• Microbiology and Biotechnology Letters
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• v.17 no.2
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• pp.160-164
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• 1989

A 5.7Kb EcoRI fragment containing alkaline amylase gene of Bacillus sp. AL-8 obtained in the previons experiment (10) was transformed in B. subtilis via plasmid pUB110. The enzymatic proper-ties of the amylase produced by the transformants were Identical to those of the donor strain. Thus, the alkaline amylase activity from the transformant was maximum at pH 10 and 5$0^{\circ}C$. And the enzyme was very stable over the ranges of alkaline pH. In order to determine the location of the alkaline amylase gene within the 5.7Kb DNA fragment, the fragment was subcloned in E. coli. It was found that the alkaline amylase gene was located k EcoRI fragment of 3.7Kb.

• Journal of the Korean institute of surface engineering
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• v.28 no.1
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• pp.55-63
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• 1995

Alkaline solutions such as $NH_4$OH, choline and TMAH (($CH_3$)$_4$NOH) have been introduced in semiconductor wet processing of silicon wafers to control ionic and particulate impurities following etching in acidic solutions. These chemicals usually mixed with hydrogen peroxide and/or surfactants to control the etch rate of silicon. The highest etch rate was observed in $NH_4$OH solutions at a pH in alkaline solutions. It indicates that the etch rate depends on the content of $OH^{-}$ as well as cations of alkaline solutions. STM/AFM techniques were used to characterize the effect of alkaline solutions on silicon surface roughness. In SC1 (mixture of $NH_4$OH : $H_2$$O_2$ : $H_2$O) solutions, the reduction of the ammonium hydroxide proportion from 1 to 0.1 decreased the surface roughness ($R_{rms}$) from 6.4 to $0.8\AA$. The addition of $H_2$$O_2$ and surfactants to choline and TMAH reduced the values of $R_{p-v}$ and $R_{rms}$ significantly. $H_2$$_O2$ and surfactants added in alkaline solutions passivate bare silicon surfaces by the oxidation and adsorption, respectively. The passivation of surfaces in alkaline solutions resulted in lower etch rate of silicon thereby provided smoother surfaces.s.ces.s.

• Journal of Korea Technical Association of The Pulp and Paper Industry
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• v.43 no.3
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• pp.106-112
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• 2011

The effects of alkaline treatment on the WRV, crystalline structure and sheet structure of softwood and hardwood bleached kraft pulp were investigated. Sodium hydroxide and sodium carbonate were used as chemicals for alkaline treatment and two levels of alkali dosage (5%, 10%) were applied respectively. Alkali treated and untreated pulp were refined to three levels (550, 450 and 350 mL CSF). WRV of the alkali treated pulps depended on the alkaline type and concentration. It was found that the crystalline structures of softwood and hardwood pulp were not changed by refining. Sodium carbonate and lower concentration of sodium hydroxide treatment did not caused any modification of cellulose crystalline structure, while higher concentration of sodium hydroxide treatment caused the partial modification of cellulose crystalline structure. Alkaline treatment of hardwood bleached kraft pulp led to the shrinkage of fiber diameter and bulky structure of sheet. Alkaline treatment of softwood bleached kraft pulp did not cause the significant change in fiber shrinkage and bulk of sheet.

• Journal of the Korean Ceramic Society
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• v.52 no.3
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• pp.180-185
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• 2015

Low-cost ceramic membrane supports with pore sizes in the range of $0.52-0.62{\mu}m$ were successfully prepared by uniaxial dry compaction method using inexpensive raw materials including kaolin, bentonite, talc, sodium borate, and alkaline-earth oxides in carbonate forms (e.g., $MgCO_3$, $CaCO_3$, and $SrCO_3$). The prepared green supports were sintered at $1000^{\circ}C$ for 8 hr in air. The effect of alkaline-earth oxide additives on the flexural strength of clay-based membrane supports was investigated. The porosity of the clay-based membrane supports was found to be in the range of 33-34%. The flexural strength of the clay-based membrane supports with 1% alkaline-earth carbonates was found to be in the range of 42.8-52.7 MPa. The addition of alkaline-earth carbonates to clay-based membrane supports resulted in large increases (47-80%) in the flexural strength of the membrane supports, compared to that of membrane supports without alkaline-earth carbonates. The typical flexural strength of the clay-based membrane support with 1% $SrCO_3$ was 52.7 MPa at 33.8% porosity.

• Korean Journal of Microbiology
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• v.28 no.3
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• pp.204-209
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• 1990

The total and heterotrophic bacterial distributions, compositions and alkaline phosphatese actibities were analyzed in Lake Soyang from Sep. 1987 to Aug. 1988. The heterotrophic bacteria was small portion, 0.07-2.63% of total bacterial number which ranged from $3.2{\times}10^{5}$ to $3.2{\times}10^{6}$ cells/${\mu}\ell$. The composition of bacterial community was less diverse in summer and at the fish farm site and Peridinium blooming site. Pseudomonas and Flavo bacterium were the dominant genera in all sites. The highest proportion and activity of alkaline phsophatase was appeared in Flavobacterium, while Pseudomonas was the most predominant group.

• Microbiology and Biotechnology Letters
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• v.17 no.4
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• pp.358-364
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• 1989

A crystalline alkaline pretense- producing Streptomyce sp. YSA-130 was isolated from soil in alkaline medium(pH 10.5). The optimum culture condition of Streptomyce sp. YSA-130 for the production of alkaline protease was as follows; 2.0% soluble starch, 1.0% soytone, 0.3% $K_2$HPO$_4$, 0.02% MgSO$_4$.7$H_2O$, 0.8% Na$_2$CO$_3$, pH 10.5, 3$0^{\circ}C$, and 12 hr. The alkaline pretense from the culture broth of Streptomyce sp. YSA-130 was purified about 24 folds by ammonium sulfate precipitation , dialysis, DEAE-cellulose ion exchange chromatography, gel filtration on Sephadex G-15 and crystallization. Optimum temperature and pH of purified enzyme were 6$0^{\circ}C$, and 11.5. Temperature and pH stability of purified enzyme were 5$0^{\circ}C$, and 5.5-12.0. Calcium ion was effective to stabilize the enzyme at higher temperature. The molecular weight of the purified enzyme was approximately 30,000. The purified enzyme was inactivated by diisopropyl flurophosphate(DFP) but not affected by metal ion, EDTA, sulfhydryl reagent and stable detergent.

• Biomedical Science Letters
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• v.5 no.1
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• pp.119-129
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• 1999

This study was aimed to investigate the enzyme-histochemical localization and characteristics of alkaline and acid phosphatase extracted from adult of Echinostoma hortense. Using the Gomori calcium stain and the Gomori lead nitrate satin method, we found that the alkaline and acid phosphatases were localized mostly in the intestine, vitellaria and pharynx of Echinostoma hortense. The three isozymes of alkaline phosphatase and two isozymes of acid phosphatase were separated from Echinostoma hortense by electrophoresis. The isozymes of alkaline phosphatase were 145.9, 207.5, 220.8 kDa and the isozymes of acid phosphatase were 179.5 and 209.4 kDa. The activity of alkaline phosphatase was denatured completely after heating at 9$0^{\circ}C$ for 12 seconds. The optimum pH and temperature for activity of alkaline phosphatase were about pH 9 and 4$0^{\circ}C$, while the optimum pH for activity of acid phosphatase was about pH 5. The maximum activity of alkaline phosphatase was at 189 unit, but maximum activity of acid phosphatase was at 71 unit As the result from above, we observed that alkaline and acid phosphatases funtion mainly in the alimentary tract and vitellaria. Echinostoma hortense performs the parasitism in the intestine of host by using proper isozyme of phosphatase.

• Journal of environmental and Sanitary engineering
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• v.5 no.2
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• pp.103-110
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• 1990

For production of thermophilic and alkaline protease, Bacillus sp. strain AP-5 was isolated from a compost. The production of the protease was reached at maximum for 4 days at $55^{\circ}$ in standing culture. Chitin and Cellulose as carbon source, and Skim Milk as nitrogen source were favorable for the production of the enzyme. Optimal temperature and optimal pH of the enzyme was $55^{\circ}$ and 11, respectively. Metal ion didn't effect on the enzyme activity, the protease was very stable at heat treatment of 30 min at $55^{\circ}$.

• Journal of Veterinary Clinics
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• v.14 no.1
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• pp.65-69
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• 1997

The bone alkaline phosphatase(BALP) in 130 sera of normal dogs were assayed according to the lectin precipitation method of Rosalki and Foo. The serum BALP activities showed a wide variation as $23.27({\pm}14.73)$ IU/L in young dogs from 6weeks to 12 months old and were lower in magnitude as $9.24({\pm}3.36)$ IU/L in elder dogs from 1 years to 6years old. The serum BALP activities in normal dogs were no significant correlation in sex.

• Korean Journal of Microbiology
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• v.24 no.1
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• pp.32-37
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• 1986

In fermentation studies it revealed that Streptomyces sp. SMF 3001 started to synthesize extracellular alkaline protease from early exponential phase of cell growth. The biosynthesis of the alkaline protease was greatly induced by skim milk as a sola nitrogen source and further stimulation was observed under inorganic sulphur limited culture. However, it was found that the biosynthesis was apparently repressed by $NH_4^+$ and free amino acids, specially by cysteine. It was considered that the strain SMF 301 of Streptomyces sp. would produce the alkaline protease for the uptake of sulphur compounds from protein contained in the culture broth.