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KMID : 0545120030130020269
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Journal of Microbiology and Biotechnology
2003 Volume.13 No. 2 p.269 ~ p.275
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Purification and Characterization of the Exo-β-D-Glucosaminidase from Aspergillus flavus IAM2044
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JI, JAE-HOON
YANG, JU-SEOK/HUR, JONG-WHA
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Abstract
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Chitosan-degrading activity induced by chitosan was found in cultrate of Aspergillus flavus IAM2044. Aspergillus flavus IAM2044 had a higher level of chitosanolytic activity when chitosan was used as a carbon source, and yeast extract and peptone were supplemented as nitrogen sources. One of the Chitosan-degrading enzymes was purified to homogeneity by ammonium sulfate precipitation followed by cation-exchange and gel filtration chromatographies. The enzyme was monomeric, and its molecular mass was 45 kDa. The optimum pH and temperature of the enzyme were 5.0 and 50℃, respectively. The activity was stable in the pH range of 3.5 to 7.0 and at a temperature below 50℃. Reaction products analyzed by the viscosimetric assay and thin payer chromatography clearly indicated that the enzyme was an exo-type chitosanase exo-β-D-glucosaminidase, that released GlcN from the nonreducing ends of the oligosaccharide chains.
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