α-L-arabinofuranosidase from cell walls of Japanese pear fruits

Akira Tateishi, Yoshinori Kanayama, Shohei Yamaki

Research output: Contribution to journalArticle

36 Citations (Scopus)

Abstract

Cell wall-bound glycosidase activities were measured in pre-ripe and ripe fruits of Japanese pears (Pyrus serotina Rehd. var. culta. cv. Hosui). α-L-Arabinofuranosidase (EC. 3.2.1.55) activity increased dramatically with fruit ripening and its activity was assayed during fruit development and ripening. After the fruit enlargement stage, cell wall-bound α-L-arabinofuranosidase activity increased 15-fold with fruit ripening. The enzyme was solubilized from cell walls using the chelator trans-1,2-cyclohexanediamine-N,N,N′,N′-tetraacetic acid and the solubilized enzyme purified using DEAE-cellulose, hydroxyapatite, Mono Q and Sephadex G-100 chromatography. The purified enzyme was a Mr 42 000 monomer on SDS-PAGE. Optimum pH activity was 5.0 and the Km value was 34 mM for p-nitrophenyl-α-L-arabinofuranoside.

Original languageEnglish
Pages (from-to)295-299
Number of pages5
JournalPhytochemistry
Volume42
Issue number2
DOIs
Publication statusPublished - 1996 Jan 1
Externally publishedYes

Keywords

  • Cell walls
  • Japanese pear
  • Purification
  • Pyrus serotina
  • Ripening
  • Rosaceae
  • α-L-arabinofuranosidase

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Plant Science
  • Horticulture

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