Purification, Characterization, and Molecular Cloning of a Chitinase from the Seeds of Benincasa hispida.

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  • SHIH Chao-Yun T.
    RCMI Program, Health Research Center, Department of Biology, Southern University
  • KHAN Anwar A.
    Department of Biological Sciences, Louisiana State University and LSU Agricultural Center
  • JIA Shifang
    RCMI Program, Health Research Center, Department of Biology, Southern University Current address: Institute of Microbiology, Academia Sinica
  • WU Junlin
    Department of Biological Sciences, Louisiana State University and LSU Agricultural Center Current adress: Center for Agricultural Biotechnology, University of Maryland
  • SHIH Ding S.
    Department of Biological Sciences, Louisiana State University and LSU Agricultural Center

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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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