Purification and characterization of beta-agarase from marine bacterium Bacillus cereus ASK202

Citation
Bj. Kim et al., Purification and characterization of beta-agarase from marine bacterium Bacillus cereus ASK202, BIOTECH LET, 21(11), 1999, pp. 1011-1015
Citations number
16
Categorie Soggetti
Biotecnology & Applied Microbiology",Microbiology
Journal title
BIOTECHNOLOGY LETTERS
ISSN journal
01415492 → ACNP
Volume
21
Issue
11
Year of publication
1999
Pages
1011 - 1015
Database
ISI
SICI code
0141-5492(199911)21:11<1011:PACOBF>2.0.ZU;2-K
Abstract
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.