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 Da is stable over pH 3 to 10 at 25 o C. BTCI showed high thermal stability ranging from 25 to 95 o C at pH 3.0 and 7.0. However, the protein lost about 20 percent of its inhibitory activity over 75 o C at pH 8.2. The results indicated that BTCI is extremely stable to heat and pH as typical of Bowman-Birk inhibitors.
Keywords: TRYPSIN CHYMOTRYPSIN INHIBITOR, chymotrypsin
Protein & Peptide Letters
Title: Stability Of A Black Eyed Pea Trypsin Chymotrypsin Inhibitor (BTCI)
Volume: 8 Issue: 1
Author(s): Luciano Paulino da Silva, Jose Roberto S.A.Leite, Carlos Bloch Jr. and Sonia Maria de Freitas
Affiliation:
Keywords: TRYPSIN CHYMOTRYPSIN INHIBITOR, chymotrypsin
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 Da is stable over pH 3 to 10 at 25 o C. BTCI showed high thermal stability ranging from 25 to 95 o C at pH 3.0 and 7.0. However, the protein lost about 20 percent of its inhibitory activity over 75 o 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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Cite this article as:
da Silva Paulino Luciano, S.A.Leite Roberto Jose, Bloch Jr. Carlos and de Freitas Maria Sonia, Stability Of A Black Eyed Pea Trypsin Chymotrypsin Inhibitor (BTCI), Protein & Peptide Letters 2001; 8 (1) . https://dx.doi.org/10.2174/0929866013409715
DOI https://dx.doi.org/10.2174/0929866013409715 |
Print ISSN 0929-8665 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-5305 |
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