Studies on acylase activity and microorganism. Purification and properties of d-aminoacylase (N-acyl-d-amino acid amidohydrolase) from AAA 6029 (Pseudomonas sp.)

• 亀田 幸雄

• 長谷 哲

• 金友 昭一

• 喜多 洋子

書誌事項

タイトル別名

• Studies on acylase activity and micro-organisms. XXVI. Purification and properties of D-acylase (N-acyl-D-amino-acid amidohydrolase) from AAA 6029 (Pseudomonas sp.).

抄録

AAA 6029 (Pseudomonas sp.) was isolated from soil by using the synthetic medium containing N-benzoyl-D-phenylalanine as a sole source of carbon. The bacteria produce a D-acylase which hydrolyzes N-acyl-D-amino acids. The D-acylase was extracted by means of sonic oscillation and purified by ammonium sulfate fractionation, DEAE cellulose chromatography, and Sephadex G-100 gelfiltration. The purified enzyme was represented about 900 fold purification over the cell free extract. The molecular weight of this enzyme was estimated to be about 45000 by gelfiltration. This enzyme can hydrolyze N-benzoyl and N-acetyl derivatives of the D-form of phenylalanine, methionine, leucine, alanine, and valine. But the acylase can not hydrolyze N-acyl derivatives of L-amino acids.

収録刊行物

• ＣＨＥＭＩＣＡＬ　＆　ＰＨＡＲＭＡＣＥＵＴＩＣＡＬ　ＢＵＬＬＥＴＩＮ

  ＣＨＥＭＩＣＡＬ　＆　ＰＨＡＲＭＡＣＥＵＴＩＣＡＬ　ＢＵＬＬＥＴＩＮ 26 (9), 2698-2704, 1978

  公益社団法人 日本薬学会

キーワード

• D-amino acid

詳細情報

• CRID: 1390001204169498368
• NII論文ID: 110003623359
• NII書誌ID: AA00602100
• DOI: 10.1248/cpb.26.2698
• COI: 1:CAS:528:DyaE1MXit1Wk
• ISSN: 13475223
• ISSN: 00092363
• ISSN: http://id.crossref.org/issn/00092363
• PubMed: 699212
• Web Site: http://www.jstage.jst.go.jp/article/cpb1958/26/9/26_9_2698/_pdf
• Web Site: https://search.jamas.or.jp/link/ui/1979080962
• 本文言語コード: en
• データソース種別:
  • JaLC
  • Crossref
  • PubMed
  • CiNii Articles
• 抄録ライセンスフラグ: 使用不可