Abstract
A bacterium, Azotobacter chroococcum 4A1M, isolated from a soil sample, produced an alginate-decomposing enzyme in the culture broth. The enzyme was purified to an electrophoretically homogeneous state. The purified enzyme showed maximum activity at pH 6.0 and 60°C;it was stable up to 60°C at pH 6.0 and activated by Ca2+ and inhibited strongly by Hg2+. The molecular mass of the enzyme was estimated to be 23 kDa by sodium dodecyl sulfate/polyacrylamide gel electrophoresis and 24 kDa by gel filtration. Therefore, the enzyme was considered to be monomeric. The NH2-terminal amino acid sequence was determined to be H2N-Ala-Ser-Ile-Ala-Ile-Thr-Asn-Pro-Gly-Phe. The enzyme reacted only on the polymannuronate block of alginic acid, and two main reaction products were obtained when short-chain polymannuronate was used as a substrate. The degrees of polymerization of the two products were three and two respectively.
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Haraguchi, K., Kodama, T. Purification and propertes of poly(β-d-mannuronate) lyase from Azotobacter chroococcum . Appl Microbiol Biotechnol 44, 576–581 (1996). https://doi.org/10.1007/BF00172488
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DOI: https://doi.org/10.1007/BF00172488