• Clean Technology
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• v.18 no.4
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• pp.446-450
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• 2012

Strong alkaline electrolyzed water which is produced in cathode by electrolyzing the solution where electrolytes (NaCl, $K_2CO_3$ etc.) are added in diaphragm electrolytic cell, is eco-friendly and has cleaning effects. So, it is viewed as a substitution of chemical cleaner. In addition, strong alkaline electrolyzed water is being used by some Japanese automobile and precision parts manufacturing industries. When strong alkaline electrolyzed water is produced by using diaphragm electrolytic cell, it is necessarily produced at the anode side. Since strong acidic electrolyzed water produced is discarded when its utilization cannot be found, production efficiency of electrolyzed water is consequently decreased. Also, there is a weakness electrolytic efficiency is decreasing due to the pollution of diaphragm. In order to overcome this, non-diaphragm all-in-one electrolytic cell integrated with electrode reaction chamber and dilution chamber was applied. Strong alkaline electrolyzed water was produced for different composition of electrolytes, and their properties and characteristics were identified. In comparing the properties between strong alkaline electrolyzed water produced in diaphragm electrolytic cell and that produced in all-in-one electrolytic cell, the differences in ORP and chlorine concentration were found. In emulsification test to confirm surface-active capability, similar results were obtained and strong alkaline electrolyzed water produced in non-diaphragm all-in-one electrolytic cell was identified to be useable as a cleaner like strong alkaline electrolyzed water produced in diaphragm electrolytic cell. Strong alkaline electrolyzed water produced in non-diaphragm all-in-one electrolytic cell is thought to have sterilizing power because it has active chlorine which is different from strong alkaline electrolyzed water produced in diaphragm electrolytic cell.

• Microbiology and Biotechnology Letters
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• v.26 no.4
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• pp.290-296
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• 1998

Interspecific hybrids between Aspergillus oryzae var. oryzae and Penicillium chrysogenum (Tyr$\^$-/), high alkaline protease producing fungi, were obtained by nuclear transfer technique. Nuclei isolated from the wild type Aspergillus oryzae var. oryzae strain were transferred into auxotrophic Penicillium chrysogenum mutants and selected the new strains showing an increased protein degrading capability. Maximum production of protoplasts were obtained by 1% Novozym 234 at $30^{\circ}C$ for 3 hours and the most effective osmotic stabilizers for the isolation of protoplasts were 0.6M KCl. Frequencies of hybrid formation by nuclear transfer were 1.3${\times}$10$\^$-3/∼2.8${\times}$10$\^$-3/. They could be suggested as an aneuploid by the observation of genetic stability, conidial size, DNA content, and nuclear strain. The hybrids showed 1.1～2.2 fold higher alkaline pretense activities than parental strains.

• Korean Journal of Microbiology
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• v.40 no.2
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• pp.139-146
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• 2004

A bacterium producing alkaline cellulase was isolated from soil, leaf mold and compost, and was identified as alkalophilic Bacillus sp. HSH-810 by morphological, cultural and biochemical determination. The optimum cul-ture condition of Bacillus sp. HSH-810 for the growth and alkaline cellulase production was $30^{\circ}C$ and pH 10.0. The maximum alkaline cellulase production was obtained when 1.0%(w/v) CMC, 0.5%(w/v) peptone, 0.02%(w/v) $CaCl_2$ and 0.02(w/v) $CoCl_2$ were used as carbon source, nitrogen source and mineral source, respectively. The optimum pH and temperature of the enzyme activity were pH 10.5 and $50^{\circ}C$, respectively. This enzyme was fairly stable in the pH range of 6.0-13.0 and at $50^{\circ}C$. For the effect of surfactants, the activity of alkaline cellulase was stable in the presence of sodium-$\alpha$-olefin sulfonate (AOS), sodium dodecyl sulfonate (SDS), Tween 20 and Tween 80, but inhibited by the presence of 0.1 linear alkyl-benzene sulfonate (LAS) sig-nificantly.

• Microbiology and Biotechnology Letters
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• v.26 no.5
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• pp.427-434
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• 1998

An alkaline protease was 4-fold purified, yielding 2.3% of recovery by ammonium sulfate precipitation, CM-cellulose column chromatography and Sephadex G-100 column chromatography. The purified enzyme was estimated to be monomeric with molecular weight of about 62,000 from polyacrylamide gel eletrophoresis (PAGE) and sodiumdodecylsulfate polyacrylamide gel electrophoresis (SDS-FAGE). The optimal pH and temperature of the alkaline pretense activity were 11.0 and 50$^{\circ}C$, respectively, exhibiting high stability at pH value from 6.0 to 11.0 at 50$^{\circ}C$ for 30 minute. The alkaline pretense was activated by MnSO$_4$, CaCl$_2$, and was inhibited by CuSO$_4$, ZnSO$_4$, HgCl$_2$, EDTA and EGTA. Also, the enzyme was found to be a metaloenzyme requiring Mn$\^$2+/ as cofactor. The NH$_2$-terminal amino acid of alkaline protease was alanine. The Km and Vmax values of this enzyme for casein was 4.0 mg/$m\ell$ and 5,500 unit/$m\ell$, respectively.

• Microbiology and Biotechnology Letters
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• v.26 no.5
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• pp.450-455
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• 1998

Aspergillus oryzae M-2-3 strain (argB$\^$-/) was transformed with pTAalp plasmid which was constructed for expression of the alkaline pretense gene, alpA, and 16 transformants were selected on arginine minus medium. When these transformants were tested for productivity of alkaline proteases using agar plate containing skim milk, the halo was observed around each colony of transformants, but not observed around the host strain in this condition. Southern analysis showed that the pTAalp plasmid having alpA gene was integrated into the chromosome of the host strain. The highest level of alkaline protease production was obtained in the culture filtrate of the transformant No. 14, which was estimated to 80-90% of total secreted proteins, and the enzyme activity was 64-450 times higher than those of host strain and industrial strain. Total nitrogen content and the digestion rate in soybean Koji extracts were also increased to 1.5 times in Aspergillus oryzae transformant No. 14.

• Applied Biological Chemistry
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• v.31 no.4
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• pp.356-360
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• 1988

The alkaline protease producing bacteria isolated from soil and identified as Bacillus subtilis. The optimum medium for alkaline protease production from the microorganism was as follows; soluble starch, 1.5% ; proteose peptone, 0.5% ; $K_2HPO_4$, 0.1% ; $MgSO_4{\cdot}7H_2O$, 0.02% and sodium carbonate, 1.0%. The optimum temperature for alkaline protease production was $35^{\circ}C$, and the initial pH of medium was pH 10.5. The alkaline protease activity was about 2,300 U per ml of culture broth by Casein-Folin Method. A 9.2 fold purification of alkaline protease was obtained from culture broth. The recovery was 14% and purified enzyme was identified as single band, and its molecular weight was about 19,000. The optimum temperature for enzyme reaction was $70^{\circ}C$, and optimum pH was 12. The activity of purified enzyme was inhibited by metal ion ($Fe^{++}$), and Phenylmethylsulfonyl Fluoride, a serine protease inhibitor.

• Korean Journal of Food Science and Technology
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• v.23 no.2
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• pp.192-199
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• 1991

The rheological properties of various flour blends of HRW-WW and DNS-WW having protein contents of $9.12{\sim}9.78%$ in the presence or absence of salt and alkaline reagent (an equal mixture of$Na_2CO_3\;and\;K_2CO_3$) were studied. The farinograph absorptions of HRW-WW and DNS-WW blends was increased by 1% and 0.6%, respectively, with increasing protein content by 0.33%. Salt (0.17%) decreased the absorption by 1% regardless protein contents. Alkaline reagent (0.17%) or a combination of salt and alkaline reagent had no effect on absorption of flours, indicating that the effect of salt on decreasing absorption is masked by alkaline reagent. The protein content of the flour in the presence or absence of salt, alkaline reagent or both showed a highly positive correlation with all reference points of farinograph and extensograph, but the peak viscosity of amylograph was negatively correlated with protein content only in the presence of salt, alkaline reagent or both.

• Proceedings of the Korean Society of Toxicology Conference
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• 2001.05a
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• pp.116-116
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• 2001

The alkaline Comet assay has been used with increasing popularity to investigate the level of DNA damage in terms of strand breaks and alkaline labile sites in biomonitoring studies within the last decade in western countries.(omitted)

• Korean Journal of Microbiology
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• v.31 no.2
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• pp.175-178
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• 1993

Alkaline .alpha.-amylase expressed in the transformant, Baciollus subtills MB809, containing alkaline amylase gene cloned from alkalophilic Bacillus sp. AL-8, was purified through for step separation processes. The purified alkaline .alpha.-amylase had molecular weight of app[roximately 59, 000 daltons on SDS-PAGE and Sephaex G-100 gel filtration. Amino acid sequence of terminal portion of the enzyme was analyzed with pure amylase eluted form the SDS-PAGE gel. N-terminal amino acid sequence of .alpha.-amylase was determined by the Edman degradation method and resulted in $NH_{2}$-ser-thr-ala-pro-ser-(ile)-lys-ala-gly-thr-(ile)-leu. For C-terminal amino acid sequencing, purified .alpha.-amylase was digested with carboxypuptidase A and B, and reverse-phase HPLC gradient elution system resulted in -thr-trp-pro-lys-COOH.

• Journal of Korea Technical Association of The Pulp and Paper Industry
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• v.31 no.3
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• pp.68-76
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• 1999

Coprinus cinereus 2249 producing alkaline-active cellulase was screened from 29 species of Corpinaceae and constitutively produced alkaline carboxymethyl cellulase (CMCase) and filter paper cellulase (Fpase). When cultivated at pH 9.0, 25$^{\circ}C$ and 5 days, copnnus cinereus 2249 produced higher alkaline activity on 0.5% CMC, 2% wheat bran as carbon source and 0.5% peptone, 0.05% yeast extract as nitrongen source compared with other culture conditions. The level of cellulase production was higher in the presence of wheat bran than in the presence of CMC. The optimum temperature and pH for alkaline -active cellulase activity weas 50$^{\circ}C$ and 9, 0, respectively.