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KMID : 0364820130490010078
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Korean Journal of Microbiology
2013 Volume.49 No. 1 p.78 ~ p.82
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Characterization of Extracellular Protease Secreted from Chryseobacterium sp. JK1
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Lee Yu-Kyong
Oh Ji-Sung
Roh Dong-Hyun
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Abstract
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A novel Chryseobacterium sp. JK1 strain isolated from soil had been reported that this isolate produced large
amount of extracellular protease at mesophilic temperature in previous study. The optimal temperature and pH of
extracellular protease were 40℃ and 7.0, respectively, showing narrow range of optimal temperature and relatively
broad activity from pH 6.0 to 9.0. In addition, the protease showed greatest activity against skim milk and lowest
against bovine serum albumin (BSA). The protease strongly inhibited by ethylenediaminetetraacetic acid (EDTA),
ethylene glycol tetraacetic acid (EGTA) or phenylmethylsulfonyl fluoride (PMSF), and addition of cation Ag+ or
Cu2+, and slightly inhibited by Al3+. No significant inhibition was found with pepstatin, and addition of cation, K+,Ca2+, Na+
, Fe2+ or Mg2+. On the contrary, protease was enhanced by addition of divalent cation Mn2+ (5 mM).Zymography analysis of concentrated culture supernatant revealed two major bands at 67 and 145 kDa. These results suggest that Chryseobacterium sp. JK1 strain produced extracellular neutral serine proteases which could apply in
food industry
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KEYWORD
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Chryseobacterium sp. JK1, extracellular protease, optimal conditions
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