中性域で働くマサバ カテプシンB様酵素の精製と性状

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  • Purification and characterization of cathepsin B-like enzyme active in neutral pH from the chub mackerel <i>Scomber japonicus</i>
  • チュウセイイキ デ ハタラク マサバカテプシン B ヨウ コウソ ノ セイセイ ト セイジョウ

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As a part of researches for endogenous proteinases, we attempted with purification and characterization of a cysteine protease active in neutral pH from the spleen of chub mackerel Scomber japonicus. The molecular mass of the purified enzyme was estimated to be 35 kDa by gel filtration. In addition, the purified enzyme was detected as two protein bands of 35 and 27 kDa by SDS-PAGE, and N-terminal amino-acid sequences of the former and latter shared high homology with those of single and heavy chains, respectively, of rainbow trout, mouse, and bovine cathepsin B. The optimum pH of the purified enzyme were 7.0 and 7.7, respectively, on Z-Phe-Arg-MCA and Z-Arg-Arg-MCA hydrolyzing activity. The activity was suppressed by cysteine protease inhibitors such as E-64, TLCK, and leupeptin. From these results, the purified enzyme active in neutral pH was considered to be a new type of cathepsin B, which was different from well-known cathepsin B active in acidic conditions. Moreover, myosin heavy chain and actin were hydrolyzed with addition of the enzyme in neutral pH, suggesting that the cathepsin B-like enzyme purified from the spleen of chub mackerel is one of the proteases responsible for post-mortem fish muscle tenderization.

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