Purification and Characterization of an Autolysin of Bacillus polymyxa var. colistinus Which is Most Active at Acidic pH
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概要
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Bacillus polymyxa var. colistinus autolysin was purified from a 1-l culture by ammonium sulfate fractionation, gel filtration, non-binding with a DEAE-Sepharose resin, and CM-Sepharose column chromatography. SDS-polyacrylamide gel (containing B. polymyxa var. colistinus cell wall) electrophoresis of the purified autolysin gave a single band at an M_r of 23kDa exhibiting cell wall hydrolytic activity. Identification of the specific substrate bond cleaved by the autolysin indicated that the enzyme is an N-acetylmuramoyl-L-alanine amidase. The optimal temperature for the enzyme reaction was 40-50℃, and the optimal pH was 4.0,which is extraordinarily unique for amidases.
- 社団法人日本生物工学会の論文
- 1997-05-25
著者
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Sekiguchi Junichi
Department of Applied Biology, Faculty of Textile Science and Technology, Shinshu University
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Kawahara Shinji
Shiraoi Pharmaceutical Plant Asahi Chemical Industry Co. Ltd.
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UTSUNOMIYA CHIE
Department of Applied Biology, Faculty of Textile Sciencen and Technology, Shinshu University
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ISHIKAW SHU
Department of Applied Biology, Faculty of Textile Science and Technology, Shinshu University
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Ishikaw Shu
Department Of Applied Biology Faculty Of Textile Science And Technology Shinshu University
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Utsunomiya Chie
Department Of Applied Biology Faculty Of Textile Sciencen And Technology Shinshu University
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ISHIKAWA Shu
Department of Applied Biology, Faculty of Textile Science and Technology, Shinshu University
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Sekiguchi Junichi
Department Of Applied Biology Faculty Of Textile Science And Technology Shinshu University
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