(Below N is a link to NCBI taxonomic web page and E link to ESTHER at designed phylum.) > cellular organisms: NE > Bacteria: NE > Terrabacteria group: NE > Firmicutes: NE > Bacilli: NE > Lactobacillales: NE > Lactobacillaceae: NE > Lactobacillus: NE > Lactobacillus reuteri: NE > Lactobacillus reuteri JCM 1112: NE
Warning: This entry is a compilation of different species or line or strain with more than 90% amino acid identity. You can retrieve all strain data
(Below N is a link to NCBI taxonomic web page and E link to ESTHER at designed phylum.) Lactobacillus reuteri F275: N, E.
Lactobacillus reuteri 100-23: N, E.
Lactobacillus reuteri: N, E.
Lactobacillus reuteri TD1: N, E.
Lactobacillus reuteri DSM 20016: N, E.
Lactobacillus reuteri MM2-3: N, E.
Lactobacillus reuteri CF48-3A: N, E.
Lactobacillus reuteri MM4-1A: N, E.
Lactobacillus reuteri SD2112: N, E.
Lactobacillus reuteri ATCC 53608: N, E.
Lactobacillus reuteri I5007: N, E.
LegendThis sequence has been compared to family alignement (MSA) red => minority aminoacid blue => majority aminoacid color intensity => conservation rate title => sequence position(MSA position)aminoacid rate Catalytic site Catalytic site in the MSA MEITIKRDGLKLYGLLEGTTTIKNDTIAILMHGFKGNLGYDDSKILYALS HYLNQQGIPTLRFDFDGTGHSDGEFKDMTVFSEILDGMKIIDYAHTTMQA KKIYLIGHSQGGVVASMLAAYYRDIITKLVLLAPAATLKDDALKGVCQGS QYDPNHIPETVDVHGFTVGGDYFRTAQLLPIYETAQHYSGPTLLIHGLAD NVVSPEASKKYNVIMPNSELHLIPEEGHMFNGSRRQEILELVANFLKN
A high variety of plants that are used for food production contain esterified hydroxycinnamic acids. As their free forms display several benefits, like an enhanced absorption in human intestinal tract, anti-oxidative and anti-carcinogenic effects, an improved protein solubility and reduced discoloration, the microbial ability to cleave the ester bond is highly desired. In order to examine potential fermentation strains for this purpose, six different lactic acid bacteria and one bifidobacterial strain were screened for their ability to degrade esterified hydroxycinnamic acids because these strains are commonly used for fermentation of plant-based foods. Moreover, their cinnamoyl esterase activity was examined by molecular biological analyses. The enzymes were heterologously expressed in Escherichia coli, purified and biochemically characterized. The purified esterases with a molecular mass around 27-29 kDa had their optimum predominantly between pH 7 and 8 at 20-30 degreesC. Bifidobacterium animalis subsp. lactis, Lactobacillus gasseri, Lactobacillus acidophilus, Lactobacillus plantarum and Lactobacillus fermentum displayed activities against a broad substrate range (methyl caffeate, methyl trans-p-coumarate, chlorogenic acid as well as partially ethyl ferulate). Concerning substrate affinity, reaction velocity, thermal and pH stability, Lactobacillus gasseri showed the overall best performance. The herein studied lactic acid- and bifidobacteria are promising for the production of fermented plant-based foods with an increased quality and nutritional value.
