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KMID : 0364820180540010060
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Korean Journal of Microbiology
2018 Volume.54 No. 1 p.60 ~ p.68
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Characterization of an Antarctic alkaline protease, a cold-active enzyme for laundry detergents
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Park Ha-Ju
Han Se-Jong
Yim Joung-Han
Kim Doc-Kyu
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Abstract
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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°C (optimal temperature of 40°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°C and 10°C, respectively, in comparison to the 100% activity observed at 40°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 Cu2+ and remained stable in the presence of detergent surfactants (linear alkylbenzene sulfonate and sodium dodecyl sulfate) and other chemical components (Na2SO4 and metal ions, such as Ba2+, Mg2+, Ca2+, Zn2+, Fe2+, K+, and Na2+), 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°C.
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KEYWORD
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alkaline protease, Antarctic, cold-active, laundry detergent
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