• Journal of the Korean Society of Food Science and Nutrition
• /
• v.16 no.2
• /
• pp.128-135
• /
• 1987

Extracellular ${\alpha}-amylase$, ${\beta}-amylase$ and glucoamylase produced by a thermophilic and cellulolytic bacterium, Herpetosiphon geysericola CUM 317, were partially purified by salting out with ammonium sulfate and by chromatography on a DEAE-cellulose column and on a CM-cellulose column. The Km values of ${\alpha}-amylase$, ${\beta}-amylase$ and glucoamylase for potato starch were $2.31mg/m{\ell}$, $7.69mg/m{\ell}$, and $8.33mg/m{\ell}$. The molecular weights of ${\alpha}-amylase$, ${\beta}-amylase$ and glucoamylase were calculated to be about 84000 dalton, 76000 dalton and 80000 dalton, respectively.

• Journal of the Korean Society of Food Science and Nutrition
• /
• v.22 no.6
• /
• pp.777-784
• /
• 1993

The bleaching effect of potato lipoxygenase Isoenzymes on ${\beta}-carotene$ was studied. Two lipoxygenase Isoenzymes(LOX-1, LOX-2) from potato tuber were purified by CM-cellulose, DEAE-cellulose ion exchange chromatography. LOX-1 and LOX-2 seemed to have bleaching effect on ${\beta}-carotene$ in the presence of linoleic acid, which the decrease in the formation of conjugated dienes. LOX-2 was founded to have a greater pigment bleaching activity than that of LOX-1.

• KSBB Journal
• /
• v.13 no.1
• /
• pp.20-25
• /
• 1998

Optimum conditions of the cellulose-hydrolysis reaction with mixed enzymes(cellulase extracted from Penicellium funiculosum mixed with $\beta$-glucosidase extracted from Almod) were investigated to increase the production of glucose from cellulose. Experimental result showed that optimum conditions fro pH, activity ratio of $\beta$-glucosidase to cellulase, concentration of mixed enzymes, concentration of cellulose as a substrate, and temperature range were 4.2, 0.4, 0.8, U/mL, 40 g/L, and 37$\pm$3$^\circ C$, respectively. In these conditions, quantities of glucose productions by using mixed enzymes were larger than those by using cellulase at optimum conditions.

• Journal of the Korean Wood Science and Technology
• /
• v.43 no.5
• /
• pp.628-640
• /
• 2015

Cellulase is the key enzyme in the use of cellulose-based biomaterials. Because of its structure, cellulose is difficult to be degraded by enzymes. In order to utilize cellulose-based biomaterials efficiently, evolutionary wisdom of how to use enzymes accurately and harmoniously in a biological system is needed, such as the cellulose digestive system in animals. In this study, the symbiotic bacteria from snails, Achatina fulica, were identified and their cellulase activity was evaluated. The 16S rRNA sequence analysis of 100 aerobic bacteria showed that they belonged to 9 genus and almost half of the bacteria were Lactococcus spp. Among 100 identified strains, only two Aeromonas sp. strains showed cellulase activity. Aeromonas sp. KMBS020 had both endo-${\beta}$-glucanase and ${\beta}$-glucosidase activities but Aeromonas sp. KMBS018 had ${\beta}$-glucosidase activity only. None of the 100 bacterial colonies had any cellobiohydrolase activity.

• Polymer(Korea)
• /
• v.38 no.3
• /
• pp.338-350
• /
• 2014

Cellulose acetate (CA) fiber mats containing inclusion complexes of asiaticoside (AC) in 2-hydroxypropyl-${\beta}$-cyclodextrin ($HP{\beta}CD$) for potential usage as wound dressings were developed. The AC/$HP{\beta}CD$ complex-loaded CA fibers at various $HP{\beta}CD$ to AC molar ratios of 0.5, 1, and 2 were prepared in 90:10 v/v mixture of 80% (v/v) acetic acid and N,N-dimethylacetamide (DMAc) via electrospinning. The maximum released amounts of AC depended on the $HP{\beta}CD$ content and were much greater than those released from the AC-loaded CA fiber mat. In the in vitro study, indirect cytotoxic evaluation with human dermal fibroblasts (HDFa) showed that these materials released no substances in the levels that were harmful to the cells and the cells appeared to attach and proliferate well on these substrates. However, only the CA fiber mats containing AC/$HP{\beta}CD$ complexes at the $HP{\beta}CD$ to AC molar ratio of 0.5 was effective in upregulating the production of collagen of the cultured cells.

• Molecules and Cells
• /
• v.28 no.4
• /
• pp.369-373
• /
• 2009

Heterologous secretory expression of endoglucanase E (Clostridium thermocellum) and ${\beta}$-glucosidase 1 (Saccharomycopsis fibuligera) was achieved in Saccharomyces cerevisiae fermentation cultures as an ${\alpha}$-mating factor signal peptide fusion, based on the native enzyme coding sequence. Ethanol production depends on simultaneous saccharification of cellulose to glucose and fermentation of glucose to ethanol by a recombinant yeast strain as a microbial biocatalyst. Recombinant yeast strain expressing endoglucanase and ${\beta}$-glucosidase was able to produce ethanol from ${\beta}$-glucan, CMC and acid swollen cellulose. This indicates that the resultant yeast strain of this study acts efficiently as a whole cell biocatalyst.

• Journal of Microbiology and Biotechnology
• /
• v.18 no.3
• /
• pp.443-448
• /
• 2008

Multidomain proteins for the biochemical analysis of the scouring efficiency of cotton fabrics were constructed by the fusion of a reporter moiety in the N-terminal and the cellulose binding domain (CBD) in the C-terminal. Based on the specific binding of the CBD of Cellulomonas fimi exoglucanase (Cex) to crystalline cellulose (Avicel), the reporter protein is guided to the cellulose fibers that are increasingly exposed as the scouring process proceeds. Among the tested reporter proteins, a thermostable ${\beta}$-glycosidase (BglA) from Thermus caldophilus was found to be most appropriate, showing a higher applicability and stability than GFP, DsRed2, or a tetrameric ${\beta}$-glycosidase (GUS) from Escherichia coli, which were precipitated more seriously during the expression and purification steps. When cotton fabrics with different scouring levels were treated with the BglA-CBD and incubated with X-Gal as the chromogenic substrate, an indigo color became visible within 2 h, and the color depth changed according to the conditions and extent of the scouring.

• KSBB Journal
• /
• v.11 no.2
• /
• pp.151-158
• /
• 1996

For the effective ethanol fermentation, the high concentration of sugar as the substrate of microbial fermentation is required. The most important reason in the inefficient hydrolysis; the easy deactivation of enzyme by temperature or shear stress and the severe inhibition effects of its products. In our work, we comprehended the kinetic characteristics of cellulose and ${\beta}$-glucosidase in the progress of hydrolysis, and observed the potential inhibitory effects of the hydrolyzed products and the deactivation of enzymes. We also tried to present the kinetic model of enzymatic hydrolysis of cellulose, which is applicable to process at the high concentration of sugar. Cellulase and ,${\beta}$-glucosidase exhibit diverse kinetic behaviors. At a level of only 5g/$\ell$ of glucose, the ${\beta}$-glucosidase activity was reduced by more than 70%. This result means that ${\beta}$-glucosldase was the most severely inhibited by glucose. Also at l0g/$\ell$ of cellobiose, the cellulose lost approximately 70% of its activity. ${\beta}$-glucosldase was more sensitive to deactivation than cellulose by about 1.6 times. The comprehensive kinetic model in the range of confidence was obtained and the agreement between the model prediction and the experimental data was reasonably good, testifying to the validity of the model equations used and the associated parameters.

• Korean Journal of Microbiology
• /
• v.25 no.4
• /
• pp.297-297
• /
• 1987

A $C_{1}$ enriched cellulase fraction was separated from culture filtrate of anaerobic Clostridium thermocellum by hydroxyapatite column chromatography. The separated fraction showed strong synergistic action with $C_{x}$ component (endo-$\beta$-1, 4-glucanase) in digestion of crystalline cellulose, similar to the other aerobic cellulolytic microorganisms. Unlike the $C_{x}$ component the $C_{1}$ enriched fraction was rapidly inactivated by oxidation at the atmospheric condition. The enzyme activity was significantly enhanced by the addition of reducing agents, especially $\beta$-mercaptoethanol, which indicates that a $C_{1}$ component has a lot of sulfhydryl groups essential for the enzyme activity. The effect of metal ions on $C_{1}$ activity was also investigated. The $C_{1}$ fraction was found to be thermally stable compare to endo-$\beta$-1,4-glucanase. Optimal temperature and pH were found to be 60.deg.C and 6.0, respectively.

• Proceedings of the Korea Technical Association of the Pulp and Paper Industry Conference
• /
• 1999.11b
• /
• pp.50-55
• /
• 1999

Sizing development of AKD-sized paper by beta-ketoester formation has been debated until recent years because of absence of its obvious and direct spectroscopic evidence. In this study, reaction between AKD and cellulose was investigated to disclose the possibility of beta-ketoester formation between two components under no catalyzed neutral condition. In absence of water, AKD reacted with cellulose to form beta-ketoester linkage under no catalyzed neutral condition, while, in presence of water, most of AKD was hydrolyzed to a dialkyl ketone or beta-ketoacid. Therefore, the main mechanism of AKD sizing would not be the formation of beta-ketoester between AKD and cellulose in the papermaking process. It could be suggested that the sizing development of AKD-sized paper is obtained by next two mechanisms: 1) formation of a thin-layer of AKD on the fiber surface through melting and spreading of AKD emulsion particles by heat, and 2) the formation of ketone by the hydrolysis of AKD during drying and storage of AKD-sized papers.