• Journal of Microbiology and Biotechnology
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• v.11 no.2
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• pp.229-233
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• 2001

Trichoderma reesei Rut C-30 produced high levels of ${\beta}$-glucosidase, endo-${\beta}$-glucosidase, endo-${\beta}$-1,4-glucanase, and exo-${\beta}$-1,4-glucanase. In pilot-scale production (50-1 fermentor), productivity and yield of CMCase (carborymethyl cellulose) and FPase (filter paper activity) were 273 U/ml and 35 U/ml, and 162 FPU/l.h and 437 FPU/g, respectively. The fed-batch techniques were used to improve enzyme activities with constant cell concentration. The acidity was an important parameter and controlled at pH 3.9 and 5.0 by automatic addition of ammonium hydroxide. Cellulase powder was prepared by ammonium sulfate precipitation and its CMCase and FPase activities were 3,631 U/g and 407 U/g, respectively.

• Korean Journal of Microbiology
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• v.40 no.3
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• pp.230-231
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• 2004

The mycelia of Sparassis crispa DSMZ 5201 were cultivated at $24^{\circ}C$ for 15 days in yeast-malt extract-glucose broth (pH 4.0) and the filtrate was used as crude enzyme solution to determined the extracellular enzyme activity. The specific activity of $\alpha$-amylase was 44.27 unit/protein. The specific activities of protease, CMCase, $\beta$-glucosidase, chitinase, exo-$\beta$-l,4-glucanase were relatively high. However, a very little activity of xylanase was found.

• Journal of Applied Biological Chemistry
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• v.43 no.3
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• pp.141-146
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• 2000

Glycosidase activities were tested from the grape berries, Vitis labruscana B. Takasumi. Among various glycosidases, $\alpha$-D-galactosidase was found to be the most active in the flesh and other glycosidases were considerably active in the order of the following: $\alpha$-D-mannosidase>$\alpha$-D-glucosidase>$\beta$-D-glucosidase>$\beta$-D-galactosidase. In the seeds, $\alpha$-D-glucosidase activity was the highest and other glycosidases such as $\alpha$-D-galactosidase, $\beta$-D-glucosidase, and $\beta$-D-galactosidase were still significantly active. The $\alpha$-D-galactosidase in the grape flesh was purified over 83-folds through salting-out with $(NH_4)_2SO_4$ and a series of chromatographies employing Sephadex G-50, Octyl-Sepharose, Q-Sepha- rose, and Biogel P-100. The enzyme was a monomer of 45 kDs as determined through SDS-PAGE and Sephacryl S-200 chromatography. The purified enzyme showed a preference of $\alpha$-D-galactose to $\beta$-D-galactose as a substrate about 5.4 times. Sulfhydryl specific reagents such as N-ethylmaleimide and iodoacetamide significantly inhibited the enzyme activity to the extents of 48 and 52% of its initial activity, respectively. The optimumpH range of $\alpha$-D-galactosidase was around 6.5-7.0. The enzyme activity increased by 46% in the presence of 1mM $Fe^{2+}$.

• The Korean Journal of Food And Nutrition
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• v.25 no.3
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• pp.620-628
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• 2012

We examined the effects of biological activity Phellinus linteus mycelium culture with cassiae semen extract. Firstly, the optimal temperature, initial pH and culture period for mycelial growth in a liquid culture of P. linteus were determined, and they were $30^{\circ}C$, pH 5.0 and 8 days respectively. The five herbal materials were examined against several health functional efficacies, and, as a result, Cassiae semen was chosen, with its superior inhibitory effects in ${\beta}$-glucuronidase inhibitory activity, electron donating activity, ACE inhibitory, and ${\alpha}$-glucosidase inhibitory activities(95.3%, 80.9%, 96.1 and 24.2%, respectively). P. linteus fruit body was investigated on ${\beta}$-glucuronidase inhibitory activity, electron donating activity, ACE inhibitory, and ${\alpha}$-glucosidase inhibitory activities, and they were 54.7%, 81.9%, 30.0% and 20.1%, respectively. Accordingly, C. semen was used in the following experiment, to give an additive functional effect on the P. linteus. As the amount of C. semen in the cultural media increased, mycelial weight and ${\beta}$-glucan contents also increased, but final pH was not influenced. In addition, the ${\beta}$-glucuronidase inhibitory activity, electron donating activity, and ${\alpha}$-glucosidase inhibitory activity increased. P. linteus mycelium culture showed higher activities in the other three tests above, except for electron donating activity, when C. semen was added to the medium before cultivation.

• Korean Chemical Engineering Research
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• v.49 no.1
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• pp.101-104
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• 2011

Cellobiose dehydrogenase(CDH) as a hemoflavoenzyme is secreted out of cell in the cellulose degradation. As CDH strongly bound to amorphous cellulose, it helps cellulose hydrolysis by cellulase. CDH may have an important role of saccharification process for bioethanol production. In this study, Phanerochaete chrysosporium ATCC 32629 was selected for the production of CDH among other strains tested. The optimal temperature and pH of CDH produced by P. chrysosporium ATCC 32629 were ${55^{\circ}C}$ and 4, respectively. To improve the activity of CDH, the mutation of P. chrysosporium was performed using proton beam that has high energy level partially. As a result, P. chrysosporium mutant with the high activity was selected at 1.2 kGy in a range of 99.9% lethal rate. The CDH and $\beta$-glucosidase activities of mutant were 1.4 fold and 20 fold higher than those of wild strain. Therefore, P. chrysosporium mutant with the high activities of CDH and $\beta$-glucosidase was obtained from mutation by proton beam irradiation.

• Applied Biological Chemistry
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• v.38 no.6
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• pp.490-495
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• 1995

Among the cellulases by Cellulomonas sp. KL-6. CMCase and filter paperase, which were produced as the out enzymes of cell, had been much produced, but very small amounts of ${\beta}-glucosidase $, the enzyme of which is cell bound form, was produced by this organism. The optimal culture times for CMCase and filter paperase productions were 5 days, while that of ${\beta}-glucosidase$ was 4 days. When this strain was cultured under the optimal medium for enzyme production, CMCase, FPase and ${\beta}-glucosidase$ were $82\;units/m{\ell},\;80\;units/m{\ell}\;and\;1.2\;units/m{\ell}$, respectively. Thus these results were showed to increase enzyme productivities as about $60{\sim}70%$ than those produced in basal medium. $CaCO_3$ injected to the medium as the ratio of 0.1% was not only enhanced cellulase activities but also effective as acid neutralizing agent. The production effects of lignase and lactase by this bacterium in filter paper medium was not appeared.

• The Korean Journal of Zoology
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• v.34 no.2
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• pp.159-172
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• 1991

It has been investigated what could be the selective marker distinguishing the immature from mature spermatozoa and whether fi -glucuronidase and fi -glucosidase are dependent on androgen in the luminal fluid of the epididymis or not. The contents of hexose, hexosamine and sialic acid in the epithelial cells, luminal fluid and spermatozoa of the epididymis were examined and the patterns of protein bands were compared in each group of the luminal fluid by SDS-PAGE. Lactate dehydrogenase, glucose-6-phosphatase, Na+ -K+ -ATPase and MgNa-ATPase showed higher activities in the cauda than the caput epididymal spermatozoa but only $Mg^2$+-ATPase activity appeared to be changed significantly. When the contents of hexose, hexosamine and sialic acid were analyzed and compared quantitatively, those of hexose were significantly different in the luminal fluid of caput and cauda epididymis, those of hexosamine in the epithelial cells and those of sialic acid in the epithelial cells and luminal fluid. When SDS-PAGE has been performed in each group, the band of MW 33-37 KD which was absent in the luminal fluid of caput epididymis appeared obviously in the luminal fluid of cauda epididymis and ako apeared in the cauda sperm crude membrane fraction. In addition, $\beta$ -glucuronidase and $\beta$ -glucosidase activities and their dependence on androgen were measured and the SDS-PAGE patiems of proteins and/or glycoproteins in the luminal fluid were examined. The activities of these two enzymes in the luminal fluid of the epididymis decreased significantly from the 5th day after castration. When testosterone was injected, the activity of $\beta$ -glucuronidase began to increase significantly from the 5th day following injection and that of $\beta$ -glucosidase from the loth day. On the other hand, the band of about MW 21 KD was newly observed in the lumen of caput epididymis when testosterone was administered.

• Journal of the Korean Wood Science and Technology
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• v.38 no.3
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• pp.251-261
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• 2010

Cellulase from Formiptosis pinicola KMJ812 is an efficient cellulose degradation enzyme complex, especially with a high ${\beta}$-glucosidase activity. In this study, the change in enzymatic characteristics by immobilization and the reduction of immobilized enzyme activity by repeated usages were evaluated using cellulases from F. pinicola KMJ812. Among tested four resins, Duolite A568 resin had the best enzyme activity yield with 61.7% cellulase activity and 64.4% ${\beta}$- glucosidase activity during the cellulase immobilization. The best reaction temperature was $55^{\circ}C$ for both cellulase and ${\beta}$-glucosidase activities which were higher than the unimmobilized soluble cellulases. The best reaction pH was 4.0 for cellulase activity which was a little more basic than a soluble form and 4.5 for ${\beta}$-glucosidase activity. The immobilized cellulase activity was remained 98% of the beginning activity after 72 h incubation at $50^{\circ}C$ and 50% of the beginning activity after eight times usage at $50^{\circ}C$.

• The Korean Journal of Mycology
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• v.42 no.3
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• pp.207-212
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• 2014

This study was conducted in order to investigate the physiological activities, including antioxidative, fibrinolytic, thrombin inhibitory, and ${\alpha}$-glucosidase inhibitory activities of the water extract and solvent fractions isolated from Pholiota adiposa. The antioxidative activities of the water extract and water fraction were 57.57% and 48.27%, respectively. The fibrinolytic activity was strong only in the ethyl acetate fraction at 0.70 plasmin units/mL. The ethyl acetate fraction showed high thrombin inhibitory activity, and a-glucosidase inhibitory activity at 77.67% and 89.32%, respectively. The ethyl acetate fraction hydrolyzed both $A{\alpha}$ and $B{\beta}$ subunits of human fibrinogen, but did not show reactivity for the ${\gamma}$ form of human fibrinogen. Fibrinolytic activity of the ethyl acetate fraction was not decreased by heating for 10 min at $100^{\circ}C$.

• KSBB Journal
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• v.5 no.3
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• pp.279-291
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• 1990

Partial hydrolysed and deacetylated chitin, CHITA and CHITB as supports of immobilized enzyme were obtained by treatment of acid and base respectively. Glutaraldehyde, bifunctional reagent, was employed for crosslinking between $\beta$-glucosidase and support. Immobilized enzyme activities of CHITA-Gase and CHITB-Gase were determined with the reaction of p-nitrophenol-$\beta$-D-glucopyranoside(PNG) in batch reactor, CSTR and PFR. Their optimum temperature, pH and enzymatic characteristics including Km and Vmax values were observed with variation of the flow rates. Mass transfer coefficient(h), effectiveness factor(η), deactivation rate(kd ) of two immobilized enzymes were also examined to compare efficiency of reactors.