• Title/Summary/Keyword: Linear alkylbenzene sulfonate

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Purification of Water Contaminated with Synthetic Detergent by a Wild Strain of Oenanthe javanica (미나리에 의한 합성세제에 오염된 물의 정화효과)

  • 김종규
    • Journal of Food Hygiene and Safety
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    • v.17 no.1
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    • pp.1-7
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    • 2002
  • This study was performed to investigate the possibility of water purification by a wild train of Oenanthe javanica DC. Three commercially available dishwashing detergents and a standard surfactant, linear alkylbenzene sulfonate (LAS), were used for this study. The experiment was done in 1.5 ι transluscent aquariums. The plants were distributed into various concentrations of detergents and various kinds of detergent in the separate aquariums. The wet weight of the plants was significantly decreased (p<0.05), and the visual vitality of the plants also decreased in 2 days. The higher the concentration of detergent was, and the more time the plants were exposed to the detergents, the more decrease of growth was observed. The pH value of the culture media decreased in 2 days and in 4 days, then slightly increased in 6 days. However, the pH value of the media did not return to the initial neutral level of pH in 6 days. The pH value of the culture media containing the LAS remarkably increased in 6 days and increased to a neutral pH value in 18 days (p<0.01) as the pH of the other culture media. The chemical oxygen demand (COD) of the culture media gradually increased over the 4 days. A decrease of COD was observed in 6 days, but no tendency was observed between 12 and 18 days. The detergent in the culture media was highly significantly decreased in 2 days (p<0.01) and gradually decreased after this. After 6 days the remaining detergent was 12.4∼23.7% from the various levels of initially added concentration, and 22.4 ∼34.2% from the flour kinds of detergents. These results show that the reduction of detergent was caused by Oenanthe javanica and the effect was significant during the first 6 days when the plants were still growing well. These results indicate that the plant purifies contaminated water for several days and the effect could be variable according to the level of contamination and the environment in which the plant grows.

Isolation of High Yielding Alkaline Protease Mutants of Vibrio metschnikovii Strain RH530 and Detergency Properties of Enzyme

  • Chung, So-Sun;Shin, Yong-Uk;Kim, Hee-Jin;Jin, Ghee-Hong;Rho, Hyune-Mo;Lee, Hyune-Hwan
    • Journal of Microbiology and Biotechnology
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    • v.10 no.3
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    • pp.349-354
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    • 2000
  • Abstract A facultative alkalophilic gram-negative Vibrio metschnikovii strain RH530, isolated from the wastewater, produced several alkaline proteases (VAP) including six alkaline serine proteases and a metalloprotease. From this strain, high yielding YAP mutants were isolated by NTG treatment. The isolated mutant KS1 showed nine times more activity than the wild-type after optimization of the culture media. The production was regulated by catabolite repression when glucose was added to the medium. The effects of several organic nitrogen sources on the production of the YAP were investigated to avoid catabolite repression. The combination of 4% wheat gluten meal (WGM), 1.5% cotton seed flour (eSF), and 5% soybean meal (SBM) resulted in the best production when supplemented with 1% NaCl. The YAP showed a resistance to surfactants such as $sodium-{\alpha}-olefin$ sulfonate (AOS), polyoxy ethylene oxide (POE), and sodium dodecyl sulfate (SDS), yet not to linear alkylbenzene sulfonate (LAS). However, the activity of the YAP was restored completely when incubated with LAS in the presence of POE or $Na_2SO_4$. The YAP was stable in a liquid laundry detergent containing 6.6% SLES (sodium lauryl ether sulfate), 6.6% LAS, 19.8% POE, and stabilizing agents for more than two weeks at $40^{\circ}C$, but the stability was sharply decreased even after 1 day when incubated at $60^{\circ}C$. A washing performance test with the YAP exhibited it to be a good washing power by showing 51 % and 60% activity at $25^{\circ}C{\;}and{\;}40^{\circ}C$, respectively, thereby indicating that the YAP also has a good detergency at a low temperature. All the results suggest that the YAP produced from the mutant strain KSI has suitable properties for use in laundry detergents.rgents.

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Acute Toxicity of Oncheon Stream Water to the Sea Urchin, Hemicentrotus pulcherrimus (말똥성게에 대한 온천천수의 급성독성)

  • LEE Suk-MO;PARK Chung-Kil
    • Korean Journal of Fisheries and Aquatic Sciences
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    • v.17 no.5
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    • pp.414-422
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    • 1984
  • This research was conducted to evaluate the effect of polluted Oncheon Stream on the marine organisms in the Suyeong Bay. Water quality and 96 hr acute toxicity to the sea urchin, Hemicentrotns pulcherrimus by recirculation bioassay were examined from Feb. 20 to Apr. 15, 1984. The 96 hr $50\%$ effective concentration($EC_{50}$) on the attachment of the podia of the sea urchin was observed to occur at test concentrations between 40.0 and $51.0\%$ (v/v), and safe concentrations may be assumed to be within 4.0 and $5.1\%$. These values indicate as follows : 1. Oncheon Stream was extremely polluted by oxygen-demanding wastes and synthetic organic compounds from sewage and industrial waste water. 2. Linear alkylbenzene sulfonate(LAS) which has not been yet included in water quality standard was discharged above the TLm. 3. Unknown toxicity may be synergy among complex substances. In consideration of the relationship between COD values of Oncheon Stream and dilution water, the effect of toxicity of Oncheon Stream water reached to the area of the Suyeong Bay where the COD value was found to be 12.2 ppm.

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Characterization of an Antarctic alkaline protease, a cold-active enzyme for laundry detergents (세탁세제 첨가용 효소 개발을 위한 남극 해양세균 유래 저온성 단백질분해효소의 특성 연구)

  • Park, Ha Ju;Han, Se Jong;Yim, Joung Han;Kim, Dockyu
    • 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 $15^{\circ}C$.