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Structural and functional properties of the p60 proteins from different Listeria species.

ABSTRACT: The major extracellular protein p60 of Listeria monocytogenes seems to be required for this microorganism's adherence to and invasion of 3T6 mouse fibroblasts but not for adherence to human epithelial Caco-2 cells. Western blot analysis with polyclonal antibodies against p60 of L. monocytogenes indicated the presence of cross-reacting proteins in the culture supernatants of all Listeria species. Protein p60 of L. monocytogenes could restore adhesion of the L. monocytogenes mutant RIII (impaired in the synthesis of p60) to mouse fibroblasts more efficiently than that of Listeria grayi. The amino acid sequences of the p60-related proteins of L. innocua, L. ivanovii, L. seeligeri, L. welshimeri, and L. grayi indicated highly conserved regions of about 120 amino acids at both the N-terminal and the C-terminal ends. The middle portions of these proteins, consisting of about 240 amino acids, varied considerably. These parts include the repeat domain consisting of repetitions of Thr (T) and Asn (N) which was present only, albeit in different arrangements, in the p60 proteins of L. monocytogenes and L. innocua. The p60-related proteins of L. grayi, L. ivanovii, L. seeligeri, and L. welshimeri each contained an insertion of 54 amino acids which was absent in the p60 proteins of L. monocytogenes and L. innocua.

SUBMITTER: Bubert A

PROVIDER: S-EPMC207560 | biostudies-other | 1992 Dec

REPOSITORIES: biostudies-other

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Structural and functional properties of the p60 proteins from different Listeria species.

Bubert A A Kuhn M M Goebel W W Köhler S S

Journal of bacteriology 19921201 24

The major extracellular protein p60 of Listeria monocytogenes seems to be required for this microorganism's adherence to and invasion of 3T6 mouse fibroblasts but not for adherence to human epithelial Caco-2 cells. Western blot analysis with polyclonal antibodies against p60 of L. monocytogenes indicated the presence of cross-reacting proteins in the culture supernatants of all Listeria species. Protein p60 of L. monocytogenes could restore adhesion of the L. monocytogenes mutant RIII (impaired ...[more]

PMID: 1459966

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Project description:Plant proteins with improved solubility, foaming, and emulsifying properties are required to meet the demand for plant-based foods. This study evaluated the influence of alkaline extraction combined with enzyme- and ultrasound-assisted extraction on lentil protein structure and functionality. Enzyme- and ultrasound-assisted extractions were not capable of increasing the protein yield compared to alkaline extraction alone. However, the purity of isolated protein was dependent on the extraction process, ranging from 82.7% to 90%. Although the molecular mass, zeta potential profiles, and denaturation temperature were not dependent on the extraction method, the enthalpy of denaturation for protein obtained solely by alkaline extraction was significantly lower than that for assisted processes, indicating that protein denaturation is caused by an alkaline process. Changes in protein structure were also suggested by solubility analyses that showed that lentil proteins obtained by enzyme-assisted and ultrasound-assisted extraction have better solubility at pH 7 when compared to alkaline extraction alone. The surface activity of lentil protein was evidenced by interfacial and surface analysis, and it was influenced by the extraction process applied. We demonstrated that combining alkaline extraction with assisted processes, especially ultrasound technology, results in concentrates/isolates with higher solubility as compared to ones obtained solely by the traditional alkaline method, even though the choice of extraction method should depend on the desired functionality. Highlights • Proteins from lentil were efficiently recovered by alkaline extraction.• Lentil protein solubility was improved by ultrasound and enzyme extraction.• Lentil protein surface activity was dependent on the extraction process.• Foaming properties were improved by ultrasound extraction.• Emulsifying properties were not influenced by the extraction process. Ultrasound-assisted; Enzyme-assisted; Viscozyme L; Plant protein; Functional properties.

Dataset Information

Structural and functional properties of the p60 proteins from different Listeria species.

Publications

Structural and functional properties of the p60 proteins from different Listeria species.

Similar Datasets

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