Abstract
Unripe fruit extracts of Bromelia balansae Mez (Bromeliaceae), whose principal endopeptidase is balansain I (isolated for anion exchange chromatography: pI = 5.45, molecular weight = 23192), exhibit a pH profile with a maximum activity around pH 9.0 and are inhibited only by cysteine peptidases inhibitors. The alanine and glutamine derivatives of N-alpha-carbobenzoxy-L-amino acid p-nitrophenyl esters were strongly preferred by the enzyme. Enzymatic hydrolysis of milk and soy proteins yield characteristic patterns at pH 9.0. The N-terminal sequence showed a very high homology (85-90%) with other known Bromeliaceae endopeptidases.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Animals
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Cysteine Endopeptidases / isolation & purification
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Cysteine Endopeptidases / metabolism
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Cysteine Proteinase Inhibitors / pharmacology
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Endopeptidases / isolation & purification
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Endopeptidases / metabolism*
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Fruit / enzymology*
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Hydrogen-Ion Concentration
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Milk / drug effects
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Milk / metabolism*
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Milk Proteins / analysis
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Milk Proteins / metabolism
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Molecular Sequence Data
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Protease Inhibitors / pharmacology
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Soybean Proteins / analysis
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Soybean Proteins / metabolism
Substances
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Cysteine Proteinase Inhibitors
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Milk Proteins
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Protease Inhibitors
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Soybean Proteins
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Endopeptidases
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balansain I
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Cysteine Endopeptidases