Enzymatic hydrolysis of agar: purification and characterization of beta-neoagarotetraose hydrolase from Pseudomonas atlantica.
Agarose is degraded by a beta-agarase from Pseudomonas atlantica to neoagarooligosaccharides of degree of polymerization (DP), 4, 6, 8, and 10. A beta-neoagarotetraose hydrolase cleaves the central beta-linkage in neoagarotetraose and the beta-linkage near the nonreducing end in neoagarohexaose and -octaose to yield neoagarobiose. The beta-neoagarotetraose hydrolase was localized on or outside the cytoplasmic membrane, in the cell wall region. The enzyme was activated by NaCl, KCl, CaCl2, MnCl2, and MgSO4, has a Km of 3.4 X 10(-3) M for neoagarotetraose, was free from beta-agarase and alpha-neoagarobiose hydrolase activity, and showed no transglycosidic activity.
D000362:Agar; D002462:Cell Membrane / Q000201:enzymology; D003979:Diazonium Compounds / Q000494:pharmacology; D004790:Enzyme Induction; D005696:Galactosidases / Q000096:biosynthesis / Q000302:isolation & purification* / Q000378:metabolism; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D011549:Pseudomonas / Q000201:enzymology*; D012965:Sodium Chloride / Q000494:pharmacology
D003979:Diazonium Compounds; D012965:Sodium Chloride; D000362:Agar; D005696:Galactosidases