scholarly journals Excess of threonine compared with serine promotes threonine aldolase activity in Lactococcus lactis IL1403

Microbiology ◽  
2015 ◽  
Vol 161 (5) ◽  
pp. 1073-1080 ◽  
Author(s):  
Kadri Aller ◽  
Kaarel Adamberg ◽  
Indrek Reile ◽  
Veronica Timarova ◽  
Karl Peebo ◽  
...  
Keyword(s):  
Lactococcus Lactis ◽  
Threonine Aldolase ◽  
Aldolase Activity ◽  
Lactis Il1403

Measurement of l-Threonine Aldolase Activity in Rat Liver

1979 ◽  
Vol 7 (6) ◽  
pp. 1274-1276 ◽  
Author(s):  
MICHAEL I. BIRD ◽  
PETER B. NUNN
Keyword(s):  
Rat Liver ◽  
Threonine Aldolase ◽  
Aldolase Activity

Ribosomes, ribosomal subunits and ribosomal proteins of Lactococcus lactis IL1403

Biochimie ◽  
1992 ◽  
Vol 74 (11) ◽  
pp. 995-1005 ◽  
Author(s):  
N LIMASNZOUZI ◽  
M GUERIN ◽  
D HAYES
Keyword(s):  
Lactococcus Lactis ◽  
Ribosomal Proteins ◽  
Ribosomal Subunits ◽  
Lactis Il1403

Non-enzymic copper reduction by menaquinone enhances copper toxicity in Lactococcus lactis IL1403

Microbiology ◽  
2013 ◽  
Vol 159 (Pt_6) ◽  
pp. 1190-1197 ◽  
Author(s):  
Helge K. Abicht ◽  
Yulia Gonskikh ◽  
Simon D. Gerber ◽  
Marc Solioz
Keyword(s):  
Lactococcus Lactis ◽  
Copper Toxicity ◽  
Lactis Il1403

Recombinant interleukin 6 with M cell-targeting moiety produced in Lactococcus lactis IL1403 as a potent mucosal adjuvant for peroral immunization

Vaccine ◽  
2015 ◽  
Vol 33 (16) ◽  
pp. 1959-1967 ◽  
Author(s):  
Hui-Shan Li ◽  
Da-Chuan Piao ◽  
Tao Jiang ◽  
Jin-Duck Bok ◽  
Chong-Su Cho ◽  
...  
Keyword(s):  
Lactococcus Lactis ◽  
Interleukin 6 ◽  
Cell Targeting ◽  
M Cell ◽  
Mucosal Adjuvant ◽  
Lactis Il1403

scholarly journals Alternative Lactose Catabolic Pathway in Lactococcus lactis IL1403

2005 ◽  
Vol 71 (10) ◽  
pp. 6060-6069 ◽  
Author(s):  
Tamara Aleksandrzak-Piekarczyk ◽  
Jan Kok ◽  
Pierre Renault ◽  
Jacek Bardowski
Keyword(s):  
Lactococcus Lactis ◽  
Protein A ◽  
Lactose Hydrolysis ◽  
Galactosidase Activity ◽  
Solid Media ◽  
Pathway Gene ◽  
Leloir Pathway ◽  
Catabolite Control Protein A ◽  
Lactis Il1403 ◽  
Strong Control

ABSTRACT In this study, we present a glimpse of the diversity of Lactococcus lactis subsp. lactis IL1403 β-galactosidase phenotype-negative mutants isolated by negative selection on solid media containing cellobiose or lactose and X-Gal (5-bromo-4-chloro-3-indolyl-β-d-galactopyranoside), and we identify several genes essential for lactose assimilation. Among these are ccpA (encoding catabolite control protein A), bglS (encoding phospho-β-glucosidase), and several genes from the Leloir pathway gene cluster encoding proteins presumably essential for lactose metabolism. The functions of these genes were demonstrated by their disruption and testing of the growth of resultant mutants in lactose-containing media. By examining the ccpA and bglS mutants for phospho-β-galactosidase activity, we showed that expression of bglS is not under strong control of CcpA. Moreover, this analysis revealed that although BglS is homologous to a putative phospho-β-glucosidase, it also exhibits phospho-β-galactosidase activity and is the major enzyme in L. lactis IL1403 involved in lactose hydrolysis.

Threonine aldolase and alcohol dehydrogenase activities in Lactobacillus bulgaricus and Lactobacillus acidophilus and their contribution to flavour production in fermented milks

1983 ◽  
Vol 50 (3) ◽  
pp. 375-379 ◽  
Author(s):  
Valerie M. Marshall ◽  
Wendy M. Cole
Keyword(s):  
Alcohol Dehydrogenase ◽  
Dehydrogenase Activity ◽  
Lactobacillus Acidophilus ◽  
Lactobacillus Bulgaricus ◽  
Flavour Compound ◽  
Threonine Aldolase ◽  
Fortified Milk ◽  
Alcohol Dehydrogenase Activity ◽  
Aldolase Activity ◽  
Acetaldehyde Production

SummaryCell-free extracts of both Lactobacillus bulgaricus and L. acidophilus demonstrated threonine aldolase activity, the end product of which was acetaldehyde, the major flavour compound of yoghurt. L. acidophilus also possessed an alcohol dehydrogenase activity capable of reducing acetaldehyde so that little yoghurt flavour was present in milks fermentation with this organism. Addition of threonine to fortified milk before fermentation with L. acidophilus increased acetaldehyde production and resulted in a well flavoured product similar to that of yoghurt made with L. bulgaricus. The contribution of these 2 enzymes to flavour production is discussed.

scholarly journals Starvation-Induced Stress Resistance in Lactococcus lactis subsp. lactis IL1403

1994 ◽  
Vol 60 (9) ◽  
pp. 3474-3478 ◽  
Author(s):  
Axel Hartke ◽  
Sandrine Bouche ◽  
Xavier Gansel ◽  
Philippe Boutibonnes ◽  
Yanick Auffray
Keyword(s):  
Lactococcus Lactis ◽  
Stress Resistance ◽  
Lactococcus Lactis Subsp ◽  
Induced Stress ◽  
Lactis Il1403

Low-redundancy sequencing of the entire Lactococcus lactis IL1403 genome

1999 ◽  
pp. 27-76 ◽  
Author(s):  
Alexander Bolotin ◽  
Stéphane Mauger ◽  
Karine Malarme ◽  
S. Dusko Ehrlich ◽  
Alexei Sorokin
Keyword(s):  
Lactococcus Lactis ◽  
Lactis Il1403

Chimeras of Mature Pediocin PA-1 Fused to the Signal Peptide of Enterocin P Permits the Cloning, Production, and Expression of Pediocin PA-1 in Lactococcus lactis

2007 ◽  
Vol 70 (12) ◽  
pp. 2792-2798 ◽  
Author(s):  
MARÍA MARTÍN ◽  
JORGE GUTIÉRREZ ◽  
RAQUEL CRIADO ◽  
CARMEN HERRANZ ◽  
LUIS M. CINTAS ◽  
...  
Keyword(s):  
Antimicrobial Activity ◽  
Lactococcus Lactis ◽  
Signal Peptide ◽  
Biologically Active ◽  
Enzyme Linked Immunosorbent Assay ◽  
Minimum Requirement ◽  
Recombinant Plasmids ◽  
Genes Encoding ◽  
Lactis Il1403 ◽  
Enterocin P

Chimeras of pediocin PA-1 (PedA-1), a bacteriocin produced by Pediococcus acidilactici PLBH9, fused to the signal peptide of enterocin P (EntP), a sec-dependent bacteriocin produced by Enterococcus faecium P13, permitted the production of PedA-1 in Lactococcus lactis. Chimeric genes encoding the EntP signal peptide (SPentP) fused to mature PedA-1 (pedA), with or without its immunity gene (pedB), were cloned into the expression vector pMG36c to generate the recombinant plasmids pMPP9 (SPentP:pedA) and pMPP14i (SPentP:pedA+pedB). Transformation of competent L. lactis subsp. lactis IL1403, L. lactis subsp. cremoris NZ9000, and L. lactis subsp. lactis DPC5598 with the recombinant plasmids has permitted the detection and quantitation of PedA-1 and the coproduction of nisin A and PedA-1 in supernatants of producer cells with specific anti–PedA-1 antibodies and a noncompetitive indirect enzyme-linked immunosorbent assay. Recombinant L. lactis hosts carrying pMPP9 or pMPP14i displayed antimicrobial activity, suggesting that mature PedA-1 fused to SPEntP is the minimum requirement for the synthesis, processing, and secretion of biologically active PedA-1 in L. lactis. However, the production and antimicrobial activity of the PedA-1 produced by L. lactis was lower than that produced by the P. acidilactici control strains.

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