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2000
Volume 14, Issue 8
  • ISSN: 0929-8665
  • E-ISSN: 1875-5305

Abstract

Two 30-kDa proteins with N-terminal sequence homology to chitinases have been isolated from fruits of the emperor banana by using a protocol that involved (NH4)2SO4 precipitation, affinity chromatography on Affi-gel blue gel, ion exchange chromatography by fast protein liquid chromatography (FPLC) on Mono S and gel filtration by FPLC on Superdex 75. The proteins were adsorbed on Affi-gel blue gel and Mono S. They both inhibited mycelial growth in Fusarium oxysporum but not in Mycosphaerella arachidicola. The chitinase-like protein more strongly bound on Mono S was obtained with a slightly lower yield and exhibited a higher antifungal potency toward F. oxysporum when compared with the less strongly bound chitinase-like protein.

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/content/journals/ppl/10.2174/092986607781483750
2007-08-01
2025-05-22
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/content/journals/ppl/10.2174/092986607781483750
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  • Article Type:
    Research Article
Keyword(s): chitinases; Emperor banana; isolation
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