Abstract
An extracellular agarase from marine bacterium Stenotrophomonas sp. NTa was purified to homogeneity. By size exclusion chromatography and SDS-PAGE analysis, the enzyme was determined to be a homodimer with monomeric molecular mass of 89.0kDa. The optimal temperature and pH of strain NTa agarase were 40°C and 10.0, respectively. It exhibited striking stability across a wide pH range of 5.0–11.0. Agarase from Stenotrophomonas sp. NTa had a relatively good resistance against the detected inhibitors, detergents and urea denaturant. The Km and Vmax for agar were 11.3mg/ml and 25.4U/mg, respectively. Thin layer chromatography analysis, mass spectrometry, and enzyme assay using p-nitrophenyl-α/β-d-galactopyranoside revealed that strain NTa agarase was a β-agarase that degraded agarose into neoagarobiose, neoagarotetraose and neoagarohexaose as the predominant products, as well as a small amount of 3,6-anhydro-α-l-galactose. This is the first to present evidence of agarolytic activity in strain from genus Stenotrophomonas.
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