A Simple Intact Protein Analysis by MALDI-MS for Characterization of Ribosomal Proteins of Two Genome-Sequenced Lactic Acid Bacteria and Verification of Their Amino Acid Sequences

2007 ◽  
Vol 6 (10) ◽  
pp. 3899-3907 ◽  
Author(s):  
Kanae Teramoto ◽  
Hiroaki Sato ◽  
Liwei Sun ◽  
Masaki Torimura ◽  
Hiroaki Tao

1993 ◽  
Vol 56 (4) ◽  
pp. 338-356 ◽  
Author(s):  
CATHERINE G. NETTLES ◽  
SUSAN F. BAREFOOT

Numerous strains of lactic acid bacteria associated with food systems are capable of producing bacteriocins, or antibacterial proteins with activity against foodborne pathogens such as Listeria monocytogenes, Staphylococcus aureus, and Clostridium botulinum. Recently, considerable emphasis has been placed on the identification of these proteins and their biochemical properties, including spectrum of activity, production conditions, purification procedures, amino acid composition, amino acid sequence, and modes of action. Advances in genetic engineering techniques have facilitated the characterization of these proteins at. the genetic level, providing information on hydropathic index, protein synthesis and structure, immunity determinants for resistance and/or tolerance, and cloning of bacteriocin genes into other organisms. Prior to the utilization of bacteriocins and/or the producer organism in food systems, a thorough understanding of the physical, biochemical, and genetic properties is required. Additional parameters for use of bacteriocins and bacteriocin-producing organisms in food systems also are discussed.



2008 ◽  
Vol 74 (14) ◽  
pp. 4454-4462 ◽  
Author(s):  
Steven W. Singer ◽  
Clara S. Chan ◽  
Adam Zemla ◽  
Nathan C. VerBerkmoes ◽  
Mona Hwang ◽  
...  

ABSTRACT A novel, soluble cytochrome with an unusual visible spectral signature at 579 nm (Cyt579) has been characterized after isolation from several different microbial biofilms collected in an extremely acidic ecosystem. Previous proteogenomic studies of an Fe(II)-oxidizing community indicated that this abundant red cytochrome could be extracted from the biofilms with dilute sulfuric acid. Here, we found that the Fe(II)-dependent reduction of Cyt579 was thermodynamically favorable at a pH of >3, raising the possibility that Cyt579 acts as an accessory protein for electron transfer. The results of transmission electron microscopy of immunogold-labeled biofilm indicated that Cyt579 is localized near the bacterial cell surface, consistent with periplasmic localization. The results of further protein analysis of Cyt579, using preparative chromatofocusing and sodium dodecyl sulfate-polyacrylamide gel electrophoresis, revealed three forms of the protein that correspond to different N-terminal truncations of the amino acid sequence. The results of intact-protein analysis corroborated the posttranslational modifications of these forms and identified a genomically uncharacterized Cyt579 variant. Homology modeling was used to predict the overall cytochrome structure and heme binding site; the positions of nine amino acid substitutions found in three Cyt579 variants all map to the surface of the protein and away from the heme group. Based on this detailed characterization of Cyt579, we propose that Cyt579 acts as an electron transfer protein, shuttling electrons derived from Fe(II) oxidation to support critical metabolic functions in the acidophilic microbial community.



2006 ◽  
Vol 27 (13) ◽  
pp. 2638-2650 ◽  
Author(s):  
Elvira Balaguer ◽  
Uwe Demelbauer ◽  
Matthias Pelzing ◽  
Victoria Sanz-Nebot ◽  
José Barbosa ◽  
...  


2021 ◽  
Vol 709 (1) ◽  
pp. 012020
Author(s):  
Evy Rossi ◽  
Akhyar Ali ◽  
Raswen Efendi ◽  
Fajar Restuhadi ◽  
Yelmira Zalfiatri ◽  
...  




2014 ◽  
Vol 685 ◽  
pp. 486-489 ◽  
Author(s):  
Yan Yan Wu ◽  
Gang You ◽  
Lai Hao Li ◽  
Xian Qing Yang ◽  
Ya Wei

Inoculation with compound lactobacillus in the low-salt pickled fish, fermented and dried to produce cured fish. The paper studied the effects of inoculating compound lactobacillus on the pH, total volatile basic nitrogen (TVB-N), amino acid nitrogen content (AA-N) and total acid content of salted fish quality. The results showed that, compared with the non-vaccinated groups (CK), The cured fish inoculated lactobacillus had a lower pH and TVB-N content, higher the amino acid nitrogen content and total acid content. Inoculated compound lactic acid bacteria into salted fish, to a certain extent, could improve the nutritional value and edible value, which had positive effects on the fish quality.



2012 ◽  
Vol 58 (3) ◽  
pp. 163-172 ◽  
Author(s):  
Jie Yu ◽  
Wa Gao ◽  
Manjun Qing ◽  
Zhihong Sun ◽  
Weihong Wang ◽  
...  


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