Production of natural antimicrobial compoundd-phenyllactic acid usingLeuconostoc mesenteroidesATCC 8293 whole cells involving highly actived-lactate dehydrogenase

2014 ◽  
Vol 59 (4) ◽  
pp. 404-411 ◽  
Author(s):  
L. Li ◽  
S.-Y. Shin ◽  
K.W. Lee ◽  
N.S. Han
Keyword(s):  
Lactate Dehydrogenase ◽  
Natural Antimicrobial ◽  
Phenyllactic Acid ◽  
Whole Cells

scholarly journals Enzymological characterization of a novel d-lactate dehydrogenase from Lactobacillus rossiae and its application in d-phenyllactic acid synthesis

3 Biotech ◽  
2020 ◽  
Vol 10 (3) ◽  
Author(s):  
Xi Luo ◽  
Yingying Zhang ◽  
Fengwei Yin ◽  
Gaowei Hu ◽  
Qiang Jia ◽  
...  
Keyword(s):  
Lactate Dehydrogenase ◽  
Acid Synthesis ◽  
Phenyllactic Acid

The antibacterial action of phenoxiodinin-5-ium chloride

1968 ◽  
Vol 14 (9) ◽  
pp. 949-956
Author(s):  
W. E. Inniss
Keyword(s):  
Staphylococcus Aureus ◽  
Antibacterial Activity ◽  
Lactate Dehydrogenase ◽  
Organic Compound ◽  
Specific Inhibitor ◽  
Cellular Material ◽  
Sodium Malonate ◽  
Whole Cells ◽  
Growing Cell ◽  
Insight Into

Phenoxiodinin-5-ium chloride (PC) is a synthetic organic compound possessing a little known type of iodine-containing structure and has been found to possess antibacterial activity. A study was conducted to gain some insight into the mechanism by which it exerted its effect on bacteria. The compound inhibited oxygen uptake and 14CO2 evolution from uniformly labelled glucose-14C by Staphylococcus aureus, under both resting and growing cell conditions. The assimilation of glucose-14C and L-methionine-methyl-14C into cellular material was also affected. A release of 14C-labelled cellular material from whole cells and from spheroplasts stabilized in 0.5 M sucrose occurred in the presence of PC. PC also inhibited succinate and lactate dehydrogenase systems in whole cells and cell membranes of Bacillus megaterium. When sodium malonate, a highly specific inhibitor of succinate dehydrogenase, was substituted for PC, an increased release of 14C-intra-cellular material also occurred. PC possesses the ability to inhibit enzymes located on the cell membrane of S. aureus and B. megaterium.

scholarly journals Cellular localization of D-lactate dehydrogenase and NADH oxidase fromArchaeoglobus fulgidus

Archaea ◽  
2002 ◽  
Vol 1 (2) ◽  
pp. 95-104 ◽  
Author(s):  
Vishwajeeth Reddy Pagala ◽  
Joohye Park ◽  
David W. Reed ◽  
Patricia L. Hartzell
Keyword(s):  
Lactate Dehydrogenase ◽  
Cellular Localization ◽  
Nadh Oxidase ◽  
Optimal Growth ◽  
Binding Pocket ◽  
Integral Membrane Protein ◽  
Dissimilatory Sulfate Reduction ◽  
Gene Encoding ◽  
Thin Sections ◽  
Whole Cells

Members of the genusArchaeoglobusare hyperthermophilic sulfate reducers with an optimal growth temperature of 83 °C.Archaeoglobus fulgiduscan utilize simple compounds including D-lactate, L-lactate and pyruvate as the sole substrate for carbon and electrons for dissimilatory sulfate reduction. Previously we showed that this organism makes a D-lactate dehydrogenase (Dld) that requires FAD and Zn2+for activity. To determine the cellular location and topology of Dld and to identify proteins that interact with Dld, an antibody directed against Dld was prepared. Immunocytochemical studies using gold particle-coated secondary antibodies show that more than 85% of Dld is associated with the membrane. A truncated form of Dld was detected in immunoblots of whole cells treated with protease, showing that Dld is an integral membrane protein and that a significant portion of Dld, including part of the FAD-binding pocket, is outside the membrane facing the S-layer. The gene encoding Dld is part of an operon that includesnoxA2, which encodes one of several NADH oxidases inA. fulgidus. Previous studies have shown that NoxA2 remains bound to Dld during purification. Thin sections ofA. fulgidusprobed simultaneously with antibodies against Dld and NoxA2 show that both proteins co-localized to the same sites in the membrane. Although these data show a tight interaction between NoxA2 and Dld, the role of NoxA2 in electron transport reactions is unknown. Rather, NoxA2 may protect proteins involved in electron transfer by reducing O2to H2O2or H2O.

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