{"refrec":{"BRefID":218627,"RR":"Beloqui, A. (2010). Diversity of glycosyl hydrolases from cellulose-depleting communities enriched from casts of two earthworm species. Appl. Environ. Microbiol. 76(17): 5934-5946. http://dx.doi.org/10.1128/AEM.00902-10","BEntID":210370,"PublicFlag":1,"CheckedFlag":1,"wosflag":1,"vabbflag":1,"RefStringPartII":". Appl. Environ. Microbiol. 76(17): 5934-5946. http://dx.doi.org/10.1128/AEM.00902-10","DocTypID":8,"DocType":"Journal article","MarineFlag":0,"FreshFlag":0,"BrackishFlag":0,"TerrestrialFlag":1,"Authorstring":"Beloqui, A.","OrigTitleTranslFlag":0,"Authorstringtrunc":"Beloqui, A.","Englishabstract":"The guts and casts of earthworms contain microbial assemblages that process large amounts of organic polymeric substrates from plant litter and soil; however, the enzymatic potential of these microbial communities remains largely unexplored. In the present work, we retrieved carbohydrate-modifying enzymes through the activity screening of metagenomic fosmid libraries from cellulose-depleting microbial communities established with the fresh casts of two earthworm species, Aporrectodea caliginosa and Lumbricus terrestris, as inocula. Eight glycosyl hydrolases (GHs) from the A. caliginosa-derived community were multidomain endo-ß-glucanases, ß-glucosidases, ß-cellobiohydrolases, ß-galactosidase, and ß-xylosidases of known GH families. In contrast, two GHs derived from the L. terrestris microbiome had no similarity to any known GHs and represented two novel families of ß-galactosidases/a-arabinopyranosidases. Members of these families were annotated in public databases as conserved hypothetical proteins, with one being structurally related to isomerases/dehydratases. This study provides insight into their biochemistry, domain structures, and active-site architecture. The two communities were similar in bacterial composition but significantly different with regard to their eukaryotic inhabitants. Further sequence analysis of fosmids and plasmids bearing the GH-encoding genes, along with oligonucleotide usage pattern analysis, suggested that those apparently originated from Gammaproteobacteria (pseudomonads and Cellvibrio-like organisms), Betaproteobacteria (Comamonadaceae), and Alphaproteobacteria (Rhizobiales). 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