Purification and characterization of a novel β‐agarase from Vibrio sp. AP‐2

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Abstract
.beta.-Agarase was purified from the culture fluid of a porphyran-decomposing marine bacterium (strain AP-2) by ammonium sulfate precipitation, successive column chromatography and DNase and RNase treatment. The final enzyme preparation appeared to be homogeneous on polyacrylamide gel electrophoresis. The enzyme had a molecular mass of 20 kDa, a pH optimum of 5.5, and was stable in the pH region 4.0-9.0 and at temperatures below 45.degree. C. The .beta.-agarase was a novel endo-type enzyme which hydrolyzed neoagarotetraose, larger neoagarooligosaccharides and agar to give neoagarobiose [3,6-anhydro-.alpha.-L-galactopyranosyl-(1 .fwdarw. 3)-D-galactose] as the predominant product. The enzyme did not act on K-carrageenan. According to the criteria of Bergey''s Manual of Systematic Bacteriology, the strain was assigned to the genus Vibrio.