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1.
Foods ; 10(10)2021 Sep 25.
Article in English | MEDLINE | ID: mdl-34681316

ABSTRACT

The aim of this study was to determine the impact of environmental conditions on the antimicrobial properties of 21 lactic acid bacteria strains in the selected indicator bacteria. To assess the antimicrobial activity of the whole bacteria culture (WBC), the agar well diffusion method was used. The interference of LAB strains with the growth of the selected indicator bacteria was evaluated by incubating co-cultures in the food matrix. Based on the conducted research, it was found that environmental conditions have a significant impact on the antimicrobial activity of lactic acid bacteria strains. The highest antimicrobial activity was recorded under optimal conditions for the development of LAB, the incubation time being different depending on the indicator strain used. The tested LAB strains were characterized by a high ability to inhibit indicator strains, especially in the food matrix. These results led us to further characterize and purify the antimicrobial compound produced by lactic acid bacteria taking into account changing environmental conditions.

2.
Nucleic Acids Res ; 31(14): e74, 2003 Jul 15.
Article in English | MEDLINE | ID: mdl-12853651

ABSTRACT

The TspDTI restriction endonuclease, which shows a novel recognition specificity 5'-ATGAA(N(11/9))-3', was isolated from Thermus sp. DT. TspDTI appears to be a 'twin' of restriction endonuclease TspGWI from Thermus sp. GW, as we have previously reported. TspGWI was isolated from the same location as TspDTI, it recognizes a related sequence 5'-ACGGA(N(11/9))-3' and has conserved cleavage positions. Both enzymes resemble two other class-IIS endonucleases from Thermus sp.: TaqII and Tth111II. N-terminal amino acid sequences of TspGWI tryptic peptides exhibit 88.9-100% similarity to the TaqII sequence. All four enzymes were purified to homogeneity; their polypeptide sizes (114.5-122 kDa) make them the largest class-IIS restriction endonucleases known to date. The existence of a Thermus sp. sub-family of class-IIS restriction endonucleases of a common origin is herein proposed.


Subject(s)
Deoxyribonucleases, Type II Site-Specific/metabolism , Thermus/enzymology , Amino Acid Sequence , Base Sequence , Binding Sites/genetics , DNA, Bacterial/chemistry , DNA, Bacterial/genetics , Deoxyribonucleases, Type II Site-Specific/genetics , Deoxyribonucleases, Type II Site-Specific/isolation & purification , Evolution, Molecular , Sequence Analysis, DNA , Sequence Homology, Amino Acid , Substrate Specificity , Thermus/genetics
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