Objective: This study was carried out to isolate and characterize an agarase from a marine bacterium Agarivorans albus QM38.
Methods: SDS-PAGE grade agarase was obtained from the fermentation broth after removing the bacteria by centrifugation, ammonium sulfate precipitation, DEAE-sepharose fast flow anion exchange chromatography and Sephacryl S-100 gel filtration. Enzyme's molecular weight was determined with SDS-PAGE. The catalysates of the isolated enzyme were determined withmass spectrography.
Results: Agarase A was isolated. The molecular weight of agarase A was 127.80 kDa. More characterizations of agarase A were studied and the results showed that the optimal reaction condition for agarase A was at 35 degrees C, pH 7.6, and agar concentration of 0.9% (w/v), while most of the metal ions inhibited the activity of it. The catalysates of agarase A were mainly tetrose and hexose.
Conclusion: Agarase A was purified from the medium. It could hydrolyze jellied agar and yield simple catalysates. Its molecular weight is different from all the agarases reported so far.