A novel putative lysophospholipase hydrolase (833) from Xanthomonas axonopodis pv was identified, characterized. Sequence analysis of 833 revealed a putative catalytic triad (Ser61, Asp209, and His212), and a conserved sequence motif Ser(S)61-Gly(G)126-Asn(N)128-His(H)212 with moderate identities with other members of the SGNH-hydrolase superfamily. 833 was able to hydrolyze short-chain esters such as p-nitrophenyl acetate (C2), butyrate (C4), and valerate (C5) suggesting that the hydrophobic binding pocket of 833 seems to be optimized to accommodate short acyl chain lengths. 833 displayed its maximal activity at pH 7.0 , 60 °C. Higher thermal and chemical stability of the 833 highlight its potential applicability as a biocatalyst in the pharmaceutical and chemical industries.
