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from indigenous fermented foods and human gut ... - Thapar University

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40<br />

Chapter II Review of Literature<br />

IIc bacteriocins are grouped on the fact that their N- <strong>and</strong> C-termini are covalently linked,<br />

resulting in a cyclic structure (Maqueda et al., 2004). Class II bacteriocins are small, heat-<br />

stable, cationic <strong>and</strong> hydrophobic peptides. They are generally very stable at acidic pH <strong>and</strong> as<br />

pH increases, their heat stability decreases. Moreover, bacteriocins are usually sensitive to<br />

proteolytic enzymes, such as trypsin, proteinase K <strong>and</strong> protease (Chen <strong>and</strong> Hoover, 2003).<br />

Unlike lantibiotics, class II bacteriocins are not subject to extensive post-translational<br />

modification, but synthesized as precursor molecules mostly containing a leader peptide of<br />

the so called double glycine type (Cotter et al., 2005; Håvarstein, Diep <strong>and</strong> Nes, 1995).

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