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KMID : 0545120000100030349
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Journal of Microbiology and Biotechnology
2000 Volume.10 No. 3 p.349 ~ p.354
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Isolation of High Yielding Alkaling Protease Mutants of Vibrio metschnikovii Strain RH530 and Detergency Properties of Enzyme
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CHUNG, SO-SUN
SHIN, YONG-UK/KIM, HEE-JIN/JIN, GHEE-HONG/RHO, HYUNE-MO/LEE, HYUNE-HWAN
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Abstract
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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 VAP 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 VAP were investigated to avoid catabolite repression. The combination of 4% wheat gluten meal (WGM), 1.5% cotton seed flour (CSF), and 5% soybean meal (SBM) resulted in the best production when supplemented with 1% NaC1. The VAP showed a resistance to surfactants such as sodium-α-olefin sulfonate (AOS), polyoxy ethylene oxide (POE), and sodium dodecyl sulfate (SDS), yet not to linear alkylbenzene sulfonate (LAS). However, the activity of the VAP was restored completely when incubated with LAS in the presence of POE or Na_2SO_4. The VAP 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℃, but the stability was sharply decreased even after 1 day when incubated at 60℃. A washing performance test with the VAP exhibited it to be a good washing power by showing 51% and 60% activity at 25℃ and 40℃, respectively, thereby indicating that the VAP also has a good detergency at a low temperature. All the results suggest that the VAP produced from the mutant strain KS1 has suitable properties for use in laundry detergents.
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