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Molecular Recognition and Chemical Modification of Biopolymers — Two Main Components of Affinity Modification
Published in Dmitri G. Knorre, Valentin V. Vlassov, Affinity Modification of Biopolymers, 1989
Dmitri G. Knorre, Valentin V. Vlassov
In the preceding section we have presented an example of a transport protein, lactose permease, coded by one of the genes of lactose operon. Although a detailed mechanism of action of transport proteins remains unknown, it is evident that the process starts from the recognition of protein by molecules which must be transferred across the membrane. This means that the recognition site resides at the outer surface of the membrane. It is believed that some conformational change follows which makes the inner side of the cell accessible to the bound molecule.
Synergistic antibacterial and anti-biofilm activity of nisin like bacteriocin with curcumin and cinnamaldehyde against ESBL and MBL producing clinical strains
Published in Biofouling, 2020
Garima Sharma, Shweta Dang, Aruna K, Manjula Kalia, Reema Gabrani
E. coli ML-35p has been genetically modified to express cytoplasmic β-galactosidase but cannot produce lactose permease (Epand et al. 2010). Nisin like bacteriocin-GAM217 appeared to alter membrane permeability, resulting in leakage of the intracellular enzyme in a time-dependent manner as evident by the increase in absorbance (Figure 3). SDS (0.1%) treated cells were used as positive control. The statistical significance analysed by Tukey’s HST test showed that the treatment group was significantly different from untreated cells. These results were in agreement with previous reports where two bacteriocins (nisin and lactacin F) from L. lactis have been reported for channel formation as their mode of action to target bacterial cells, as studied by the planar lipid bilayer method (Héchard and Sahl 2002). Lactoccocin A, another bacteriocin from L. lactis, has been reported to kill bacterial cells by causing pore formation (Yildirim et al. 2007).