Purification and Properties of Extracellular Protease of Bacillus sp. 11-4 Isolated from Vietnamese Fish Sause

概要

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Bacillus sp. 11-4 isolated from Vietnamese fish sauce was slightly halophilic and produced some extracellular protease. The proteases from Bacillus sp. 11-4 were purified by ion-exchange chromatography and gel filtration. The major extracellular protease (Protease I) from Bacillus sp. 11-4 was neutral protease, which was 33.5 kDa and pI 7.4. The protease I required Ca ion to expression protease activity. As protease activity was inhivited with chelating reagents such as EDTA and o-phenanthroline, protease I was metallo protease. The protease I that hydrolyzed native collagen, azocoll and specific substrate for collagenase such as FALGPA and z-Gly-Pro-Leu-Gly-Pro·H2O·AcOH was collagenase. The protease I had caseinolytic activity. A molecular mass of protease I differed from other collagenase.
日本食品保蔵科学会の論文