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  • Title: Purification, characterization, and molecular cloning of a chitinase from the seeds of Benincasa hispida.
    Author: Shih CY, Khan AA, Jia S, Wu J, Shih DS.
    Journal: Biosci Biotechnol Biochem; 2001 Mar; 65(3):501-9. PubMed ID: 11330660.
    Abstract:
    A chitinase was purified from the seeds of Benincasa hispida, a medicinal plant also called white gourd, and a member of the Cucurbitaceae family. Purification was done by using a procedure consisting of only two fractionation steps: an acid denaturation step followed by ion-exchange chromatography. The sequence of the N-terminal forty amino acid residues was analyzed and the sequence indicated that the enzyme is a class III chitinase. The enzyme, which is a basic chitinase, is one of at least five chitinases detected in the seed extract of B. hispida. Like other class III chitinases, this enzyme also has lysozyme activity. A genomic clone of the gene encoding the enzyme was isolated and sequenced. The gene has the potential to encode a protein of 301 amino acid residues. The deduced amino acid sequence of the protein, as expected from the N-terminal amino acid sequence, shares high degrees of similarity with other class III chitinases.
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