Isolation and properties of a thermostable endoglucanase from a thermophilic mutant strain of Tielavia terrestris

Edisher G. Kvesitadze, Tamara B. Lomitashvili, Maia P. Khutsishvili, Raphael Lamed, Edward A. Bayer

Research output: Contribution to journalArticlepeer-review

Abstract

A heat-stable enzyme was isolated from the cellulase complex of a thermophilic strain of the micromycete Thielavia terrestris. The purified enzyme exhibited both endoglucanase and xylanase activities and had a mol mass of 69,000 Daltons and an isoelectric point of 6.4. When the cells were grown at 48°C, the initial activity of the purified enzyme using carboxymethylcellulose as a substrate was 150 nkat/mg and the Michaelis constant was 6.6 g/L. The heat stability of the enzyme was high, losing only 20% of the initial activity after a 6-h incubation at 65 °C. When cultures were grown on microcrystalline cellulose and xylose was added after 48 h of growth, endoglucanase and xylanase activities were more than doubled. Similar increases in these activities were observed by growing the cultures on straw.

Original languageEnglish
Pages (from-to)137-143
Number of pages7
JournalApplied Biochemistry and Biotechnology
Volume50
Issue number2
DOIs
StatePublished - Feb 1995

Keywords

  • Thielavia terrestris (Allesheria terrestris)
  • cellulase complex
  • endoglucanase
  • thermostability
  • xylanase

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