• Korean Journal of Food Science and Technology
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• v.2 no.2
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• pp.38-42
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• 1970

The crude enzyme, tamylase, was produced by cultivating the Bacillus subtilis on wheat bran. It is composed of amylase and protease, and can be used as an additive material to the synthetic detergent, Suny which is manufactured by Ae-kyung Oil and Fat Co. Amylase activity of the enzyme as an additive material to the synthetic detergent; 1. is decreased by increasing the amount of detergent. But inhibitory rate under the practical used concentration of detergent is less than ten percents. 2. have optimal temperature at $ 40^{\circ}C$. 3. have optimal pH of substrate on pH $5{\sim}6.5$. 4. is inhibited by $Fe^{+++}$. When enzyme and detergent are mixed both as powder, the enzyme is good for storage. Proteolytic activity is good at the practical used concentration of the detergent, but it is inhibited by strong concentration.

• The Microorganisms and Industry
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• v.13 no.3
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• pp.39-41
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• 1987

인간이 효소의 작용을 이용한 것은 꽤 오래된 일이나 실제로 효소라는 생명체내의 촉매를 자세히 알고 공업적으로 이용하기 시작한 전환점이라 할 수 있는 것은 지금부터 약 20년전 남짓의 효소를 세제공업에 이용하기 시작한 것이라 할수있다. 그후 전분산업등 효소를 사용하는 사업체는 급진적으로 증가하기 시작하였으며 여러분야에서 품질향상과 경제적 제품 생산을 위해, 그리고 의학계에서 임상용으로 또는 분석용도 생산되어 사용디고 있으며 그수는 앞으로도 계속하여 늘어날 추세에 있다.

• The Microorganisms and Industry
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• v.20 no.3
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• pp.23-25
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• 1994

효소가 산업적 의미를 갖게 되는 시작은 1884년 네덜란드의 Christian Hansen이 송아지의 위에서 rennet를 추출하여 사용함에 따라서 시작되었고, 이후, 일본인 Takamine가 1894년 Koji 배양법에 의해서 곰팡이 Amylase를 상업화하면서 미생물을 이용한 효소생산이 성공되어서 대량생산이 가능하게 되었다. 이후, 20세기에 들면서 독일의 Otto Rohm에 의해서 피혁가공 및 세제에의효소이용, 1911년 미국의 Leo Waltersten이 효소를 이용한 Chill-proofing beer의 개발 등으로 효소의 이용용도가 식품에서 환경공업으로 확대되었고 효소의 산업적 수요가 확대됨에 따라서 이에 따른 막대한 연구투자가 이루어져 비로소 효소산업이 태동하게 되었다.

• Journal of the Korean Society of Clothing and Textiles
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• v.26 no.7
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• pp.1085-1092
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• 2002

Changes in laundering habits and the efficacy claims made for oxygen bleach added to detergents necessitate a deeper investigation into the testing of the washing efficacy of detergents and washing process. The effect of the addition of a sodium percarbonate and bleach activator TAED to an enzyme containing detergent on the soil removal and antimicrobial properties were investigated with the measuring of residual H$_2$O$_2$. The addition of sodium percarbonates to enzyme containing detergent lowered the soil removal of EMPA 116 cloth. But sodium percarbonates had greater effects on that of colored stained cloths such as EMPA 115 and artificially soiled with wine and red pepper while they were presoaked at 20$^{\circ}C$ or higher for So minutes or longer. Most of hydrogen peroxide was remained after washing. Over 99.9% of Staphylococcus aureus on the cotton cloth was removed in every washing solutions, but the cloth washed with enzyme containing detergent or detergent with oxygen bleach didn't show the antimicrobial property.

• Applied Biological Chemistry
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• v.43 no.3
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• pp.169-173
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• 2000

For the development of enzyme detergent capable of effectively washing at low temperature, a bacterium producing alkaline protease was isolated from soil samples, and properties of the enzyme were investigated. The selected strain was Gram negative, rod shape$(0.6{\sim}0.7{\times}1.3{\sim}2.6\;{\mu}m\;in\;size)$ and motile. It had the degradation activity of aesculin, gelatin and casein, and was catalase-positive. The cell wall components was meso-DAP, and G+C mole contents was 43.3%. From these results, the strain was identified as Acinetobacter sp. KN-27. The activity of alkaline protease by this strain peaked with 3,300 D.U/mL after 36 hours in the liquid culture at $40^{\circ}C$. The optimal pH and temperature of the enzyme were pH 9 and $60^{\circ}C$, respectively. Alkaline protease produced by Acinetobacter sp. KN-27 has shown two active bands on the electrophoresis of native gel.

• Korean Journal of Microbiology
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• v.54 no.1
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• pp.60-68
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• 2018

A cold-active and alkaline serine protease (Pro21717) was partially purified from the Antarctic marine bacterium Pseudoalteromonas arctica PAMC 21717. On a zymogram gel containing skim milk, Pro21717 produced two distinct clear-zones of approximately 37 kDa (low intensity) and 74 kDa (high intensity). These were found to have identical N-terminal sequences, suggesting they arose from an identical precursor and that the 37 kDa protease might homodimerize to the more active 74 kDa form of the protein. Pro21717 displayed proteolytic activity at $0-40^{\circ}C$ (optimal temperature of $40^{\circ}C$) and maintained this activity at pH 5.0-10.0 (optimal pH of 9.0). Notably, relative activities of 30% and 45% were observed at $0^{\circ}C$ and $10^{\circ}C$, respectively, in comparison to the 100% activity observed at $40^{\circ}C$, and this enzyme showed a broad substrate range against synthetic peptides with a preference for proline in the cleavage reaction. Pro21717 activity was enhanced by $Cu^{2+}$ and remained stable in the presence of detergent surfactants (linear alkylbenzene sulfonate and sodium dodecyl sulfate) and other chemical components ($Na_2SO_4$ and metal ions, such as $Ba^{2+}$, $Mg^{2+}$, $Ca^{2+}$, $Zn^{2+}$, $Fe^{2+}$, $K^+$, and $Na^{2+}$), which are often included in commercial detergent formulations. These data indicate that the psychrophilic Pro21717 has properties comparable to the well-characterized mesophilic subtilisin Carlsberg, which is commercially produced by Novozymes as the trademark Alcalase. Thus it has the potential to be used as a new additive enzyme in laundry detergents that must work well in cold tap water below $15^{\circ}C$.

• Biomedical Science Letters
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• v.6 no.3
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• pp.209-221
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• 2000

The purpose of this study was to investigate the practical availability of pretense production that can be used at home after isolating Serratia sp.2000-1 which produced extracellular pretense from clinical specimen. Basic production conditions and partial enzymatic characteristics of pretense produced by Serratia sp. 2000-1 was as follows: The kind and concentration of carbohydrate, nitrogen and metal salts for optimal enzyme production condition were each identified as the concentration of 1.5% glucose, 2.0% CSP, and 0.1% CaCl$_2$, and the optimal temperature, time and initial pH for culture were each 3$0^{\circ}C$, 72 hours, and pH 8.0. The final enzymatic yeild that was purified by 3 steps with ammonium sulfate precipitation (45~80%), DEAE-cellulose column chromatography, and Sephadex G-200 gel chromatography was 14.4%, and enzyme inactivity rate increased approximately 291314s. The optimal temperature and pH for purified pretense activity were 35$^{\circ}C$ and pH 7.0~8.0, and purified pretense activity was relatively stable by 4$0^{\circ}C$ at pH 6~10 for 30 min, however heating at 6$0^{\circ}C$ for 30 min, it liminated detectable pretense activity. The pretense activity was activated by $Mg^{2+}$, $Ba^{2+}$, $Ca^{2+}$, Mn$^{2+}$, but inactiviaed by Hg$^{2+}$, Ag$^{2+}$, Cu$^{2+}$, and the pretense activity was inhibited strongly by SDS among enzyme activity inhibitors. Further study is required to evaluate the practical availability of pretense production that can be used at home by isolating Serratia sp. from more clinical specimen and examining pretense more in details.

• Journal of Life Science
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• v.16 no.4
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• pp.555-560
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• 2006

A bacterium producing novel lipolytic enzyme was isolated from house sewage and identified as Acinetobacter sp. BD5 based on physiological characterization and 16S rDNA sequencing. The lipolytic activity of Acinetobacter sp. BD5 was tested using an EL agar medium and CE agar medium supplemented with 1% tributyrin and olive oil, respectively. The formation of a clear zone around the colony was detected by agar medium supplemented with 1% tributyrin and olive oil, respectively and Acinetobacter sp. BD5 formed powder-like zone around the colony on LB agar medium containing Tween 20. The quantitative lipolytic activity was determined by using p-NP butyrate as substrate. Acinetobacter sp. BD5 secreted the lipolytic enzyme during exponential growth phase, reaching a maximum amount after 6 hours of incubation. The lipolytic enzyme was found to be optimally active at $60^{\circ}C$ and retained more than 70% at $70-80^{\circ}C$. It displayed a high degree of activity in a pH of 7.0 to 10.6, with an optimal pH of 9.0.

• Microbiology and Biotechnology Letters
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• v.25 no.1
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• pp.51-55
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• 1997

To utilize the alkaline protease produced by Halomonas sp. ES-10 as an enzyme detergent, the crude enzyme was obtained by methanol precipitation and lyophilization. And it was processed to coated enzyme.The best mixing ratio of components such as coated enzyme, builders, actives, fillers and adjuvants on detergency was examined, and temperature and pH influencing detergency were also tested. Detergency test 0.15% detergent solution was carried out on EMPA test cloth #116 with shaking(90 rpm) for 10 min after 30 min of pretreatment. The detergent which contained coated-enzyme 1%, Zeolite 4A 20%, Tween 80 1. 5%, sodium borate 30%, sodium meta silicate 7.5% and water 40% showed about 90% of washing efficiency at 40$\circ $C and pH 10.0.

• Textile Coloration and Finishing
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• v.10 no.6
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• pp.55-66
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• 1998

In order to investigate the detergency effects of various detergents to stained polyester & cotton fabric with solid soils such as carbon black, liquid paraffin and fat, the optimum washing conditions according to the types of washing agent, the assesment of detergency effect by the measurement of reflectance after and before washing were studied. The detergency effect of various detergents to stained polyester and cotton fabric increased by using the mixtures of bleaching and enzyme detergent. In order to obtain the excellent detergency effect, 2-step treatment, the pre-washing with bleaching agent and bleaching-enzyme mixture detergent treatment is preferred. In comparison of the detergency to polyester and cotton fabric, it is assumed that the detergency to polyester stained fabric was superior than that to cotton stained fabric because of the difference of adhesive force between soil material and fabric in preparing solid stained fabric.