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Properties of a Milk Clotting Protease Isolated from Fruits of Bromelia balansae Mez by Marcelo F. Pardo; Laura M.I. López; Néstor O. Caffini; Claudia L. Natalucci is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.

What is Properties of a Milk Clotting Protease Isolated from Fruits of Bromelia balansae Mez about?

## Unripe fruit extracts of Bmmelia 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-a-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.

Who reads Properties of a Milk Clotting Protease Isolated from Fruits of Bromelia balansae Mez?

Author

Marcelo F. Pardo; Laura M.I. López; Néstor O. Caffini; Claudia L. Natalucci

Publisher

Walter de Gruyter GmbH

Published

2001

Language

EN

Field

Biochemistry, Genetics and Molecular Biology (Life Sciences)