Isolation of alkalophilic nylon-oligomer-degrading bacterium: Cloning and sequencing analysis of 6-aminohexanoate-oligomer hydrolase

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  • YASUHIRA KENGO
    Department of Materials Science and Chemistry, Graduate School of Engineering, University of Hyogo
  • TAKEO MASAHIRO
    Department of Materials Science and Chemistry, Graduate School of Engineering, University of Hyogo
  • NEGORO SEIJI
    Department of Materials Science and Chemistry, Graduate School of Engineering, University of Hyogo

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  • アルカリ性ナイロンオリゴマー分解菌の分離：6－アミノカプロン酸オリゴマー加水分解酵素遺伝子のクローニングと配列分析
  • アルカリセイ ナイロン オリゴマー ブンカイキン ノ ブンリ 6 アミノカプロンサン オリゴマー カスイ ブンカイ コウソ イデンシ ノ クローニング ト ハイレツ ブンセキ

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Abstract

We isolated alkalophilic bacterium, Agromyces sp. KY5R, which degrades 6-aminohexanoate (Ahx)-oligomer (by-product of nylon-6 manufacture, designated as nylon-oligomer), from activated sludge of sewage disposal plant. The strain KY5R exhibited good growth on LB-plate containing insoluble Ahx-oligomer (pH10), and produced clear zone by hydrolysis of the oligomers. 6-Aminohexanoate-oligomer hydrolase from KY5R (A-EIII) had optimum pH at 7.5-8.0. This value was 0.5 point higher than the optimum pH of P-EIII (EIII encoded on plasmid pOAD2 in Arthrobacter sp. KI72). In addition, thermostability test revealed that the A-EIII was stable up to 60 ℃, while the P-EIII was stable up to 50 ℃ under the same condition. Cloning and sequencing analysis demonstrated that the amino acid sequence of the two EIII enzymes differs only at 5 positions among 355 amino acid residues. These results suggest that at least one of the five alterations affects the differences in the enzyme characteristics.

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