Stability of a black eyed pea trypsin/chymotrypsin inhibitor (BTCI)

Luciano   Paulino   Silva; Jose   Roberto S. A.   Leite; Carlos      Bloch Jr.; Sonia   Maria   de Freitas

doi:10.2174/092986650706221207164315

Abstract

The stability of BTCI has been investigated as function of pH and temperature, following its inhibitory activity against trypsin. The isolated inhibitor of 9,084 Oa is stable over pH 3 to 12 at 25°C. BTCI showed high thermal stability ranging from 25 to 95°C at pH 3 and 7. However, the protein lost about 20% of its inhibitory activity over 75°C at pH 8.2. The results indicated that BTCI is extremely stable to heat and pH as typical of Bowman-Birk inhibitors.

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Protein & Peptide Letters

Title:Stability of a black eyed pea trypsin/chymotrypsin inhibitor (BTCI)

Volume: 7 Issue: 6

Author(s): Luciano Paulino Silva, Jose Roberto S. A. Leite, Carlos Bloch Jr. and Sonia Maria de Freitas*

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Abstract: The stability of BTCI has been investigated as function of pH and temperature, following its inhibitory activity against trypsin. The isolated inhibitor of 9,084 Oa is stable over pH 3 to 12 at 25°C. BTCI showed high thermal stability ranging from 25 to 95°C at pH 3 and 7. However, the protein lost about 20% of its inhibitory activity over 75°C at pH 8.2. The results indicated that BTCI is extremely stable to heat and pH as typical of Bowman-Birk inhibitors.

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Silva Paulino Luciano, Leite Roberto S. A. Jose, Bloch Jr. Carlos and de Freitas Maria Sonia*, Stability of a black eyed pea trypsin/chymotrypsin inhibitor (BTCI), Protein & Peptide Letters 2000; 7 (6) . https://dx.doi.org/10.2174/092986650706221207164315

DOI https://dx.doi.org/10.2174/092986650706221207164315	Print ISSN 0929-8665
Publisher Name Bentham Science Publisher	Online ISSN 1875-5305