(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 > Actinobacteria [phylum]: NE > Actinobacteria [class]: NE > Bifidobacteriales: NE > Bifidobacteriaceae: NE > Bifidobacterium: NE > Bifidobacterium animalis: NE > Bifidobacterium animalis subsp. lactis: 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.) Bifidobacterium animalis subsp. lactis DSM 10140: N, E.
Bifidobacterium animalis subsp. lactis BB-12: N, E.
Bifidobacterium animalis subsp. lactis HN019: N, E.
Bifidobacterium animalis subsp. lactis AD011: N, E.
Bifidobacterium animalis subsp. lactis V9: N, E.
Bifidobacterium animalis subsp. lactis Bl-04: N, E.
Bifidobacterium animalis subsp. lactis Bl12: N, E.
Bifidobacterium animalis subsp. lactis CECT 8145: N, E.
Bifidobacterium animalis subsp. lactis BS 01: N, E.
Bifidobacterium animalis subsp. lactis Bi-07: N, E.
Bifidobacterium animalis subsp. lactis ATCC 27673: N, E.
Bifidobacterium animalis subsp. lactis CNCM I-2494: N, E.
Bifidobacterium animalis subsp. lactis B420: N, E.
Bifidobacterium animalis subsp. lactis BLC1: 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 MTTSTHTEEITVMRDGLRLHGRIDAPQGEPKGPVVILMHGFMADLGYEPG SLLQQVSDQLVEAGFTSVRFDFNGRGNSDGSFANSDVCNQVEDAIAVLNF VRDRFEPAEISLLGHSQGGVIAGMTAGMYADVVHSLVLLSPAASIKDDAL RGRVLGVPFDPYHIPRRIALADGKHEVAGKYSRIAKTIPVYEAAAMFKGP ALAIQGEQDKVIDPSCAHNYGNAMANCTVSLYTNLDHKFNGDDRMRAIGE AVAFLQTHHEVA
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.
This study aimed to explore the capability of potentially probiotic bifidobacteria to hydrolyze chlorogenic acid into caffeic acid (CA), and to recognize the enzymes involved in this reaction. Bifidobacterium strains belonging to eight species occurring in the human gut were screened. The hydrolysis seemed peculiar of Bifidobacterium animalis, whereas the other species failed to release CA. Intracellular feruloyl esterase activity capable of hydrolyzing chlorogenic acid was detected only in B. animalis. In silico research among bifidobacteria esterases identified Balat_0669 as the cytosolic enzyme likely responsible of CA release in B. animalis. Comparative modeling of Balat_0669 and molecular docking studies support its role in chlorogenic acid hydrolysis. Expression, purification, and functional characterization of Balat_0669 in Escherichia coli were obtained as further validation. A possible role of B. animalis in the activation of hydroxycinnamic acids was demonstrated and new perspectives were opened in the development of new probiotics, specifically selected for the enhanced bioconversion of phytochemicals into bioactive compounds.
