Purification and properties of phospholipase D from Actinomadura sp. strain No. 362.

• KOKUSHO Yoshitaka

  Tokyo Research Laboratory, Meito Sangyo Co., Ltd.

• KATO Shigeaki

  Tokyo Research Laboratory, Meito Sangyo Co., Ltd.

• MACHIDA Haruo

  Tokyo Research Laboratory, Meito Sangyo Co., Ltd.

• IWASAKI Shinjiro

  Tokyo Research Laboratory, Meito Sangyo Co., Ltd.

抄録

An extracellular phospholipase D from Actinomadura sp. Strain No. 362 was purified about 430-fold from the culture filtrate. The purified enzyme preparation was judged to be homogeneous on polyacrylamide gel electrophoresis. The molecular weight and isoelectric point of the enzyme were estimated to be about 50, 000-60, 000 and 6.4, respectively. The enzyme was most active at pH 5.5 and 50°C in the presence of Triton X-100, but showed the highest activity at pH 7.0 and 60-70°C in its absence. The enzyme was stable up to 30°C at pH 7.2 and also stable in the pH range of 4.0 to 8.0 on 2hr incubation at 25°C. With regard to substrate specificity, this enzyme hydrolysed lecithin best among the phospholipids tested. It was activated by Fe³⁺, A1³⁺, Mn²⁺, Ca²⁺, diethyl ether, sodium deoxycholate and Triton X-100, but was inhibited by cetyl pyridinium chloride and dodecylsulfate.

収録刊行物

• Agricultural and Biological Chemistry

  Agricultural and Biological Chemistry 51 (9), 2515-2524, 1987

  公益社団法人 日本農芸化学会

キーワード

• General Agricultural and Biological Sciences
• General Biochemistry, Genetics and Molecular Biology

詳細情報

• CRID: 1390001206465832832
• NII論文ID: 130000024891
• DOI: 10.1271/bbb1961.51.2515
• COI: 1:CAS:528:DyaL1cXhvVahtg%3D%3D
• ISSN: 18811280
• ISSN: 00021369
• ISSN: http://id.crossref.org/issn/00021369
• 本文言語コード: en
• データソース種別:
  • JaLC
  • Crossref
  • CiNii Articles
• 抄録ライセンスフラグ: 使用不可