Stability Of A Black Eyed Pea Trypsin Chymotrypsin Inhibitor (BTCI)

Authors: da Silva L.Paulino; S.A.Leite J.Roberto; Bloch Jr. C.; de Freitas S.Maria

Source: Protein and Peptide Letters, Volume 8, Number 1, February 2001 , pp. 33-38(6)

Publisher: Bentham Science Publishers

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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 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

Language: English

Document Type: Review article

DOI: http://dx.doi.org/10.2174/0929866013409715

Publication date: 2001-02-01

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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.