• Korean Journal of Microbiology
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• v.18 no.2
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• pp.59-66
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• 1980

Two strains S-P and S-P-2, both Streptomyces sp., have been isolated and were found to have relatively high specific enzyme activity compared to other organisms reported. The specific activity of the enzyme produced from these two strains were 0.25 and 0.2 international units respectively. The productivity of the enzyme achieved was about 50 IU/l/hr. Glucose isomerase form these strains was found to be stable under the temperature of heat treatment (at $65^{\circ}C$) for fixation of enzyme inside the dell. This organism has an advantage in that it did not require toxic metalic ion for enzyme activity and could utilize xylan in leu of xylose as an inducer. The optimal temperature and pH of enzymatic reaction purpose of using these data for the optimal operation and designing of enzyme reactor system. The reaction mechanism was found to follow the single substrate reversible reaction kinetics. The kinetic constants determined experimentally are : $K_{mf}=0.33M,\;K_{mb}=1.0M,\;V_{mf}=0.88{\mu}mole\;per\;min.,\;V_{mb}= 2.96{\mu}mole\;per\;min.\;and\;K_{eq}=0.74.

• Microbiology and Biotechnology Letters
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• v.25 no.3
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• pp.305-310
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• 1997

For the continuous production of transglucosylated steviosides, cyclodextrin glucanotransferase from Bacillus macerans was immobilized onto Diaion HPA 75 (styrene-divinylbenzene resin) that was screened from ion exchange resins, synthetic adsorbents and chitosan derivatives. The parameters influencing enzyme immobilization were examined in order to maximize the activity of immobilized enzyme. The optimum conditions for immobilization turned out to be: contact time 2 hr at 30$circ$C, pH 6$sim$9, and enzyme loading 20mg protein/g resin at 4.4 Os/Kg as osmolarity. Competing with other molecules having low molecular weight, enzyme was immobilized reversibly. The activity of immobilized enzyme was as high as 180U/g resin when the diafiltrated solution of stock enzyme was used. The optimum conditions for transglucosylation were as follows: pH 6.0, temperature 50$circ$C, 30% substrate solution composed of 15% stevioside mixture and 15% dextrin of which value of dextrose equivalent was about 9.0.

• 한국생물공학회:학술대회논문집
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• 2000.04a
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• pp.239-242
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• 2000

Experimental studies on the effects of impeller to provide the microbial transglutaminase derived from Streptoverticillium mobaraense have been conducted. The optimal production medium was determined by latin-square design, and the effects of aeration and agitation were observed by using different sizes and shapes of impellers for the poduction of transglutaminase. The effects of pH and temperature were also evaluated for the production of transglutaminase in flasks. As a result, pH is more effective than temperature for both enzyme production and growth of the microorganism. The peak enzyme activity for transglutaminase in fermenter was 0.7 U/mL, but this was still well below the avereage enzyme activity, 1,3 U/mL, obtained in flask runs.

• Journal of Applied Biological Chemistry
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• v.49 no.4
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• pp.135-139
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• 2006

A alkalophilic strain, Bacillus licheniformis MH31 producing an alkaline protease was isolated from mine soil of Boryeong in Korea. Production of a high level of alkaline protease was achieved 42 h after incubation when the bacterium was grown at pH 9.0 and $35^{\circ}C$ in Horikoshi medium supplemented with 0.5%(w/v) starch and 1%(w/v) skim milk as carbon and nitrogen source, respectively. The molecular weight of partially purified enzyme was estimated to be 30 kDa by SDS-PAGE and its optimum pH was pH 10. The enzyme showed optimum temperature at $50^{\circ}C$, and was stable up to $60^{\circ}C$ after 1 h incubation. The protease was strongly inhibited by 1 mM of PMSF which was known well as strong inhibitor of serine proteases, but almost not inhibited by 5 mM of EDTA and 1,10-phenanthroline. When the protein hydrolysis products of 1% skim milk by partially purified protease was compared with available commercial proteases using HPLC analysis, most of hydrolysis products were detected below molecular weight of 10,000 and the hydrolysis ratio of purified enzyme was 24.8% lower than those(above 32%) of commercial proteases.

• Microbiology and Biotechnology Letters
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• v.31 no.2
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• pp.157-164
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• 2003

An alkali-tolerant bacterium producing the xylanase was isolated from soil and identified as Bacillus alcaiophilus. This strain, named B. alcalophilus AX2000, was able to grow and produce xylanase optimally at pH 10.5 and $37^{\circ}C$. The maximum xylanase production was obtained when 0.5%(w/v) birchwood xylan and 0.5%(w/v) polypeptone and yeast extract were used as carbon source and nitrogen source, respectively. The biosynthesis of xylanase was under the catabolite repression by glucose in the culture medium, and inhibited in the presence of high concentration of xylose. The maximum activity of xylanase was observed at pH 10.0 and $50^{\circ}C$ and the enzyme activity remained was over 80% at $60^{\circ}C$ and from pH 5.0 to 11.0.

• Proceedings of the Korean Society for Applied Microbiology Conference
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• 2000.04a
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• pp.68-75
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• 2000

D-Tagatose is a potential bulking agent in food as a non-calorific sweetener. To produce D-tagatose from cheaper resources, plasmids harboring the L-arabinose isomerase gene (araA) from Escherichia coli was constructed because L-arabinose isomerase was previously suggested as an enzyme that mediates the bioconversion of galactose to tagatose as well as that of arabinose to ribulose. In the cultures of recombinant E.coli with pTC101, which harboring araA of E.coli, tagatose was produced from galactose in 9.9 % yield. The enzyme extract of E.coli containing pTC101 also converted galactose into tagatose in 96.4 % yield. For the economic production of D-tagatose, an L-arabinose isomerase of E.coli was immobilized using covalent binding on agarose. While the free L-arabinose isomerase produced tagatose with the rate of 0.48 mg/U$.$day, the immobilized one stably converted galactose into average 7.5 g/l$.$day of tagatose during 7 days with higher productivity of 0.87 mg/U$.$day. In the scaled up immobilized enzyme system, 99.9 g/l of tagatose was produced from galactose with 20 % equilibrium in 48 hrs. The process was stably repeated additional 2 times with tagatose production of 104.1 and 103.5 g/l.

• Journal of Microbiology and Biotechnology
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• v.9 no.2
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• pp.223-226
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• 1999

A bacterial strain producing high level of an extracellular phytase was isolated from cooked rice and identified as a strain of Bacillus sp. and designated as Bacillus sp. KHU-10. Optimum culture conditions were investigated for the maximum productivity of phytase by Bacillus sp. KHU-10. 1.0% Maltose and 1.0% peptone with 0.5% beef extract were the best carbon source and nitrogen source, respectively. The addition of $CaCl_2$, stimulated the enzyme productivity with concentration between 0.01% and 0.2%, in the medium. Although sodium phosphate increased the cell mass, the enzyme activity decreased. Calcium phytate and wheat bran containing phytate did not enhance the enzyme production. Under the optimum medium, the production of the phytase reached the highest level of 0.2 unit/ml after 4 days of incubation.

• Microbiology and Biotechnology Letters
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• v.22 no.3
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• pp.283-289
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• 1994

The production of maltose utilizing swollen extrusion starch seems to have many technical advantages, such as, high reaction rate and high yield, production of high purity concentrated maltose, and low energy consumption, over the conventional method utilizing liquefied starch. The characteristics of maltose formation in heterogeneous enzyme reaction system comtaining swollen extrusion starch was investigated using fungal $\alpha $-amylase. The influence of extrusion conditions on structure of extruded starch, such as, degree of gelatinization, water absorption index, and water solubility index was analyzed. The relationship between the structural features and maltose forming reaction was investigated, and the result was analyzed in terms of surface reaction of insoluble extruded swollen starch. The characteristics of maltose formation from swollen sxtrusion starch was compared using endo-type fungal $\alpha $-amylase and exo-type $\beta $anylase, and the structural trasformation of extruded starch was also observed to clarify the reaction mechanism.

• The Journal of Korean Medicine
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• v.17 no.1 s.31
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• pp.21-36
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• 1996

This study was undertaken to examine the effect of Jwagyuyeum and Woogyuycum, being known to reinforce Kidney-yin and yang, on the activities of endogenous antioxidant enzymes and the production of oxygen free radicals in the liver and kidney tissues, Alterations in enzyme activities were observed after in vivo treatment in rats, Jwagyuyeum and Woogyuyeum caused a significant increase in the activities of superoxide dismutase(SOD) and catajase Jwagyuyeum significantly increased the activity of glutathione peroxidase in both liver and kidney, but the enzyme activity was not significantly altered by Woogyuyeum. Treatment in vitro of Jwagyuyeum and Woogyuyeum decreased the production of oxygen free radicals in a dose-dependent fashion. These results suggest that Jwagyuyeum and Woogyuyeum stimulate the activities of antioxidant enzymes and inhibit directly the production of oxygen free radicals. These effects of both herbs may contribute to prevent the oxygen free radical-induced impairment of cell function.

• Journal of Microbiology and Biotechnology
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• v.31 no.5
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• pp.740-746
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• 2021

Efficient cellulolytic enzyme production is important for the development of lignocellulose-degrading enzyme mixtures. However, purification of cellulases from their native hosts is time- and labor-consuming. In this study, a constitutive expression system was developed in Penicillium oxalicum for the secreted production of proteins. Using a constitutive polyubiquitin gene promoter and cultivating with glucose as the sole carbon source, nine cellulolytic enzymes of different origins with relatively high purity were produced within 48 h. When supplemented to a commercial cellulase preparation, cellobiohydrolase I from P. funiculosum and cellobiohydrolase II from Talaromyces verruculosus showed remarkable enhancing effects on the hydrolysis of steam-exploded corn stover. Additionally, a synergistic effect was observed for these two cellobiohydrolases during the hydrolysis. Taken together, the constitutive expression system provides a convenient tool for the production of cellulolytic enzymes, which is expected to be useful in the development of highly efficient lignocellulose-degrading enzyme mixtures.