Revised safety evaluation of the food enzyme endo-1,4-β-xylanase from the genetically modified strain LMG S-24584 produced by a modified process.

The food enzyme endo-1,4-β-xylanase (4-β-d-xylan xylanohydrolase, EC 3.2.1.

Safety evaluation of the food enzyme glucan-1,4-α-glucosidase from the non-genetically modified strain DP-Azh100.

The food enzyme glucan-1,4-α-glucosidase (4-α-d-glucan glucohydrolase; EC 3.2.1.

Safety evaluation of the food enzyme α-amylase from the non-genetically modified strain AE-BAA.

The food enzyme α-amylase (4-α-d-glucan glucanohydrolase; EC 3.2.1.

Safety evaluation of the food enzyme α-amylase from the non-genetically modified strain UN-01.

The food enzyme α-amylase (4-α-d-glucan glucanohydrolase; EC 3.2.1.

Safety evaluation of the food enzyme -galactosidase from the genetically modified strain DSM 34099.

The food enzyme -galactosidase (-d-galactoside galactohydrolase; EC 3.2.1.

Safety evaluation of the food enzyme subtilisin from the non-genetically modified strain AP-01.

The food enzyme subtilisin (EC 3.4.21.

Taxonomic identity of the strains used to produce food enzymes evaluated in published EFSA opinions.

, a species known to produce the antimicrobial bacitracin, could be misidentified as , depending on the identification method used. For this reason, the European Commission requested EFSA to review the taxonomic identification of formerly assessed production strains. Following this request, EFSA retrieved the raw data from 27 technical dossiers submitted and found that the taxonomic identification was established by 16S rRNA gene analyses for 15 strains and by whole genome sequence analysis for 12 strains.

Safety evaluation of the food enzyme -amylase from the non-genetically modified strain AE-TA.

The food enzyme -amylase (4--d-glucan glucanohydrolase; EC 3.2.1.

Safety evaluation of the food enzyme preparation D-psicose 3-epimerase from the non-genetically modified strain SYG27B.

This assessment addresses a food enzyme preparation consisting of the immobilised non-viable cells of the non-genetically modified bacterium identified by the applicant (Samyang Corporation) as strain SYG27B. This strain produces the enzyme D-psicose 3-epimerase (EC 5.1.

Safety evaluation of the food enzyme mucorpepsin from the non-genetically modified strain M19-21.

The food enzyme mucorpepsin (EC 3.4.23.

Safety evaluation of the food enzyme microbial collagenase from the genetically modified strain pCol.

The food enzyme microbial collagenase (EC 3.4.24.

Safety evaluation of the food enzyme α-amylase from the non-genetically modified strain NZYM-WR.

The food enzyme α-amylase (4-α-d-glucan glucanohydrolase; EC 3.2.1.

Safety evaluation of the food enzyme glucan 1,4--maltohydrolase from the genetically modified strain MAMDSM.

The food enzyme glucan 1,4--maltohydrolase (4--d-glucan -maltohydrolase; EC 3.2.1.

Safety evaluation of the food enzyme subtilisin from the non-genetically modified strain NZYM-CX.

The food enzyme subtilisin (EC 3.4.21.

Safety evaluation of the food enzyme α-amylase from the non-genetically modified strain LMG-S 32676.

The food enzyme -amylase (4--d-glucan glucanohydrolase; EC 3.2.1.

Safety evaluation of the food enzyme α-amylase from the non-genetically modified strain T74.

The food enzyme α-amylase (4-α-D-glucan glucanohydrolase; EC 3.2.1.

Safety evaluation of the food enzyme subtilisin from the non-genetically modified strain DP-Dzx96.

The food enzyme subtilisin (serine endopeptidase, EC 3.4.21.

Safety evaluation of the food enzyme α-amylase from the non-genetically modified strain BA.

The food enzyme α-amylase (4-α-d-glucan glucanohydrolase; EC 3.2.1.

Safety evaluation of the food enzyme endo-1,4-β-xylanase from the genetically modified strain XAN.

The food enzyme endo-1,4-β-xylanase (4-β-d-xylan xylanohydrolase, EC 3.2.1.

Safety evaluation of the food enzyme subtilisin from the non-genetically modified strain LMG S-30155.

The food enzyme subtilisin (serine endopeptidase, EC 3.4.21.

Safety evaluation of the food enzyme asparaginase from the genetically modified strain NZYM-OA.

The food enzyme asparaginase (l-asparagine amidohydrolase; EC 3.5.1.

Safety evaluation of the food enzyme glucan 1,4--glucosidase from the non-genetically modified strain NZYM-BO.

The food enzyme glucan 1,4--glucosidase (4--d-glucan -glucohydrolase; EC 3.2.1.

Safety evaluation of the food enzyme d-tagatose 3-epimerase from the genetically modified strain PS-Sav-001.

The food enzyme d-tagatose 3-epimerase (EC 5.1.3.

Ubiquitin-protein ligase Ubr5 cooperates with hedgehog signalling to promote skeletal tissue homeostasis.

Mammalian Hedgehog (HH) signalling pathway plays an essential role in tissue homeostasis and its deregulation is linked to rheumatological disorders. UBR5 is the mammalian homologue of the E3 ubiquitin-protein ligase Hyd, a negative regulator of the Hh-pathway in Drosophila. To investigate a possible role of UBR5 in regulation of the musculoskeletal system through modulation of mammalian HH signaling, we created a mouse model for specific loss of Ubr5 function in limb bud mesenchyme.

Fibroblast growth factors (FGFs) prime the limb specific enhancer for chromatin changes that balance histone acetylation mediated by E26 transformation-specific (ETS) factors.

Sonic hedgehog () expression in the limb bud organizing centre called the zone of polarizing activity is regulated by the ZRS enhancer. Here, we examine in mouse and in a mouse limb-derived cell line the dynamic events that activate and restrict the spatial activity of the ZRS. Fibroblast growth factor (FGF) signalling in the distal limb primes the ZRS at early embryonic stages maintaining a poised, but inactive state broadly across the distal limb mesenchyme.