PMID: 9438997Jan 24, 1998Paper

Purification and characterization of two chitinase isoforms from the bulbs of gladiolus (Gladiolus gandavensis)

Bioscience, Biotechnology, and Biochemistry
T YamagamiM Ishiguro

Abstract

Two chitinase isoforms, designated GBC-a and GBC-b, were purified from the bulbs of gladiolus (Gladiolus gandavensis) using CM-cellulose column chromatography followed by Butyl-Toyopearl 650 M hydrophobic column chromatography, gel filtration on Sephadex G-75, and Mono-S FPLC. GBC-a and GBC-b are weakly acidic and weakly basic proteins with molecular masses of 30 kDa, and isoelectric points of 6.0 and 7.5, respectively. GBC-a and GBC-b were found to be homologous proteins with similar amino acid compositions and N-terminal sequences. The number of half-cystine residues in GBC-a and GBC-b was only one each, which is much lower than those of plant class I (15-17 Cys residues/mol), class II (5-8 Cys residues/mol), and class III (6 Cys residues/mol) chitinases. The N-terminal sequences of GBC-a and GBC-b were completely different from those of plant three classes of chitinases. The optimal pHs of these chitinases toward glycolchitin were pH 5. GBC-a hydrolyzed (GlcNAc)5 into (GlcNAc)2, (GlcNAc)3 and (GlcNAc)4, and (GlcNAc)5 into (GlcNAc)2 and (GlcNAc)3.

Citations

Jul 19, 2013·Critical Reviews in Biotechnology·Anand NagpureRajinder K Gupta
May 8, 1998·Bioscience, Biotechnology, and Biochemistry·T YamagamiM Ishiguro
May 6, 2003·Bioscience, Biotechnology, and Biochemistry·Keisuke SuzukawaMasatsune Ishiguro

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