Bj. Kim et al., Purification and characterization of beta-agarase from marine bacterium Bacillus cereus ASK202, BIOTECH LET, 21(11), 1999, pp. 1011-1015
Extracellular agarase of Bacillus cereus ASK202 was purified 32-fold, givin
g a single band on PAGE with activity staining. The M-r of purified agarase
was determined as 90 kDa by SDS-PAGE. The N-terminal amino acid was sequen
ced and the sequence did not show homology to any other known agarases. The
optimum pH and temperature were 7.0 and 40 degrees C, respectively. This e
nzyme was found to be a beta-agarase which catalyzed the hydrolysis of the
beta-1,4 linkage of agarose to yield neoagarohexaose, neoagarotetraose and
neoagarobiose.