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Updated: Jun 25, 2026

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Purification and characterization of two soluble acid invertase isozymes from Japanese pear fruit.

Hiroshi Hashizume1, Koji Tanase, Katsuhiro Shiratake

  • 1Laboratory of Horticultural Science, Graduate School of Bioagricultural Sciences, Nagoya University, Chikusa, Nagoya 464-8601, Japan.

Phytochemistry
|April 25, 2003
PubMed
Summary

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Researchers purified two soluble acid invertase isozymes (AIV I and AIV II) from Japanese pear fruit. These enzymes exhibit distinct properties, with AIV I being an 80 kDa monomer and AIV II showing susceptibility to cleavage.

Area of Science:

  • Biochemistry
  • Enzymology
  • Plant Science

Background:

  • Soluble acid invertase (EC 3.2.1.26) plays a crucial role in plant carbohydrate metabolism.
  • Understanding the properties of invertase isozymes in fruit is essential for comprehending fruit development and ripening.

Purpose of the Study:

  • To purify and characterize two soluble acid invertase isozymes (AIV I and AIV II) from Japanese pear fruit.
  • To determine the biochemical and physical properties of these purified isozymes.

Main Methods:

  • Enzyme purification using ammonium sulfate precipitation, DEAE-Sephacel, Concanavalin A-Sepharose, hydroxyapatite, and Mono Q HR 5/5 chromatography.
  • Enzyme activity assays and SDS-PAGE for protein characterization.
  • Determination of kinetic parameters (Km) and optimal pH.

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Main Results:

  • Two soluble acid invertase isozymes, AIV I and AIV II, were successfully purified.
  • Purified AIV I exhibited a specific activity of 2670 nkat/mg protein and was an 80 kDa monomer.
  • AIV II, with a specific activity of 2340 nkat/mg protein, appeared monomeric but was prone to cleavage into 52 kDa and 34 kDa polypeptides. Both isozymes had a Km for sucrose of approximately 3.33-4.58 mM and an optimal pH of 4.5.

Conclusions:

  • Japanese pear fruit contains at least two distinct soluble acid invertase isozymes with different molecular properties.
  • The characterized kinetic and physical properties provide insights into the enzymatic function of soluble acid invertase in pear fruit.