PMID: 9546051Apr 18, 1998Paper

The purification and characterization of a Trichoderma harzianum exochitinase

Biochimica Et Biophysica Acta
E E DeaneJohn F Peberdy

Abstract

A chitinolytic enzyme was purified from the culture filtrate of T. harzianum (T198) by precipitation with ammonium sulphate followed by affinity binding to swollen chitin and release with 10% (v/v) acetic acid. The molecular weight of the enzyme was calculated to be 28 and 27.5 kD by gel filtration chromatography and SDS-PAGE, respectively. The isoelectric point of the enzyme was 7.4. The pH optimum for activity was 3.5 and maximum activity was obtained at 50 degrees C. The enzyme displayed activity on a wide array of chitin substrates of more than two N-acetylglucosamine units in length. HPLC analysis of hydrolysis products demonstrated that the enzyme was an exochitinase releasing N-acetylglucosamine only.

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Citations

Jul 19, 2005·Applied Microbiology and Biotechnology·C DelattreJ Courtois
Mar 27, 2001·Enzyme and Microbial Technology·S -Y. WangN K. Singh
Aug 17, 2000·Journal of Applied Microbiology·W SugintaL A Fothergill-Gilmore
Apr 28, 2001·Journal of Experimental Botany·J M Whipps
Jan 1, 2009·Protein Expression and Purification·Yoon Gyo LeeHyeun-Jong Bae
Mar 26, 2015·Applied Biochemistry and Biotechnology·Zehra Tavsan, Hulya Ayar Kayali
Jul 3, 2013·International Journal of Biological Macromolecules·Guillaume PierrePhilippe Michaud
Oct 24, 2008·Phytopathology·Kenneth G MooreGary A Payne
Jun 9, 2006·Mycopathologia·Li Duo-Chuan

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