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• pp.1-11
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• 1983

${\beta}$-Glucuronidase from bull seminal plasma was partially purified by $(NH_4)_2SO_4$fractionation, two successive DEAE-cellulose columns, isoelectric focusing (pH 4 to 6) and Gel filtration on Sephadex G-200. Only one form of ${\beta}$-glucuronidase was obtained by isoelectric focusing at pH 5.13. Highly purified ${\beta}$-glucuronidase had specific activity of 34 units/mg protein and showed one major and some minor contaminants by disc gelk electrophoresis. The enzyme showed maximum activity at pH 5.2 and at $48^{\circ}C$. The enzyme was completely inhibited by 1,4 saccharo-${\alpha}$-lactone (5 mM). Albumin and 0.15 M NaCl increased the ${\beta}$-glucuronidase activity. Km of ${\beta}$-glucuronidase using phenolphthalein mono-${\beta}$-glucuronic acid as substrate was 2.9 mM and Vmax was $0.8{\mu}$mole/min. The enzyme appeared to be a glycoprotein by its binding to concanvalin·A. Rabbit and human sperm-acrosomal extracts and seminal plasma showed high ${\beta}$-glucuronidase activity.