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Preliminary Functional Characterization, Cloning and Primary Sequence of Fastuosain, a Cysteine Peptidase Isolated from Fruits of Bromelia fastuosa

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The present work reports the characterization of Fastuosain, a novel cysteine protease of 25kDa, purified from the unripe fruits of Bromelia fastuosa, a wild South American Bromeliaceae. Proteolytic activity, measured using casein and synthetic substrates, was dependent on the presence of thiol reagents, having maximum activity at pH 7.0. The present work reports cDNA cloning of Fastuosain; cDNA was amplified by PCR using specific primers. The product was 1096pb long. Mature fastuosain has 217 residues, and with the proregion has a total length of 324 residues. Its primary sequence showed high homology with ananain(74%), stem bromelain (66%) and papain (44%).

Keywords: Peptidase; bromelain; cysteine-protease; papain; plant peptidase; protease

Document Type: Research Article


Affiliations: Departamento de Quimica e Ciencias Ambientais, IBILCE-UNESP, Rua Cristovao Colombo 2265, Sao Jose do Rio Preto SP, Brasil 15054-000.

Publication date: January 1, 2006

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  • Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.

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