Expression of alkaline phosphatase induces rapid and artificial mineralization in specific transformed Escherichia coli

Naoko Ohara, Naoya Oohara, K. Yanagiguchi, S. Yamada, I. L. Viloria, Y. Hayashi

Research output: Contribution to journalArticle

1 Citation (Scopus)

Abstract

Matrix vesicles (MV) having high alkaline phosphatase (ALP) activity act as initiators of biological mineralization. Although bacteria have similar membranous structures to MV, ALP mediated mineralization has not been studied in bacterial cells. Escherichia coli was transformed with a bacterial ALP gene in this study. Recombinant E. coli overproducing ALP induced mineralization through hydrolysis of calcium-glycerophosphatc (Ca-GP). Fourier transform infrared spectroscopy and electron microscopy combined with electron diffraction revealed newly formed hydroxyapatite mineral deposits. These findings suggest that hydrolysis of Ca-GP through ALP induced high Ca and Pi concentrations within bacterial cells followed by complete bacterial mineralization.

Original languageEnglish
Pages (from-to)107-110
Number of pages4
JournalNew Microbiologica
Volume25
Issue number1
Publication statusPublished - Jan 2002
Externally publishedYes

Fingerprint

Alkaline Phosphatase
Escherichia coli
Hydrolysis
Calcium
Fourier Transform Infrared Spectroscopy
Durapatite
Minerals
Electron Microscopy
Electrons
Bacteria
Genes

Keywords

  • Alkaline phosphatase
  • Escherichia coli
  • Fourier transform infrared spectroscopy
  • Mineralization
  • Transformation
  • Transmission electron microscopy

ASJC Scopus subject areas

  • Microbiology
  • Microbiology (medical)

Cite this

Expression of alkaline phosphatase induces rapid and artificial mineralization in specific transformed Escherichia coli. / Ohara, Naoko; Oohara, Naoya; Yanagiguchi, K.; Yamada, S.; Viloria, I. L.; Hayashi, Y.

In: New Microbiologica, Vol. 25, No. 1, 01.2002, p. 107-110.

Research output: Contribution to journalArticle

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