Purification and properties of β-1,4-xylanases 2 and 3 from aeromonas caviae w-61

Nguyen Viet Dung, Sopit Vetayasuporn, Yoshiyuki Kamio, Naoki Abe, Jun Kaneko, Kazuo Izaki

Research output: Contribution to journalArticle

Abstract

A system of multiple xylaiiase enzymes was detected in the culture supernatant of Aeromonas caviae W-61. Among the detected xylanases, two β-l,4-xylanases (l,4-β-D-xylan xylanohydrolases, EC 3.2.1.8), designated xylanases 2 and 3, have been purified to homogeneity, by using ultrafiltration, ammonium sulfate precipitation, DEAE-Toyopearl 650M, CM-Sephadex C-50, and high-pressure liquid chromatographies. Endoxylanase 2 was a basic protein of 41 kDa, and endoxylanase 3 was an acidic protein of 58 kDa. The two xylanases had different pH and temperature optima, as well as thermal stabilities. The two purified enzymes had no activity on β-1,3-xylan, cellulose, carboxymethyl cellulose, or water-soluble starch. Various xylo-oligosaccharides such as xylotriose, xylotetraose, xylopentaose, xylohexaose, and higher oligosaccharides were formed, and only a small amount of xylobiose was detected as the hydrolysis products of oat spelt xylan by endoxylanase 2. Endoxylanase 3 released higher xylo-oligosaccharides as main products with very small amounts of xylotetraose and xylopentaose.

Original languageEnglish
Pages (from-to)1708-1712
Number of pages5
JournalBioscience, Biotechnology and Biochemistry
Volume57
Issue number10
DOIs
Publication statusPublished - 1993 Jan 1

ASJC Scopus subject areas

  • Biotechnology
  • Analytical Chemistry
  • Biochemistry
  • Applied Microbiology and Biotechnology
  • Molecular Biology
  • Organic Chemistry

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