• KSBB Journal
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• v.5 no.4
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• pp.411-414
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• 1990

The extraction behavior of an alkaline protease using reversed micelles was investgated. The reversed micellar solution consisted of AOT in isooctane. It was found that distribution of arkaline protease into the organic phase increased at lower pH, lower ionic strength, and higher AOT concentration. When the real fermentation broth was extracted of alkaline protease, an activity yield of 20% and a purification factor of 2.0 were obtained.

• The korean journal of orthodontics
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• v.26 no.4
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• pp.449-454
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• 1996

The propose of this study was to evaluate the difference of cellular activity dependent on intermittent compressive force by determining the alkaline phosphatase activity. Alkaline phosphatase activity was measured on control and experimental groups every 24, 48, 72hours. Experimental groups consisted of continous and intermittent compressive group which were compressed by $300gm/cm^2$ of diaphram pump. The intermittent compressive group was connected by timer which was worked on 10 minutes an off 10 minutes. The results were as follows; 1. The alkaline phosphatase activity between control and experimental groups showed not significant difference at compressed 24 hours. 2. The alkaline phosphatase activity of experimental groups were more increased than control group at compressed 48 hours. 3. The alkaline phosphatase activity of intermittent compressive group showed significant increased to control group. Whereby continuous compressive group showed not significant difference to control at 72 hours. 4. The alkaline phosphatase activity of intermittent compressive group were stringly increased than continuous compressive groups. 5. Between experimental groups and control group no other morphologic changes were detected by microscopic findings.

• Journal of Food Hygiene and Safety
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• v.15 no.2
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• pp.176-178
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• 2000

V parahaemolyticus possessed an extracellular alkaline pretense activity during the stationary growth phase. Various factors such as nitrogen sources, the concentration of NaCl and metal ions were investigated for optimizing the production of alkaline pretense from V. parahaemolyticus ATCC 17802. Among the nitrogen sources tested skim milk showed the distinct increase of the activity and the activity was the highest at 2% in final concentration after 60 hours incubation. The addition of NaCl and metal ions did not increase the alkaline pretense activity. CoC$_2$, CuC1$_2$, and HgCl rather highly inhibited alkaline protease production.

• The Korean Journal of Zoology
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• v.25 no.2
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• pp.71-80
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• 1982

Some properties of alkaline phosphatase, partially purified from the liver of the local Pekin duck, Anas platyrhynchos, were investigated with the following results. 1. Gel-filtration of the duck liver extract indicated the presence of two molecular-weight species of alkaline phosphatase. 2. Electrophoresis of both enzyme preparations suggests the presence of two molecular forms of alkaline phosphatase with different physicochemical characteristics. 3. The liver alkaline phosphatase has an optimum pH of 9.0, and is further activated by $Mg^2+$ but not by $Ca^2+$. 4. The enzyme was relatively heat-labile, and was competitively inhibited by phosphate ions, but uncompetitively inhibited by L-phenylalanine. 5. These results are discussed in comparison with the properties of human and other animal alkaline phosphatases.

• Journal of Korean Society of Water and Wastewater
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• v.17 no.4
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• pp.567-573
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• 2003

The pretreatment process was carried out to solubilize the sewage sludge for enhancing its biodegradability using alkaline treatment, ultrasonic treatment(15kHz), ozone treatment and different combination of these three methods: alkaline followed by ultrasonic as well as ozone, and ultrasonic followed by alkaline. The solubilization efficiency was evaluated based on the SCOD/TCOD ratio and VSS/TS ratio. In results, the proper condition of alkaline treatment was shown as 30meq/l of NaOH, pH 12 and 3hours of reaction time. Solubilization efficiency increased to 17% from initial 2% based on SCOD/TCOD ratio under this condition. In ultrasonic treatment, the higher ultrasonic power, the longer treatment time and the lower sludge volume resulted in higher solubilization respectively. There was a rapid increase in solubilization efficiency after 20 minute, then it was measured as 32% of SCOD/TCOD ratio in 1 hour at a ultrasonic power of 1,300W with 1/sludge. Solubilization efficiencies in combined treatment using alkaline and ultrasonic were 47-53% higher than single treatment at a sonicated time of 1 hour. Ozone treatment followed by alkaline treatment also represented the enhanced solubilization compared to ozone treatment. Therefore, ultrasonic or ozone treatment assisted by alkaline could achieve the short treatment time as well as high solubilizetion efficiency.

• Journal of Aquaculture
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• v.18 no.4
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• pp.245-251
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• 2005

This study was investigated the condition of their maximum activity to assay the enzymes of rotifer, Brachionus rotundiformis의 $\alpha$-amylase, total alkaline Protease, trypsin and TG-lipase activities of rotifer were higher and more sensitive in phosphate-NaOH buffer than Tris-HCl buffer. $\alpha$-amylase, trypsin and TG-lipase activities were appeared the maximum at pH 8.0, and total alkaline protease activity showed the maximum activity at pH 7.0. $\alpha$-amylase activity showed the highest activity at $40^{\circ}C$, and total alkaline protease and trypsin activities were assayed the highest at $55{\~}60^{\circ}C$. However, TG-lipase activity was appeared the highest at $25{\~}30^{\circ}C$. The optimum substrate concentration of enzyme activity of a-amylase, total alkaline protease, rypsin and TG-lipase were $3.5\%$ starch, $\0.6%$ azo-casein, $87.5{\mu}M$ BApNA and 81.2 mM olive oil, respectively. The optimum reaction time of enzyme activity of $\alpha$-amylase, total alkaline protease, trypsin and TG-lipase were increased up to 40, 60, 30 and 25 min., respectively. The data obtained in this study could be used for the digestive enzyme research of rotifer, B. rotundiformis.

• Journal of Sericultural and Entomological Science
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• v.47 no.1
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• pp.36-40
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• 2005

This studies were carried out to develop the new silk degumming method by elelectrolyzed alkaline water on the silk degumming process. Using to this method, it could be collect pure sericin from the degumming water, because the degumming water by elelectrolyzed alkaline water was not contaminated by chemicals including soap. The range of elelectrolyzed alkaline water was pH 11.5 to 11.7 and maintained the first value for 8 days under the cool and closed conditions. The degumming ratio of silk was higher in elelectrolyzed alkaline water(pH 11.5~11.7)than that of soap and alkaline bath. When the pH value of elelectrolyzed alkaline water was adjusted at pH 11.0, the degumming ratio of silk was similar to that of soap and alkaline degumming. After degumming the pH value of degumming water decreased largely in the elelectrolyzed alkaline water compared to that of soap and alkaline bath. The tenacity and elongation of degummed silk by elelectrolyzed alkaline water was almost same those of soap and alkaline degumming for 90 min.

• Microbiology and Biotechnology Letters
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• v.6 no.1
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• pp.33-40
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• 1978

Immobilization of alkaline protease was investigated by absorbing the enzyme on adsorbents. Alkaline protease was adsorbed on silica gel selected as a carrier to immobilize the enzyme. In this study, properties of the immobilized enzyme were compared with those of the soluble enzyme. 1) The optimum pH (10.0) of the enzyme was not changed, but the activity was increased at alkaline pH by immobilization. 2) The optimum temperature of the immobilized enzyme was shifted from 50$^{\circ}C$ to 45$^{\circ}C$, while the temperature-activity Profile became broader than those of the soluble enzyme. 3) The pH stability of the immobilized enzyme was significantely increased at pH 4.0, althouth it did not change in the neutral and alkaline pH region. 4) The heat stability of the enzyme was enhanced in the temperature range of 55$^{\circ}C$∼65$^{\circ}C$ by the immobilization. 5) The immobilized enzyme retained 40％ of its original activity after repetitive use for 6 times. 6) The enzyme stability was greately improved for a prolonged storage at 4$^{\circ}C$.

• Microbiology and Biotechnology Letters
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• v.19 no.1
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• pp.1-7
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• 1991

A bacterial strain No.71, which produced alkaline protease, was isolated from soil and identified to the genus Bacillus. With the successive mutation, a mutant strain No. M-71, having high alkaline protease productivity, was obtanined from the parental strain No 71. Alkaline protease productivity of mutant strain No. M-71 was about 50 times as much as that of the parental strain No.71. The enzyme preparations showed strong activities toward casein, the optimum pH being 11.0 and the optimum temperature about $55^{\circ}C$.

• Journal of Korea Technical Association of The Pulp and Paper Industry
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• v.36 no.1
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• pp.24-29
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• 2004

Alkaline cellulolytic enzymes from cultured medium of Coprinus cinereus 2249 were purified with gel and ion-exchange chromatography and characteristics of those enzyme proteins were investigated. A fiber length distribution and a crystallinity of cellulose and sugar composition of enzyme treated Mixed Office Wastepaper(MOW) and Unbleached Kraft Pulp(UKP) were analysed. The conclusion could summarized as follows; \circled1 Alkaline and acidic, endo- and exo-glucanases were purified from cultured medium of Coprinus cinereus 2249. \circled2 The approximate molecular weight of alkaline endo-glucanase was 42 kDa, and also that of alkaline exo-glucanase was 50 kDa. A fiber length distribution and a crystallization of cellulose and sugar composition of enzyme treated MOW and UKP were not so much changed with original paper and pulp.