Purification and partial characterization of an acid phosphatase from the body wall of sea cucumber Stichopus japonicus

Bei Wei Zhu, Jian Wei Yu, Zongshen Zhang, Da Yong Zhou, Jing Feng Yang, Dong Mei Li, Yoshiyuki Murata

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14 Citations (Scopus)


A high molecular weight (HMW) acid phosphatase from the body wall of sea cucumber Stichopus japonicus was purified to homogeneity by a combination of anion exchange chromatography, gel filtration chromatography and high performance liquid chromatography (HPLC). The enzyme was purified 19.3-fold with a total yield of 1.2%. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) of the purified enzyme showed a single protein band of MW 147.9 kDa. The enzyme displayed maximum activity at pH 4.0 and 50 °C with p-nitrophenyl phosphate as substrate. The enzyme activity appeared to be stable over pH 2.0-5.0 and up to 40 °C. The enzyme activity was enhanced slightly by Mg2+, whereas inhibited strongly by Cu2+ and Zn2+. The enzyme hydrolyzes several phosphate esters, suggesting a probable non-specific nature. The amino acid sequences of three segments of the purified enzyme were analyzed by mass spectroscopy, which did not have any homology with previously described acid phosphatase.

Original languageEnglish
Pages (from-to)875-879
Number of pages5
JournalProcess Biochemistry
Issue number8
Publication statusPublished - Aug 1 2009



  • Acid phosphatase
  • Amino acid sequences
  • Autolysis
  • Characterization
  • Purification
  • Sea cucumber (Stichopus japonicus)

ASJC Scopus subject areas

  • Bioengineering
  • Biochemistry
  • Applied Microbiology and Biotechnology

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