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KMID : 0545119950050010026
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Journal of Microbiology and Biotechnology
1995 Volume.5 No. 1 p.26 ~ p.30
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Internal Cleavage of Bacillus subtilis BSE 616 Endo-β-1, 4-glucanase expressed in Escherichia coli
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Kim, Hoon
Kim, Sungmin F/Ahn, Dong Ho/Lee, Jin Ho/Pack, Moo Young
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Abstract
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The cytoplasmic endo-β-1,4-glucanase (endoglucanase) was purified from cell extracts of Escherichia coli (pBS1) transformant carrying the Bacillus subtilis endo-β-1,4-glucanase gene after full growth, and its molecular weight was found to be 52 kilodaltons (kDa). The endo-β-1,4-glucanase isolated from the periplasmic space was smaller than 52-kDa cytoplasmic enzyme. The 52-kDa endoglucanase was found to be cleaved in the periplasm and finally converted to 34.5-kDa protein. Small amounts of both 52-kDa and 34.5-kDa proteins were secreted into the culture broth. The cleavage took place in the C-terminal portion of the enzyme. The N-terminal amino acid residues of both 52-kDa and 34.5-kDa enzymes were determined to be the same, Ala, the 30th residue of the primary translation product. Cleavage of the C-terminal portion showed to have no significant effect on the basic enzyme properties.
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